Publications before 2021

2022

Photoswitchable Isoprenoid Lipids
191

Photoswitchable Isoprenoid Lipids Enable Optical Control of Peptide Lipidation

Morstein, J.; Bader, T.; Cardillo, A. L.; Schackmannb, J.; Ashoke, S.; Hougland, J. L.; Hrycyna, C. A.; Trauner, D. H.; Distefano, M. D. Photoswitchable Isoprenoid Lipids Enable Optical Control of Peptide Lipidation. ACS Chem. Biol., 2022, in press.

 
 
 
In Vitro Cytotoxicity
190

Enzymatic Construction of DARPin-Based Targeted Delivery Systems using Protein Farnesyltransferase and a Capture and Release Strategy

Zhang, Y.; Wang, Y.; Uslu, S.; Venkatachalapathy, S.; Rashidian, M.; Schaefer, J. V.; Plückthun, A.; Distefano, M. D. Enzymatic Construction of DARPin-Based Targeted Delivery Systems using Protein Farnesyltransferase and a Capture and Release Strategy. Int. J. Mol. Sci., 2022, 23, 11537.

 
 
potent antifungals that prevent Ras signaling by inhibiting protein farnesyltransferase
189

Structure-guided discovery of potent antifungals that prevent Ras signaling by inhibiting protein farnesyltransferase

Wang, Y.; Xu, F.; Nichols, C.; Shi, Y.; Hellinga, H.; Alspaugh , J. A.; Distefano, M. D.; Beese, L. Structure-guided discovery of potent antifungals that prevent Ras signaling by inhibiting protein farnesyltransferase. J. Med. Chem., 2022, in press.

Mevalonate metabolites contribute to granulocyte chemotaxis and mortality in murine endotoxemia
188

Mevalonate metabolites contribute to granulocyte chemotaxis and mortality in murine endotoxemia

Hussain, J.; Ousley, C. G.; Krauklis, S.A.; Dray, E. L.; Drnevich, J.; Justyna, K.; Distefano, M. D.; McKim, D. B. Mevalonate metabolites contribute to granulocyte chemotaxis and mortality in murine endotoxemia. bioRxiv 2022.09.13.507840.

In vivo prenylomic profiling in the brain of a transgenic mouse model of Alzheimer’s disease reveals increased prenylation of a key set of proteins
187

In vivo prenylomic profiling in the brain of a transgenic mouse model of Alzheimer’s disease reveals increased prenylation of a key set of proteins

Jeong, A.; Auger, S. A.; Maity, S.; Fredriksen, K.; Zhong, R.;  Li, L.; and Distefano, M. D. In vivo prenylomic profiling in the brain of a transgenic mouse model of Alzheimer’s disease reveals increased prenylation of a key set of proteins. ACS Chem. Biol., 2022, in press.

Thinking outside the CaaX-box: an unusual reversible prenylation on ALDH9A1
186

Thinking outside the CaaX-box: an unusual reversible prenylation on ALDH9A1

Suazo, K. F.; Schey, G. L.; Auger, S. A.; Li, L.; Distefano, M. D. Thinking outside the CaaX-box: an unusual reversible prenylation on ALDH9A1. bioRxiv 2022.04.01.486487.

Manipulating Cell Fates with Protein Conjugates
185

Manipulating Cell Fates with Protein Conjugates

Wang, Y.; Wagner, C. R.; Distefano, M. D. Manipulating Cell Fates with Protein Conjugates. Bioconj. Chem., 2022, in press.

Combining Isoprenoid Probes with Antibody Markers for Mass Cytometric Analysis of Prenylation in Single Cells
184

Combining Isoprenoid Probes with Antibody Markers for Mass Cytometric Analysis of Prenylation in Single Cells

Maxwell, Zoe; Suazo, Kiall; Brown, Heather; Distefano, Mark; Arriaga, Edgar. Combining Isoprenoid Probes with Antibody Markers for Mass Cytometric Analysis of Prenylation in Single Cells. Anal. Chem., 2022, 94, 11521-11528.

Photoresponsive Hydrogels for Studying Mechanotransduction of Cells, in Mechanosensing
183

Photoresponsive Hydrogels for Studying Mechanotransduction of Cells, in Mechanosensing

Park, K.-Y; Odde, D. J.; Distefano, M. D. (2022) Photoresponsive Hydrogels for Studying Mechanotransduction of Cells, in Mechanosensing: Methods and Protocols (Zaidel-Bar, R., Ed.), Springer, New York, in press.

Directed cell migration toward softer environments
182

Directed cell migration toward softer environments

Isomursu, A.; Park, K.-Y.; Hou, J.; Cheng, B.; Shamsan, G.; Fuller, B.; Kasim, J.; Mahmoodi, M. M.; Lu, T. J.; Genin, G. M.; Xu, F.; Lin, M.; Distefano, M. D.; Ivaska, J.; Odde, D. J. Directed cell migration toward softer environments. Nat. Mater., 2022, 21, 1081-1090.

In vivo prenylomic profiling in the brain of a transgenic mouse model of Alzheimer’s disease reveals increased prenylation of a key set of proteins
181

In vivo prenylomic profiling in the brain of a transgenic mouse model of Alzheimer’s disease reveals increased prenylation of a key set of proteins

Angela Jeong,* Shelby A. Auger,* Sanjay Maity, Ling Li, and Mark D. Distefano. In vivo prenylomic profiling in the brain of a transgenic mouse model of Alzheimer’s disease reveals increased prenylation of a key set of proteins. bioRxiv 2022.04.01.486487

*These authors contributed to the paper equally

Macro-Chemical Biology: Engineering Biomimetic Trogocytosis with Farnesylated Chemically Self-Assembled Nanorings
180

Macro-Chemical Biology: Engineering Biomimetic Trogocytosis with Farnesylated Chemically Self-Assembled Nanorings

Yiao Wang, Lakmal Rozumalski, Caitlin Lichtenfels, Jacob R. Petersberg, Ozgun Kilic, Mark D. Distefano, Carston R. Wagner. Macro-Chemical Biology: Engineering Biomimetic Trogocytosis with Farnesylated Chemically Self-Assembled Nanorings. bioRxiv 2022.03.01.482559

2021

Stepwise Stiffness Gradients
179

Negative durotaxis: cell movement toward softer environments

Aleksi Isomursu, Keun-Young Park, Jay Hou, Bo Cheng, Ghaidan Shamsan, Benjamin Fuller, Jesse Kasim, M. Mohsen Mahmoodi, Tian Jian Lu, Guy M. Genin, Feng Xu, Min Lin, Mark Distefano, Johanna Ivaska, David J. Odde. Negative durotaxis: cell movement toward softer environments. bioRxiv 2020.10.27.357178

MALDI analysis of peptide libraries expands the scope of substrates for farnesyltransferase
178

MALDI analysis of peptide libraries expands the scope of substrates for farnesyltransferase

Schey, G.L.;  Buttery P.H.; Hildebrandt, E.R.; Novak, S.X.; Schmidt, W.K.; Hougland, J.L.; Distefano, M.D. Int. J. Mol. Sci., 2021, 22, 12042.

A Not-So-Ancient Grease History: Click Chemistry and Protein Lipid Modifications
177

A Not-So-Ancient Grease History: Click Chemistry and Protein Lipid Modifications

Suazo, K.F.; Park, K.-Y; Distefano, M.D. A Not-So-Ancient Grease History: Click Chemistry and Protein Lipid Modifications. Chem. Rev., 2021, 121, 12, 7178–7248

 

Metabolic labeling with an alkyne probe reveals similarities and differences in the prenylomes of several brain-derived cell lines and primary cells
176

Metabolic labeling with an alkyne probe reveals similarities and differences in the prenylomes of several brain-derived cell lines and primary cells

Suazo, K. F; Jeong, A.; Ahmadi, M.; Brown, C.; Qu, W.; Li, L.; Distefano, M. D. Metabolic labeling with an alkyne probe reveals similarities and differences in the prenylomes of several brain-derived cell lines and primary cells. Sci. Rep. 2021, 11, 4367.

Two-Photon Uncaging of Bioactive Thiols in Live Cells at Wavelengths above 800 nm
175

Two-Photon Uncaging of Bioactive Thiols in Live Cells at Wavelengths above 800 nm

Hammers, M.D.;  Hodny, M.H.; Bader, T. K.; Mahmoodi, M.M.; Fang, S.; Fenton,A.D.; Nurie, K.; Trial, H.O.; Xu, F.; Healy, A.T.; Ball, Z.T.; Blank, D.A.; Distefano, M.D. Two-Photon Uncaging of Bioactive Thiols in Live Cells at Wavelengths above 800 nm, Org. Biomol. Chem., 2021, 19, 2213-2223.

Neuronal Protein Farnesylation Regulates Hippocampal Synaptic Plasticity and Cognitive Function
174

Neuronal Protein Farnesylation Regulates Hippocampal Synaptic Plasticity and Cognitive Function

Qu, W.; Suazo, K.F.;  Liu, W.; Cheng, S.; Jeong, A.; Hottman, D.; Yuan, L.-L.; Distefano, M.D.; Li, L. Neuronal Protein Farnesylation Regulates Hippocampal Synaptic Plasticity and Cognitive Function, Mol. Neurobiol., 2021, 58, 1128–1144.

Engineering Reversible Cell-Cell Interactions Using Enzymatically Lipidated Chemically Self-Assembled Nanorings
173

Engineering Reversible Cell-Cell Interactions Using Enzymatically Lipidated Chemically Self-Assembled Nanorings

Wang, Y.;  Kilic, O.; Csizmar, C.M.;  Ashok, S.; Hougland, J.L.; Distefano, M.D.; Wagner, C. R. Engineering Reversible Cell-Cell Interactions Using Enzymatically Lipidated Chemically Self-Assembled Nanorings, Chem. Sci., 2021, 12, 331-340.

2020

Anti-EGFR Fibronectin Bispecific Chemically Self-Assembling Nanorings
172

Anti-EGFR Fibronectin Bispecific Chemically Self-Assembling Nanorings (CSANs) Induce Potent T-cell Mediated Anti-Tumor Response and Downregulation of EGFR Signaling and PD-1/PD-L1 Expression

Kilic, O.; Matos de Souza, M.; Almotlak, A.; Wang, Y.; Siegfried, J.; Distefano, M.D.; Wagner, C.R. Anti-EGFR Fibronectin Bispecific Chemically Self-Assembling Nanorings (CSANs) Induce Potent T-cell Mediated Anti-Tumor Response and Downregulation of EGFR Signaling and PD-1/PD-L1 Expression J. Med. Chem., 2020, 63, 10235−10245.

red-shifted_backbone_n-h_photocaging_agents
171

Red-shifted backbone N–H photocaging agents

Mangubat-Medina, A. E.; Trial, H. O.; Vargas, R. D.; Setegne, M. T.; Bader, T.; Distefano, M. D.; Ball, Z. T. Red-shifted backbone N–H photocaging agents. Org. Biomol. Chem., 2020,18, 5110-5114.

 

Splice switching an oncogenic ratio of SmgGDS isoforms as a strategy to diminish malignancy
170

Splice switching an oncogenic ratio of SmgGDS isoforms as a strategy to diminish malignancy

Brandt, A. C.; McNally, L.; Lorimer, E. L.; Unger, B.; Koehn, O. J.; Suazo, K. F.; Rein,  L.; Szabo, A.; Tsaih, S.-W.; Distefano, M. D.; . Flister, M. J.; Rigo, F.; McNally, M. T.; Williams, C L. Splice switching an oncogenic ratio of SmgGDS isoforms as a strategy to diminish malignancy Proc. Nat. Acad. Sci. U.S.A. 2020, 117, 3627-3636.

A methoxy-substituted nitrodibenzofuran-based protecting group with an improved two-photon action cross-section for thiol protection in solid phase peptide synthesis
169

A methoxy-substituted nitrodibenzofuran-based protecting group with an improved two-photon action cross-section for thiol protection in solid phase peptide synthesis

Bader, T. K.; Xu, F.; Hodny, M. H.; Blank, D. A.; Distefano, M. D. A methoxy-substituted nitrodibenzofuran-based protecting group with an improved two-photon action cross-section for thiol protection in solid phase peptide synthesis J. Org. Chem. 2020, 85, 1614–1625.

2019

Site-Selective Enzymatic Labeling of Designed Ankyrin Repeat Proteins Using Protein Farnesyltransferase
168

Site-Selective Enzymatic Labeling of Designed Ankyrin Repeat Proteins Using Protein Farnesyltransferase

 Zhang, Y.; Auger, S.; Schaefer, J. V.; Plückthun, A.; Distefano, M. D. (2019) Site-Selective Enzymatic Labeling of Designed Ankyrin Repeat Proteins Using Protein Farnesyltransferase in Methods in Molecular Biology: Bioconjugation (Massa, S., Ed.), Springer, New York, p 207-219.

A quantitative FRET assay for the upstream cleavage activity of the integral membrane proteases human ZMPSTE24 and yeast Ste24
167

A quantitative FRET assay for the upstream cleavage activity of the integral membrane proteases human ZMPSTE24 and yeast Ste24

Hsu, E-. T.; Vervacke, J. S.; Distefano, M. D.; Hrycyna, C. A. (2019) A quantitative FRET assay for the upstream cleavage activity of the integral membrane proteases human ZMPSTE24 and yeast Ste24 in Protein Lipidation: Methods and Protocols (Linder, M., Ed.), Springer, New York, p 279-293,

Optimization of Metabolic Labeling with Alkyne-Containing Isoprenoid Probes
166

Optimization of Metabolic Labeling with Alkyne-Containing Isoprenoid Probes

Ahmadi, M.; Suazo, K. F.; Distefano, M. D. (2019) Optimization of Metabolic Labeling with Alkyne-Containing Isoprenoid Probes, in Protein Lipidation: Methods and Protocols (Linder, M., Ed.), Springer, New York, p 35-44.

Proteomic analysis of protein-lipid modifications: significance and application, in Mass Spectrometry-based Chemical Proteomics
165

Proteomic analysis of protein-lipid modifications: significance and application, in Mass Spectrometry-based Chemical Proteomics

Suazo, K. F.; Schey, G.; Schaber, C.; John, A. R. O.; Distefano, M. D. (2019) Proteomic analysis of protein-lipid modifications: significance and application, in Mass Spectrometry-based Chemical Proteomics (Tao, W. A., Ed.), Wiley, New York, p 317-348.

Cysteine-ethylation of tissue-extracted membrane proteins as a tool to detect conformational states by solid-state NMR spectroscopy
164

Cysteine-ethylation of tissue-extracted membrane proteins as a tool to detect conformational states by solid-state NMR spectroscopy

164.     Weber, D. K.; Bader, T.; Larsen, E. K.; Wang, S.; Gopinath, T.; Distefano, M. D.; Veglia, G. Cysteine-ethylation of tissue-extracted membrane proteins as a tool to detect conformational states by solid-state NMR spectroscopy. Meth. Enzymol. 2019, 621, 281-304,

doi.org/10.1016/bs.mie.2019.02.001.

Synthesis and NMR Characterization of the Prenylated Peptide, a-Factor
163

Synthesis and NMR Characterization of the Prenylated Peptide, a-Factor

Bader, T. K.; Rappe, T. M.; Veglia, G.; Distefano, M. D. Synthesis and NMR Characterization of the Prenylated Peptide, a-Factor. Meth. Enzymol. 2019, 614, 207-238.

2018

Recent progress in enzymatic protein labelling techniques and their applications
162

Recent progress in enzymatic protein labelling techniques and their applications

Zhang, Y.; Park,  K-. Y.; Suazo,  K. F.; and Distefano, M. D. Recent progress in enzymatic protein labelling techniques and their applications. Chem. Rev., 2018, 47, 9106-9136.

Optimization of Metabolic Labeling with Alkyne-Containing Isoprenoid Probes
161

Metabolic Labeling of Prenylated Proteins Using Alkyne-Modified Isoprenoid Analogues

Suazo, K. F.; Hurben, A. K.; Liu, K.; Xu, F.; Thao, P., Sudheer, C.; Li, L.; Distefano, M. D. Metabolic Labeling of Prenylated Proteins Using Alkyne-Modified Isoprenoid Analogues. Curr. Protoc. Chem. Biol. 2018, 10, e46. 

Isoprenoids and protein prenylation: implications in the pathogenesis and therapeutic intervention of Alzheimer’s disease
160

Isoprenoids and protein prenylation: implications in the pathogenesis and therapeutic intervention of Alzheimer’s disease

Jeong, A.; Suazo, K. F.; Wood, W. G.; Distefano, M. D. and Li, L.
 Isoprenoids and protein prenylation: implications in the pathogenesis and therapeutic intervention of Alzheimer’s disease. Crit. Rev. Biochem. Mol. Biol. 2018, 53, 279–310

Site-specific cross-linking of proteins to DNA via a new bioorthogonal approach employing oxime ligation
159

Site-specific cross-linking of proteins to DNA via a new bioorthogonal approach employing oxime ligation

Pujari, S. S.; Zhang, Y.; Ji, S.; Distefano, M. D. and Tretyakova, N. T. Site-specific cross-linking of proteins to DNA via a new bioorthogonal approach employing oxime ligation. Chem. Commun., 2018, 54, 6296-6299.

Photo-Immobilized EGF Chemical Gradients Differentially Impact Breast Cancer Cell Invasion and Drug Response in Defined 3D Hydrogels
158

Photo-Immobilized EGF Chemical Gradients Differentially Impact Breast Cancer Cell Invasion and Drug Response in Defined 3D Hydrogels

Fisher, S. A; Tam, R. T.; Fokina, A.; Mahmoodi, M. M.; Distefano, M. D.; Shoichet, M. S. Photo-Immobilized EGF Chemical Gradients Differentially Impact Breast Cancer Cell Invasion and Drug Response in Defined 3D Hydrogels. Biomaterials, 2018, 178, 751-766.

a-Factor Analogues Containing Alkyne- and Azide-Functionalized Isoprenoids Are Efficiently Enzymatically Processed and Retain Wild-Type Bioactivity
157

a-Factor Analogues Containing Alkyne- and Azide-Functionalized Isoprenoids Are Efficiently Enzymatically Processed and Retain Wild-Type Bioactivity

Diaz-Rodriguez, V., Hsu, E. T., Ganusova, E., Werst, E. R., Becker, J. M., Hrycyna, C. A., and Distefano, M. D., a-Factor Analogues Containing Alkyne- and Azide-Functionalized Isoprenoids Are Efficiently Enzymatically Processed and Retain Wild-Type Bioactivity. Bioconjug. Chem. 2018, 29, 316–323.

Efficient farnesylation of an extended C-terminal C(x)3X sequence motif expands the scope of the prenylated proteome
156

Efficient farnesylation of an extended C-terminal C(x)3X sequence motif expands the scope of the prenylated proteome

Blanden, M. J.; Suazo, K. F.; Hildebrandt, E. R.; Hardgrove, D. S.; Patel, M.; Saunders, W. P.; Distefano, M. D.; Schmidt, W. K.; Hougland, J. L., Efficient farnesylation of an extended C-terminal C(x)3X sequence motif expands the scope of the prenylated proteome. J. Biol. Chem. 2018, 293, 2770-2785.

2017

a-Factor: a chemical biology tool for the study of protein prenylation
155

a-Factor: a chemical biology tool for the study of protein prenylation

Diaz-Rodriguez, V.; Distefano, M. D., a-Factor: a chemical biology tool for the study of protein prenylation. Curr. Topics Pep. Prot. Res. 2017, 18, 133-151.

Polymeric Medical Sutures: An Exploration of Polymers and Green Chemistry
154

Polymeric Medical Sutures: An Exploration of Polymers and Green Chemistry

Knutson, C. M.; Schneiderman, D. K.; Yu, M.; Javner, C.; Distefano, M. D. Wissinger
, J. E. Polymeric Medical Sutures: An Exploration of Polymers and Green Chemistry. J. Chem. Ed. 2017, 94, 1761-1765.

2016

Global proteomic analysis of prenylated proteins in Plasmodium falciparum using an alkyne-modified isoprenoid analogue
153

Global proteomic analysis of prenylated proteins in Plasmodium falciparum using an alkyne-modified isoprenoid analogue

Suazo, K. F.; Schaber, C.; Palsuledesai, C. C.; Odom John, A. R.; Distefano, M. D., Sci. Rep. 20166, 38615.

 

 

Bypass of DNA-Protein Cross-links Conjugated to the 7-Deazaguanine Position of DNA by Translesion Synthesis Polymerases
152

Bypass of DNA-Protein Cross-links Conjugated to the 7-Deazaguanine Position of DNA by Translesion Synthesis Polymerases

Wickramaratne, S.; Ji, S.; Mukherjee, S.; Su, Y.; Pence, M. G.; Lior-Hoffmann, L.; Fu, I.; Broyde, S.; Guengerich, F. P.; Distefano, M.; Schärer, O. D.; Sham, Y. Y.; Tretyakova, N., J. Biol. Chem. 2016291, 23589-23603.

 

Metabolic Labeling with an Alkyne-modified Isoprenoid Analog Facilitates Imaging and Quantification of the Prenylome in Cells
151

Metabolic Labeling with an Alkyne-modified Isoprenoid Analog Facilitates Imaging and Quantification of the Prenylome in Cells

Palsuledesai, C. C.; Ochocki, J. D.; Kuhns, M. M.; Wang, Y.-C.; Warmka, J. K.; Chernick, D. S.; Wattenberg, E. V.; Li, L.; Arriaga, E. A.; Distefano, M. D.  ACS Chem. Biol201611, 2820-2828.

6-Bromo-7-hydroxy-3-methylcoumarin (mBhc) is an efficient multi-photon labile protecting group for thiol caging and three-dimensional chemical patterning
150

6-Bromo-7-hydroxy-3-methylcoumarin (mBhc) is an efficient multi-photon labile protecting group for thiol caging and three-dimensional chemical patterning

Mahmoodi, M. M.; Fisher, S. A.; Tam, R. Y.; Goff, P. C.; Anderson, R. B.; Wissinger, J. E.; Blank, D. A.; Shoichet, M. S.; Distefano, M. D.  Org. Biomol. Chem201614, 8289 - 8300.

Nitrodibenzofuran: A One- and Two-Photon Sensitive Protecting Group That Is Superior to Brominated Hydroxycoumarin for Thiol Caging in Peptides
149

Nitrodibenzofuran: A One- and Two-Photon Sensitive Protecting Group That Is Superior to Brominated Hydroxycoumarin for Thiol Caging in Peptides

Mahmoodi, M. M.; Abate-Pella, D.; Pundsack, T. J.; Palsuledesai, C. C.; Goff, P. C.; Blank, D. A.; Distefano, M. D.  J. Am. Chem. Soc.  2016138, 5848-5859.

Analogs of farnesyl diphosphate alter CaaX substrate specificity and reactions rates of protein farnesyltransferase
148

Analogs of farnesyl diphosphate alter CaaX substrate specificity and reactions rates of protein farnesyltransferase

Jennings, B. C.; Danowitz, A. M.; Wang, Y.-C.; Gibbs, R. A.; Distefano, M. D.; Fierke, C. A.,  Bioorg. Med. Chem201626, 1333–1336.

8-Hydroxyquinoline-based inhibitors of the Rce1 protease disrupt Ras membrane localization in human cells
147

8-Hydroxyquinoline-based inhibitors of the Rce1 protease disrupt Ras membrane localization in human cells

Mohammed, I.; Hampton, S. E.; Ashall, L.; Hildebrandt, E. R.; Kutlik, R. A.; Manandhar, S. P.; Floyd, B. J.; Smith, H. E.; Dozier, J. K.; Distefano, M. D.; Schmidt, W. K.; Dore, T. M.,  Bioorg. Med. Chem201624, 160-178.

Synthetic isoprenoid analogues for the study of prenylated proteins: Fluorescent imaging and proteomic applications
146

Synthetic isoprenoid analogues for the study of prenylated proteins: Fluorescent imaging and proteomic applications

Wang, Y.-C.; Distefano, M. D.,  Bioorg. Chem. 201664, 59-65.

2015

Simultaneous Site-Specific Dual Protein Labeling Using Protein Prenyltransferases
145

Simultaneous Site-Specific Dual Protein Labeling Using Protein Prenyltransferases

Zhang, Y.; Blanden, M. J.; Sudheer, C.; Gangopadhyay, S. A.; Rashidian, M.; Hougland, J. L.; Distefano, M. D.,  Bioconj. Chem. 201526, 2542-2553.

Synthesis of Peptides Containing C-Terminal Esters Using Trityl Side-Chain Anchoring:
144

Synthesis of Peptides Containing C-Terminal Esters Using Trityl Side-Chain Anchoring: Applications to the Synthesis of C-Terminal Ester Analogs of the Saccharomyces cerevisiae Mating Pheromone a-Factor

Diaz-Rodriguez, V.; Ganusova, E.; Rappe, T. M.; Becker, J. M.; Distefano, M. D.  J. Org. Chem201580, 11266–11274.

 

 

 

The Frequency of Naive and Early-Activated Hapten-Specific B Cell Subsets Dictates the Efficacy of a Therapeutic Vaccine against Prescription Opioid Abuse
143

The Frequency of Naive and Early-Activated Hapten-Specific B Cell Subsets Dictates the Efficacy of a Therapeutic Vaccine against Prescription Opioid Abuse

Laudenbach, M.; Baruffaldi, F.; Vervacke, J. S.; Distefano, M. D.; Titcombe, P. J.; Mueller, D. L.; Tubo, N. J.; Griffith, T. S.; Pravetoni, M.  J. Immunol. 2015, 194, 5926-5936.

Site-specific pegylation of therapeutic proteins
142

Site-specific pegylation of therapeutic proteins

Dozier, J.K.; Distefano, M.D.  Int. J. Mol. Sci. 201516, 25831-35864.

Application of meta- and para-Phenylenediamine as Enhanced Oxime Ligation Catalysts for Protein Labeling, PEGylation, Immobilization, and Release
141

Application of meta- and para-Phenylenediamine as Enhanced Oxime Ligation Catalysts for Protein Labeling, PEGylation, Immobilization, and Release

Mahmoodi, M. M.; Rashidian, M.; Zhang, Y.; Distefano, M. D.,  Curr. Protoc. Protein Sci2015, 15.4.1-15.4.28.

Protein prenylation: enzymes, therapeutics and biotechnology applications
140

Protein prenylation: enzymes, therapeutics and biotechnology applications

Palsuledesai, C. C.; Distefano, M. D.,  ACS Chem. Biol. 2015, 10, 51-62.

Error-prone Translesion Synthesis Past DNA-Peptide Cross-links Conjugated to the Major Groove of DNA
139

Error-prone Translesion Synthesis Past DNA-Peptide Cross-links Conjugated to the Major Groove of DNA

Wickramaratne, S.; Boldry, E.; Buehler, C.; Wang, Y.-C.; Distefano, M. D.; Tretyakova, N. Y.,  J. Biol. Chem. 2015920, 775-787.

2014

138. Wang, Y.-C.; Distefano, M. D., Synthesis and screening of peptide libraries with free C-termini . Curr. Topics. Pep. Prot. Sci. 201415, 1-23. researchtrends.net/tia/.

137. Dozier, J. K.; Khatwani, S. L.; Wollack, J. W.; Wang, Y.-C.; Schmidt-Dannert, C.; Distefano, M. D. Engineering Protein Farnesyltransferase for Enzymatic Protein Labeling Applications. Bioconj. Chem. 201425, 1203-1212. DOI: 10.1021/bc500240p

136. Wang, Y.-C.; Dozier, J. K.; Beese, L. S.; Distefano, M. D. Rapid Analysis of Protein Farnesyltransferase Substrate Specificity Using Peptide Libraries and Isoprenoid Diphosphate Analogues. ACS Chem. Biol. 20149, 1726-1735. DOI: 10.1021/cb5002312

135. Yeo, J. E.; Wickramaratne, S.; Khatwani, S.; Wang, Y.-C.; Vervacke, J.; Distefano, M. D.; Tretyakova, N. Y. Synthesis of Site-Specific DNA‚ÄìProtein Conjugates and Their Effects on DNA Replication. ACS Chem. Biol. 20149, 1860-1868. DOI: 10.1021/cb5001795

134. Pravetoni, M.; Vervacke, J. S.; Distefano, M. D.; Tucker, A. M.; Laudenbach, M.; Pentel, P. R. Effect of Currently Approved Carriers and Adjuvants on the Pre-Clinical Efficacy of a Conjugate Vaccine against Oxycodone in Mice and Rats. PLoS ONE 2014, 9, e96547. DOI: 10.1371/journal.pone.0096547

133. Wollack, J. W.; Monson, B. J.; Dozier, J. K.; Dalluge, J. J.; Poss, K.; Hilderbrand, S. A.; Distefano, M. D. Site-Specific Labeling of Proteins and Peptides with Trans-cyclooctene Containing Handles Capable of Tetrazine Ligation. Chem. Biol. Drug Des201484, 140-147. DOI: 10.1111/cbdd.12303

132. Palsuledesai, C. C.; Ochocki, J. D.; Markowski, T. W.; Distefano, M. D. A combination of metabolic labeling and 2D-DIGE analysis in response to a farnesyltransferase inhibitor facilitates the discovery of new prenylated proteins. Mol. Biosys. 201410, 1094-1103. DOI: 10.1039/C3MB70593E

131. Schuld, N. J.; Vervacke, J. S.; Lorimer, E. L.; Simon, N. C.; Hauser, A. D.; Barbieri, J. T.; Distefano, M. D.; Williams1, C. L. The chaperone protein SmgGDS interacts with small GTPases entering the prenylation pathway by recognizing the last amino acid in the CAAX motif. J. Biol. Chem2014289, 6862-6876. DOI: 10.1074/jbc.M113.527192

130. Vervacke, J. S.; Funk, A. L.; Wang, Y.-C.; Strom, M.; Hrycyna, C. A.; Distefano, M. D. A Diazirine-Containing Photoactivatable Isoprenoid: Synthesis and Application in Studies with Isoprenylcysteine Carboxyl Methyltransferase. J. Org. Chem201479, 1971-1978. DOI: 10.1021/jo402600b

2013

129. Tolstyka, Z. P.; Richardson, W.; Bat, E.; Stevens, C. J.; Parra, D. P.; Dozier, J. K.; Distefano, M. D.; Dunn, B.; Maynard, H. D. Chemoselective Immobilization of Proteins by Microcontact Printing and Bio-orthogonal Click Reactions. ChemBioChem 201314, 2464-2471.

128. Rashidian, M.; Kumarapperuma, S. C.; Gabrielse, K.; Fegan, A.; Wagner, C. R.; Distefano, M. D. Simultaneous Dual Protein Labeling Using a Triorthogonal Reagent. J. Am. Chem. Soc2013135, 16388–16396.

127. Rashidian, M.; Dozier, J. K.; Distefano, M. D. Chemoenzymatic Labeling of Proteins: Techniques and Approaches. Bioconj. Chem201324, 1277-1294.

126. Ochocki, J. D.; Igbavboa, U.; Wood, W. G.; Arriaga, E. A.; Wattenberg, E. V.; Distefano, M. D. Evaluation of prenylated peptides for use in cellular imaging and biochemical analysis. Meth. Mol. Biol. 20131088, 213-223.

125. Ochocki, J. D.; Distefano, M. D. Prenyltransferase inhibitors: treating human ailments from cancer to parasitic infections. Med. Chem. Commun. 2013, 4, 476-492.

124. Mahmoodi, M. M.; Rashidian, M.; Dozier, J. K.; Distefano, M. D. Chemoenzymatic Site-Specific Reversible Immobilization and Labeling of Proteins from Crude Cellular Extract Without Prior Purification Using Oxime and Hydrazine Ligation. Curr. Protoc. Chem. Biol. 20135, 89-109.

123. Wang, H.; Henry, O.; Distefano, M. D.; Wang, Y.-C.; Räikkönen, J.; Mönkkönen, J.; Tanaka, Y.; Morita, C. T. Butyrophilin 3A1 Plays an Essential Role in Prenyl Pyrophosphate Stimulation of Human Vγ2Vδ2 T Cells. J. Immunol. 2013191, 1029-1042.

122. Vervacke, J. S.; Wang, Y.-C.; Distefano, M. D. Photoactive analogues of farnesyl diphosphate and related isoprenoids: design and applications in studies of medicinally important isoprenoid-utilizing enzymes. Curr. Med. Chem. 201320, 1585-1594.

121. Satori, C. P.; Henderson, M. M.; Krautkramer, E. A.; Kostal, V.; Distefano, M. D.; Arriaga, E. A. Bioanalysis of Eukaryotic Organelles. Chem. Rev. 2013113, 2733-2811.

120 Rashidian, M.; Mahmoodi, M. M.; Shah, R.; Dozier, J. K.; Wagner, C. R.; Distefano, M. D. A Highly Efficient Catalyst for Oxime Ligation and Hydrazone-Oxime Exchange Suitable for Bioconjugation. Bioconj. Chem. 201324, 333-342.

119. Wang, Y.-C.; Distefano, M. D. "Solid-Phase Synthesis of C-Terminal Peptide Libraries for Studying the Specificity of Enzymatic Protein Farnesyltransferase" In Peptides across the Pacific: Proceedings of the 23rd American Peptide Symposium; Lebl, M., Ed.; Prompt Scientific Publishing: San Diego, 2013, p 102-103.

118. Mahmoodi, M.; Kubo, T.; Abate-Pella, D.; Wissinger, J. E.; Distefano, M. D. "Solvent-Free Synthesis of Bhc-Cl and Application to Cysteine Protection in Solid Phase Peptide Synthesis" In Peptides across the Pacific: Proceedings of the 23rd American Peptide Symposium; Lebl, M., Ed.; Prompt Scientific Publishing: San Diego, 2013, p 248-249.

117. Diaz-Rodriguez, V.; Ganusova, E.; Becker, J. M.; Distefano, M. D. "Synthesis and Bioactivity Analysis of a-Factor Analogs Containing Different Alkyl Esters at the C-Terminal Cysteine Using Trityl Side-Chain Anchoring" In Peptides across the Pacific: Proceedings of the 23rd American Peptide Symposium; Lebl, M., Ed.; Prompt Scientific Publishing: San Diego, 2013, p 206-207.

116. Vervacke, J.; Funk, A.; Schuld, N.; Williams, C.; Hrycnya, C.; Distefano, M. D. "Photoactive Prenylated Peptides for Studying Protein Isoprenylation" In Peptides across the Pacific: Proceedings of the 23rd American Peptide Symposium; Lebl, M., Ed.; Prompt Scientific Publishing: San Diego, 2013, p 208-209.

2012

115. Abate-Pella, D.; Distefano, M. D. In Cysteine: Biosynthesis, Chemical Structure and Toxicity; Chorkina, F. V., Karataev, A. I., Eds.; Nova Science Publishe: Hauppauge, NY, 2012.

114. Diaz-Rodriguez, V.; Mullen, D. G.; Ganusova, E.; Becker, J. M.; Distefano, M. D. Synthesis of Peptides Containing C-Terminal Methyl Esters Using Trityl Side-Chain Anchoring: Application to the Synthesis of a-Factor and a-Factor Analogs. Org. Lett. 201214, 5648-5651.

113. Wang, Y.-C.; Distefano, M. D., Solid-Phase Synthesis of C-Terminal Peptide Libraries for Studying the Specificity of Enzymatic Protein Prenylation. Chem. Comm.2012, 1359-7345.

112. Hahne, K.; Vervacke, J. S.; Shrestha, L.; Donelson, J. L.; Gibbs;, R. A.; Distefano, M. D.; Hrycyna, C. A., Evaluation of Substrate and Inhibitor Binding to Yeast and Human Isoprenylcysteine Carboxyl Methyltransferases (Icmts) using Biotinylated Benzophenone-containing Photoaffinity Probes. Biochem. Biophys. Res. Comm. 2012423, 98-103.

111. Khatwani, S. L.; Kang, J. S.; Mullen, D. G.; Hast, M. A.; Beese, L. S.; Distefano, M. D.; Taton, T. A., Covalent protein-oligonucleotide conjugates by copper-free click reaction. Bioorg. Med. Chem2012, 4532-4539.

110. Rashidian, M.; Song, J. M.; Pricer, R. E.; Distefano, M. D., Chemoenzymatic Reversible Immobilization and Labeling of Proteins without Prior Purification. J. Am. Chem. Soc. 2012, 134, 8455–8467.

109. Dozier, J. K.; Distefano, M. D., An enzyme-coupled continuous fluorescence assay for farnesyl diphosphate synthases. Anal. Biochem. 2012, 421, 158-163.

108. Abate-Pella, D.; Zeliadt, N. A.; Ochocki, J. D.; Warmka, J. K.; Dore, T. M.; David A. Blank; Wattenberg, E. V.; Distefano, M. D., Photochemical Modulation of Ras-Mediated Signal Transduction using Caged Farnesyltransferase Inhibitors: Activation via One- and Two-Photon Excitation. ChemBioChem 2012, 13, 1009-1016.

2011

107. Kyro, K.; Manandhar, S. P.; Mullen, D.; Schmidt, W. K.; Distefano, M. D., Photoaffinity Labeling of Ras Converting Enzyme using Peptide Substrates that Incorporate Benzoylphenylalanine (Bpa) Residues: Improved Labeling and Structural Implications. Bioorg. Med. Chem2011, 19, 7559-7569, DOI: 10.1016/j.bmc.2011.10.027. 

106. Ochocki, J. D.; Mullen, D. G.; Wattenberg, E. V.; Distefano, M. D., Evaluation of a cell penetrating prenylated peptide lacking an intrinsic fluorophore via in situ click reaction. Bioorg. Med. Chem Lett. 2011, 21, 4998-5001, DOI: 10.1016/j.bmcl.2011.04.138. 

105. Gaffarogullari, E. C.; Masterson, L. R.; Metcalfe, E. E.; Traaseth, N. J.; Balatri, E.; Musa, M. M.; Mullen, D.; Distefano, M. D.; Veglia, G., A Myristoyl/Phosphoserine Switch Controls cAMP-Dependent Protein Kinase Association to Membranes. J. Mol. Biol. 2011, 411, 823-836, DOI: 10.1016/j.jmb.2011.06.034. 

104. Mullen, D.; Kyro, K.; Hauser, M.; Becker, J. M.; Naider, F.; Distefano, M. D., Synthesis of a-factor peptide from Saccharomyces cerevisiae and photoactive analogues via Fmoc solid phase methodology.Bioorg. Med. Chem. 2011, 19, 490-497, DOI:10.1016/j.bmc.2010.11.006. 

103. Lenevich, S.; Distefano, M. D., NMR-based quantification of organic diphosphates. Anal. Biochem. 2011, 408, 316-320, DOI: 10.1016/j.ab.2010.08.030. 

102. Wang, Y.-C.; Distefano, M. Preparation and Analysis of One-Bead One-Compound Libraries for Studying Protein Prenylation Specificity. In Building Bridges: Proceedings of the 22nd American Peptide Symposium; Lebl, M., Ed.; Prompt Scientific Publishing: San Diego, 2011, p 276-277. 

101. Rashidian, M.; Distefano, M. D. Site-Specific Protein Labeling Via Oxime and Hydrazone Ligations Using Protein Farnesyltransferases. In Building Bridges: Proceedings of the 22nd American Peptide Symposium; Lebl, M., Ed.; Prompt Scientific Publishing: San Diego, 2011, p 88-89. 

100. Kyro, K.; Schmidt, W. K.; Distefano, M. D. Design and Application of Bpa-Containing Peptides for Studying Ras-Converting Enzyme. In Building Bridges: Proceedings of the 22nd American Peptide Symposium; Lebl, M., Ed.; Prompt Scientific Publishing: San Diego, 2011, p 268-269. 

99. Díaz-Rodríguez, V.; Mullen, D.; Distefano, M. D. Synthesis of a-Factor and a-Factor Analogs Using a Cysteine-Anchoring Method. In Building Bridges: Proceedings of the 22nd American Peptide Symposium; Lebl, M., Ed.; Prompt Scientific Publishing: San Diego, 2011, p 92-93. 

98. Abate-Pella, D.; Distefano, M. D. Photocaged Cysteine Peptides for Studying Protein Farnesylation. In Building Bridges: Proceedings of the 22nd American Peptide Symposium; Lebl, M., Ed.; Prompt Scientific Publishing: San Diego, 2011, p 90-91. 

2010

97. Rashidian, M.; Dozier, J. K.; Lenevich, S.; Distefano, M. D., Selective Labeling of Polypeptides Using Protein Farnesyltransferase via Rapid Oxime Ligation. Chemical Communications 2010, 46, 8998-9000, DOI: 10.1039/C0CC03305G. 

96. DeGraw, A. J.; Palsuledesai, C.; Ochocki, J. D.; Dozier, J. K.; Lenevich, S.; Rashidian, M.; Distefano, M. D., Evaluation of alkyne-modified isoprenoids as chemical reporters of protein prenylation. Chem. Bio. Drug. Des2010, 76, 460-471, DOI: 10.1111/j.1747-0285.2010.01037.x. 

95. Kyro, K.; Manandhar, S.; Mullen, D.; Schmidt, W. K.; Distefano, M. D., Photoaffinity Labeling of Ras Converting Enzyme 1 (RCE1) using a Benzophenone-Containing Peptide Substrate. Bioorganic and Medicinal Chemistry 2010, 18, 5675-5684, DOI:10.1016/j.bmc.2010.06.024. 

94. Ochocki, J. D.; Wattenberg, E. V.; Distefano, M. D., Enlarging the scope of cell penetrating prenylated peptides to include farnesylated “CAAX” box sequences and diverse cell types. Chem. Biol. Drug Des2010, 76, 107-115, DOI: 10.1111/j.1747-0285.2010.00992.x. 

93. Lopez-Gallego, F.; Agger, S. A.; Abate-Pella, D.; Distefano, M. D.; Schmidt-Dannert, C., Sesquiterpene synthases Cop4 and Cop6 from Coprinus cinereus: catalytic promiscuity and cyclization of farnesyl pyrophosphate geometric isomers. ChemBiochem2010, 11, 1093-1106, DOI: 10.1002/cbic.200900671. 

92. Mullen, D.; Weigel, B.; Barany, G.; Distefano, M. D., On-resin conversion of Cys(Acm)-containing peptides to their corresponding Cys(Scm) congeners: scope and limitations. Journal of Peptide Science 2010, 16, 219-222. DOI: 10.1002/psc.1223 

91. DeGraw, A. J.; Keiser, M. J.; Ochocki, J. D.; Shoichet, B. K.; Distefano, M. D., Prediction and evaluation of protein farnesyltransferase inhibition by commercial drugs Journal of Medicinal Chemistry 2010, 53, 2464–2471. DOI: 10.1021/jm901613f 

90. Wollack, J. W.; Zeliadt, N. A.; Mullen, D. G.; Wattenberg, E. V.; Barany, G.; Distefano, M. D., Investigation of a Minimal Sequence for Cell-Penetrating Prenylated Peptides. Bioorganic and Medicinal Chemistry Letters 2010, 20, 161-163. DOI:10.1016/j.bmcl.2009.11.026 

89. Hovlid, M. L.; Edelstein, R. L.; Henry, O.; Ochocki, J.; Talbot, T.; Lopez-Gallego, F.; Schmidt-Dannert, C.; Distefano, M. D., Synthesis and Applications of DATFP-Containing Photoactive Analogues of Farnesyl Diphosphate Containing Modified Linkages for Enhanced Stability. Chemical Biology and Drug Design 2010, 75, 51-67. DOI: 10.1111/j.1747-0285.2009.00914.x 

2009

88. Wollack, J.; Silvermann, J.; Petzold, C.; Mougous, J.; Distefano, M. D., A Minimalist Substrate for Enzymatic Peptide and Protein Conjugation. ChemBiochem 2009, 10, 2934-2943. DOI: 10.1002/cbic.200900566 

87. Abate-Pella, D.; Zeliadt, N.; Mullen, D.; McDonald, P.; Pathak, P.; Dore, T.; Mueller, J.; Wattenberg, E.; Distefano, M. D., A Photolabile Thiol Protecting Group for Cellular Studies. In Breaking Away: Proceedings of the 21st American Peptide Symposium, Lebl, M., Ed. Prompt Scientific Publishing: San Diego, 2009; pp 362-363. 

86. Wollack, J. W.; Katzenmeyer, J.; Ochocki, J. D.; Zeliadt, N. A.; Mullen, D. G.; Arriaga, E. A.; Wattenberg, E. V.; Distefano, M. D., Utilization of Hydrophobic Modification to Promote Internalization of a CAAX Box-containing Peptide. In Breaking Away: Proceedings of the 21st American Peptide Symposium, Lebl, M., Ed. Prompt Scientific Publishing: San Diego, 2009; pp 318-320. 

85. Kyro, K.; Mullen, D.; Manandhar, S.; Walter K. Schmidt; Distefano, M. D., Photoactive Isoprenoid-containing Peptides. In Breaking Away: Proceedings of the 21st American Peptide Symposium, Lebl, M., Ed. Prompt Scientific Publishing: San Diego, 2009; pp 304-305. 

84. Wollack, J. W.; Zeliadt, N. A.; Mullen, D. G.; Amundson, G.; Geier, S.; Falkum, S.; Wattenberg, E. V.; Barany, G.; Distefano, M. D., Multifunctional prenylated peptides for in vivo analysis. Journal of the American Chemical Society 2009, 131, 7293–7303. DOI: 10.1021/ja805174z 

83. Henry, O.; Lopez-Gallego, F.; Agger, S. A.; Schmidt-Dannert, C.; Sen, S.; Shintani, D.; Cornish, K.; Distefano, M. D., A Versatile Photoactivatable Probe Designed to Label the Diphosphate Binding Site of Farnesyl Diphosphate Utilizing Enzymes. Bioorganic & Medicinal Chemistry 2009, 17, 4797-4805. DOI:10.1016/j.bmc.2009.04.034 

82. Chung, J. A.; Wollack, J. W.; Okesli, A.; Hovlid, M. L.; Chen, Y.; Mueller, J. D.; Distefano, M. D.; Taton, T. A., Purification of prenylated proteins by affinity chromatography on cyclodextrin-modified agarose. Analytical Biochemistry 2009, 386, 1-8. DOI:10.1016/j.ab.2008.09.007 

2008

81. Sarikonda, G.; Wang, H.; Puan, K.-J.; Liu, X.-h.; Lee, H. K.; Song, Y.; Distefano, M. D.; Oldfield, E.; Prestwich, G. D.; Morita, C. T., Photoaffinity Antigens for Human gamma-delta T Cells. Journal of Immunology2008, 181, (11), 7738-7750. 

80. DeGraw, A. J.; Hast, M. A.; Xu, J.; Mullen, D.; Beese, L. S.; Barany, G.; Distefano, M. D., Caged Protein Prenyltransferase Substrates: Tools for Understanding Protein Prenylation. Chemical Biology and Drug Design2008, 72, 171-181. DOI: 10.1111/j.1747-0285.2008.00698.x 

79. Xie, W.; McMahan, C. M.; Distefano, M. D.; DeGraw;, A. J.; Cornish, K.; Whalen, M. C.; Shintani, D. K., Initiation of rubber biosynthesis: in vitro comparisons of benzophenone-modified diphosphate analogues in three rubber-producing species. Phytochemistry2008, 69, 2539-2545. DOI:10.1016/j.phytochem.2008.07.011

2007 

78. Lenevich, S.; Hosokawa, A.; Cramer, C. J.; Distefano, M. D., Transition State Analysis of Model and Enzymatic Prenylation Reactions. Journal of the American Chemical Society  2007, 129, 5796-5797. DOI: 10.1021/ja069119j 

77. Hosokawa, A.; Wollack, J. W.; Zhang, Z.; Chen, L.; Barany, G.; Distefano, M. D., Evaluation of an alkyne-containing analogue of farnesyl diphosphate as a dual substrate for protein-prenyltransferases. International Journal of Peptide Research 2007, 13, (1-2), 345-354. DOI: 10.1007/s10989-007-9090-3 

76. Duckworth, B. P.; Zhang, Z.; Hosokawa, A.; Distefano, M. D., Selective Labeling of Proteins using Protein Farnesyltransferase. ChemBioChem 2007, 8, (1), 98-105. DOI: 10.1002/cbic.200600340 

75. Duckworth, B. P.; Chen, Y.; Sham, Y.; Mueller, J. D.; Taton, T. A.; Distefano, M. D., A Universal Method for the Preparation of Covalent Protein-DNA Conjugates for Use in Creating Protein Nanostructures. Angewante Chemie (Int. Ed) 2007, 46, 8819-8822. DOI: 10.1002/anie.200701942 

74. DeGraw, A. J.; Zhao, Z.; Hsieh, J.; Jefferies, M.; Distefano, M. D.; Strickland, C. L.; Shintani, D.; Nural, H.; McMahan, C.; Xie, W., A photoactive isoprenoid diphosphate analogue containing a stable phosphonate linkage: synthesis and structural biochemical studies with prenyltransferases. Journal of Organic Chemistry 2007, 72, (13), 4587 - 4595. DOI: 10.1021/jo0623033. 

2006

73. Xu, J.; DeGraw, A. J.; Duckworth, B. P.; Lenevich, S.; Tann, C.-M.; Jenson, E. C.; Gruber, S. J.; Barany, G.; Distefano, M. D., Synthesis and Reactivity of 6,7-Dihydrogeranylazides: Reagents for Primary Azide Incorporation into Peptides and Subsequent Staudinger Ligation. Chemical Biology and Drug Design 2006, 68, 85-96. DOI: 10.1111/j.1747-0285.2006.00420.x 

72. Duckworth, B. P.; Xu, J.; Taton, T. A.; Guo, A.; Distefano, M. D., Site-Specific, Covalent Attachment of Proteins to a Solid Surface. Bioconjugate Chemistry 2006, 17, (4), 967-974. DOI: 10.1021/bc060125e 

71. Distefano, M. D.; Albers, L. N.; Xu, J.-H., Protein Prenylation. In Encyclopedic Reference of Genomics and Proteomics in Molecular Medicine, ed.; Ruckpaul, K.; Ganten, D., Springer-Verlag: Heidelberg, Germany, 2006; pp 349-354.

2005 and prior years

70. Duckworth, B.; Distefano, M. D., Protein-based artificial enzymes. In Artificial Enzymes, ed.; Breslow, R., Wiley-VCH Verlag: Weinheim, Germany, 2005; p 109-132. 

69. Rose, M. W.; Rose, N. D.; Boggs, J.; Lenevich, S.; Xu, J.; Barany, G.; Distefano, M. D., Evaluation of geranylazide and farnesylazide diphosphate for incorporation of prenylazides into a CAAX box-containing peptide using protein farnesyltransferase. Journal of Peptide Research 2005, 65, 529-537. DOI: 10.1111/j.1399-3011.2005.00261.x 

68. Rose, M. W.; Xu, J.; Kale, T. A.; O'Doherty, G.; Barany, G.; Distefano, M. D., Enzymatic incorporation of orthogonally reactive prenylazide groups into peptides via protein farnesyltransferase: implications for selective protein labeling. Biopolymers 2005, 80, (2-3), 164-171. 

67. Adams, D. N.; Kao, E. Y.-C.; Hypolite, C. L.; Distefano, M. D.; Hu, W.-S.; Letourneau, P. C., Growth cones turn and migrate up an immobilized gradient of the laminin IKVAV peptide. Journal of Neurobiology 2004, 62, (1), 134-147. DOI: 10.1002/neu.20075 

66. Franklin, M. C.; Kadkhodayan, S.; Ackerly, H.; Alexandru, D.; Distefano, M. D.; Elliott, L. O.; Flygare, J. A.; Mausisa, G.; Okawa, D. C.; Ong, D.; Vucic, D.; Deshayes, K.; Fairbrother, W. J., Structure and Function Analysis of Peptide Antagonists of Melanoma Inhibitor of Apoptosis (ML-IAP). Biochemistry 2003, 42, (27), 8223-8231. DOI: 10.1021/bi034227t 

65. Kale, T. A.; Distefano, M. D., Diazotrifluoropropionamido-Containing Prenylcysteines: Syntheses and Applications for Studying Isoprenoid-Protein Interactions. Organic Letters 2003, 5, (5), 609-612. DOI: 10.1021/ol026752a 

64. Kale, T. A.; Hsieh, S.-A. J.; Rose, M. W.; Distefano, M. D., Use of synthetic isoprenoid analogues for understanding protein prenyltransferase mechanism and structure. Current Topics in Medicinal Chemistry 2003, 3, (10), 1043-1074. DOI: 10.2174/1568026033452087 

63. Kale, T. A.; Raab, C.; Yu, N.; Aquino, E.; Dean, D. C.; Distefano, M. D., Synthesis of high specific activity 35S-labelled N-methanesulfonyl farnesylcysteine and a photoactive analog. Journal of Labelled Compounds & Radiopharmaceuticals 2003, 46, (1), 29-54. DOI: 10.1002/jlcr.638 

62. Turek-Etienne, T. C.; Strickland, C. L.; Distefano, M. D., Biochemical and Structural Studies with Prenyl Diphosphate Analogues Provide Insights into Isoprenoid Recognition by Protein Farnesyl Transferase. Biochemistry 2003, 42, (13), 3716-3724. DOI: 10.1021/bi0266838 

61. Distefano, M. D.; Zhong, A.; Cochran, A. G., Quantifying β-Sheet stability by phage display. Journal of Molecular Biology 2002, 322, (1), 179-188. DOI:10.1016/S0022-2836(02)00738-6 

60. Häring, D.; Lees, M. R.; Banaszak, L. J.; Distefano, M. D., Exploring routes to stabilize a cationic pyridoxamine in an artificial transaminase: site-directed mutagenesis versus synthetic cofactors. Protein Engineering 2002, 15, (7), 603-10. 

59. Kale, T. A.; Turek, T. C.; Chang, V.; Gautam, N.; Distefano, M. D., Preparation and application of G protein g subunit-derived peptides incorporating a photoactive isoprenoid. Methods in Enzymology 2002, 344, (G Protein Pathways, Part B), 245-258. 

58. Clausen, V. A.; Edelstein, R. L.; Distefano, M. D., Stereochemical Analysis of the Reaction Catalyzed by Human Protein Geranylgeranyl Transferase. Biochemistry 2001, 40, (13), 3920-3930. DOI: 10.1021/bi002011a 

57. Häring, D.; Distefano, M. D., Enzymes by Design: Chemogenetic Assembly of Transamination Active Sites Containing Lysine Residues for Covalent Catalysis. Bioconjugate Chemistry 2001, 12, (3), 385-390. DOI: 10.1021/bc000117c 

56. Häring, D.; Distefano, M. D., Specific Host-Guest Interactions in a Protein-Based Artificial Transaminase. Bioorganic and Medicinal Chemistry 2001, 9, 2461-2466. 

55. Häring, D.; Distefano, M. D., Converting a Fatty Acid Binding Protein to a Artificial Transaminase: Novel Catalysts by Chemical and Genetic Modification of a Protein Cavity. Journal of Molecular Catalysis. B, Enzymatic 2001, 11, 967-970. 

54. Kale, T. A.; Raab, C.; Yu, N.; Dean, D. C.; Distefano, M. D., A Photoactivatable Prenylated Cysteine Designed to Study Isoprenoid Recognition. Journal of the American Chemical Society 2001, 123, (19), 4373-4381. DOI: 10.1021/ja0012016 

53. Qi, D.; Tann, C.-M.; Häring, D.; Distefano, M. D., Generation of new enzymes via covalent modification of existing proteins. Chemical Reviews 2001, 101, (10), 3081-3111. DOI: 10.1021/cr000059o. 

52. Tann, C.-M.; Qi, D.; Distefano, M. D., Enzyme design by chemical modification of protein scaffolds. Current Opinion in Chemical Biology 2001, 5, (6), 696-704. 

51. Turek, T. C.; Gaon, I.; Distefano, M. D.; Strickland, C. L., Synthesis of Farnesyl Diphosphate Analogues Containing Ether-Linked Photoactive Benzophenones and Their Application in Studies of Protein Prenyltransferases. Journal of Organic Chemistry 2001, 66, (10), 3253-3264. DOI: 10.1021/jo991130x. 

50. Distefano, M. D.; Kuang, H.; Qi, D.; Häring, D.; Ory, J.; Banaszak, L. J., Semisynthetic approaches for the design of proteins with catalytic activity using fatty acid binding protein as a scaffold. Peptides for the New Millennium, Proceedings of the American Peptide Symposium, 16th, Minneapolis, MN, United States, June 26-July 1, 1999 2000, 500-502. 

49. Kale, T. A.; Distefano, M. D., Photoaffinity-labeled probes for the study of isoprenoid recognition sites. Peptides for the New Millennium, Proceedings of the American Peptide Symposium, 16th, Minneapolis, MN, United States, June 26-July 1, 1999 2000, 109-110. 

48. Kuang, H.; Häring, D.; Qi, D.; Mazhary, A.; Distefano, M. D., Synthesis of a cationic pyridoxamine conjugation reagent and application to the mechanistic analysis of an artificial transaminase. Bioorganic & Medicinal Chemistry Letters 2000, 10, 2091-2095. 

47. Davies, R. R.; Kuang, H.; Qi, D.; Mazhary, A.; Mayaan, E.; Distefano, M. D., Artificial metalloenzymes based on protein cavities: exploring the effect of altering the metal ligand attachment position by site directed mutagenesis. Bioorganic & Medicinal Chemistry Letters 1999, 9, (1), 79-84. 

46. Distefano, M. D.; Kuang, H.; Qi, D.; Mazhary, A., The design of protein-based catalysts using semisynthetic methods. Current Opinion in Structural Biology 1998, 8, (4), 459-465. 

45. Edelstein, R. L.; Weller, V. A.; Distefano, M. D.; Tung, J. S., Stereochemical Analysis of the Reaction Catalyzed by Yeast Protein Farnesyltransferase. Journal of Organic Chemistry 1998, 63, (16), 5298-5299. DOI: 10.1021/jo980304s 

44. Kuang, H.; Distefano, M. D., Catalytic Enantioselective Reductive Amination in a Host-Guest System Based on a Protein Cavity. Journal of the American Chemical Society 1998, 120, (5), 1072-1073. DOI: 10.1021/ja972771h 

43. Ory, J. J.; Mazhary, A.; Kuang, H.; Davies, R. R.; Distefano, M. D.; Banaszak, L. J., Structural characterization of two synthetic catalysts based on adipocyte lipid-binding protein. Protein Engineering 1998, 11, (4), 253-261. 

42. Qi, D.; Kuang, H.; Distefano, M. D., Effects of metal ions on the rates and enantioselectivities of reactions catalyzed by a series of semisynthetic transaminases created by site directed mutagenesis. Bioorganic & Medicinal Chemistry Letters 1998, 8, (7), 875-880. 

41. Tabakovic, I.; Gaon, I.; Distefano, M. D., Anodic oxidation of substituted [4-hydroxy-3-coumarinyl]-phenylthiomethanes in acetonitrile. Evidence for a cationic intermediate in carbon-sulfur bond fragmentation. Electrochimica Acta 1998, 43, (12-13), 1773-1778. 

40. Turek, T. C.; Edelstein, R. L.; Gaon, I.; Weller, V. A.; Distefano, M. D., [32P]-labeled analogs of farnesyl and geranylgeranyl pyrophosphate: Synthesis and application in photoaffinity labeling experiments with protein prenyltransferases. In Synthesis and Applications of Isotopically Labelled Compounds 1997, Proceedings of the International Symposium, 6th, Philadelphia, PA, United States, Sept. 14-18, 1997, 1998; p 67-70. 

39. Weller, V. A.; Distefano, M. D., Measurement of the α-Secondary Kinetic Isotope Effect for a Prenyltransferase by MALDI Mass Spectrometry. Journal of the American Chemical Society 1998, 120, (31), 7975-7976. DOI: 10.1021/ja980353m 

38. Kuang, H.; Distefano, M. D., Artificial enzymes based on protein cavities: inversion of reaction enantioselectivity by alteration of the site of catalyst attachment. Protein Eng. 1997, 10, 25. 

37. Davies, R. R.; Brown, M. L.; Distefano, M. D., An artificial metalloenzyme based on a protein cavity that catalyzes the enantio-selective hydrolysis of amino acid esters. Protein Eng. 1997, 10, 61. 

36. Hypolite, C. L.; McLernon, T.; Adams, D.; Herbert, C.; Huang, C. C.; Hu, W.-S.; Distefano, M. D., Two-dimensional surface gradients of photoactivable R-phycoerythrin. Protein Eng. 1997, 10, 84. 

35. Davies, R. R.; Distefano, M. D., A Semisynthetic Metalloenzyme Based on a Protein Cavity That Catalyzes the Enantioselective Hydrolysis of Ester and Amide Substrates. Journal of the American Chemical Society 1997, 119, (48), 11643-11652. DOI: 10.1021/ja970820k 

34. Edelstein, R. L.; Distefano, M. D., Photoaffinity Labeling of Yeast Farnesyl Protein Transferase and Enzymatic Synthesis of a Ras Protein Incorporating a Photoactive Isoprenoid. Biochemical and Biophysical Research Communications 1997, 235, 377-382. 

33. Herbert, C. B.; McLernon, T. L.; Hypolite, C. L.; Adams, D. N.; Pikus, L.; Huang, C. C.; Fields, G. B.; Letourneau, P. C.; Distefano, M. D.; Hu, W.-S., Micropatterning gradients and controlling surface densities of photoactivatable biomolecules on self-assembled monolayers of oligo(ethylene glycol) alkanethiolates. Chemistry & Biology 1997, 4, (10), 731-737. 

32. Hypolite, C. L.; McLernon, T. L.; Adams, D. N.; Chapman, K. E.; Herbert, C. B.; Huang, C. C.; Distefano, M. D.; Hu, W.-S., Formation of Microscale Gradients of Protein Using Heterobifunctional Photolinkers. Bioconjugate Chemistry 1997, 8, (5), 658-663. DOI: 10.1021/bc9701252 

31. Kuang, H.; Davies, R. R.; Distefano, M. D., Modulation of the rate, enantioselectivity, and substrate specificity of semisynthetic transaminases based on lipid binding proteins using site directed mutagenesis. Bioorganic & Medicinal Chemistry Letters 1997, 7, (15), 2055-2060. 

30. Turek, T. C.; Gaon, I.; Distefano, M. D., Synthesis and rapid purification of 32P-labeled photoactive analogs of farnesyl pyrophosphate. Journal of Labelled Compounds & Radiopharmaceuticals 1997, 39, (2), 139-146. 

29. Turek, T. C.; Gaon, I.; Gamache, D.; Distefano, M. D., Synthesis and evaluation of benzophenone-based photoaffinity labeling analogs of prenyl pyrophosphates containing stable amide linkages. Bioorganic & Medicinal Chemistry Letters 1997, 7, (16), 2125-2130. 

28. Gaon, I.; Turek, T. C.; Distefano, M. D., Farnesyl and geranylgeranyl pyrophosphate analogs incorporating benzoylbenzyl ethers: synthesis and inhibition of yeast protein farnesyltransferase. Tetrahedron Letters 1996, 37, (49), 8833-8836. 

27. Edelstein, R. L.; Distefano, M. D., Photoaffinity Labeling using Photoreactive Isoprenoid Analogs. FASEB J. 1997, 11, A1087. 

26. Weller, V. A.; Turek, T. C.; Gaon, I.; Distefano, M. D., Mechanistic and Structural Studies on Protein Prenyl Transferases. FASEB J. 1997, 11, A1086. 

25. Ory, J. J.; Kuang, H.; Davies, R. R.; Mazhary, A.; Distefano, M. D.; Banaszak, L. J., Structural Characterization of Two Artificial Enzymes Based on Adipocyte Lipid Binding Protein. FASEB. J. 1997, 11, A1323. 

24. Gaon, I.; Turek, T. C.; Weller, V. A.; Edelstein, R. L.; Singh, S. K.; Distefano, M. D., Photoactive Analogs of Farnesyl Pyrophosphate Containing Benzoylbenzoate Esters: Synthesis and Application to Photoaffinity Labeling of Yeast Protein Farnesyltransferase. Journal of Organic Chemistry 1996, 61, (22), 7738-7745. DOI: 10.1021/jo9602736 

23. Kuang, H.; Brown, M. L.; Davies, R. R.; Young, E. C.; Distefano, M. D., Enantioselective Reductive Amination of α-Keto Acids to α-Amino Acids by a Pyridoxamine Cofactor in a Protein Cavity. Journal of the American Chemical Society 1996, 118, (44), 10702-10706. DOI: 10.1021/ja954271z 

22. Turek, T. C.; Gaon, I.; Distefano, M. D., Analogs of farnesyl pyrophosphate incorporating internal benzoylbenzoate esters: synthesis, inhibition kinetics and photoinactivation of yeast protein farnesyltransferase. Tetrahedron Letters 1996, 37, (28), 4845-4848. 

 

MDD Postdoctoral Research

21. Colocci, N.; Distefano, M. D.; Dervan, P. B., Cooperative oligonucleotide-directed triple helix formation at adjacent DNA sites. Journal of the American Chemical Society 1993, 115, (11), 4468-73. DOI: 10.1021/ja00064a008 

20. Distefano, M. D.; Dervan, P. B., Energetics of cooperative binding of oligonucleotides with discrete dimerization domains to DNA by triple helix formation. Proceedings of the National Academy of Sciences of the United States of America 1993, 90, (4), 1179-83. 

19. Distefano, M. D.; Dervan, P. B., Ligand-promoted dimerization of oligonucleotides binding cooperatively to DNA. Journal of the American Chemical Society 1992, 114, (27), 11006-7. DOI: 10.1021/ja00053a073 

18. Distefano, M. D.; Shin, J. A.; Dervan, P. B., Cooperative binding of oligonucleotides to DNA by triple helix formation: dimerization via Watson-Crick hydrogen bonds. Journal of the American Chemical Society 1991, 113, (15), 5901-2. DOI: 10.1021/ja00015a076 

 

MDD Ph.D. Research

17. Schiering, N.; Kabsch, W.; Moore, M. J.; Distefano, M. D.; Walsh, C. T.; Pai, E. F., Structure of the Detoxification Catalyst Mercuric Ion Reductase from Bacillus sp. strain RC607. Nature 1991, 352, 168-172. 

16. Schiering, N.; Kabsch, W.; Moore, M. J.; Distefano, M. D.; Walsh, C. T.; Pai, E. F., The Three Dimensional Structure of Mercuric Ion Reductase from Bacillus Strain RC607. In Flavins and Flavoproteins 1990, ed.; Curti, B.; Ronchi, S.; Zanetti, G., Walter de Gruyter & Co.: Berlin, 1991; p 615-625. 

15. Distefano, M. D.; Moore, M. J.; Walsh, C. T., Active site of mercuric reductase resides at the subunit interface and requires Cys135 and Cys140 from one subunit and Cys558 and Cys559 from the adjacent subunit: evidence from in vivo and in vitro heterodimer formation. Biochemistry 1990, 29, (11), 2703-13. DOI: 10.1021/bi00463a013 

14. Miller, S. M.; Massey, V.; Ballou, D.; Williams, C. H., Jr.; Distefano, M. D.; Moore, M. J.; Walsh, C. T., Use of a site-directed triple mutant to trap intermediates: demonstration that the flavin C(4a)-thiol adduct and reduced flavin are kinetically competent intermediates in mercuric ion reductase. Biochemistry 1990, 29, (11), 2831-41. DOI: 10.1021/bi00463a028 

13. Moore, M. J.; Distefano, M. D.; Zydowsky, L. D.; Cummings, R. T.; Walsh, C. T., Organomercurial lyase and mercuric ion reductase: nature's mercury detoxification catalysts. Accounts of Chemical Research 1990, 23, (9), 301-8. DOI: 10.1021/ar00177a006 

12. Raybuck, S. A.; Distefano, M. D.; Teo, B. K.; Orme-Johnson, W.; Walsh, C. T., An EXAFS investigation of Hg(II) binding to mercuric reductase: comparative analysis of the wild-type enzyme and a mutant enzyme generated by site-directed mutagenesis. Journal of the American Chemical Society 1990, 112, (5), 1983-9. DOI: 10.1021/ja00161a051 

11. Distefano, M. D.; Au, K. G.; Walsh, C. T., Mutagenesis of the redox-active disulfide in mercuric ion reductase: catalysis by mutant enzymes restricted to flavin redox chemistry. Biochemistry 1989, 28, (3), 1168-83. DOI: 10.1021/bi00429a035 

10. Miller, S. M.; Moore, M. J.; Massey, V.; Williams, C. H., Jr.; Distefano, M. D.; Ballou, D. P.; Walsh, C. T., Evidence for the participation of Cys558 and Cys559 at the active site of mercuric reductase. Biochemistry 1989, 28, (3), 1194-205. DOI: 10.1021/bi00429a037 

9. Moore, M. J.; Distefano, M. D.; Walsh, C. T.; Schiering, N.; Pai, E. F., Purification, crystallization, and preliminary x-ray diffraction studies of the flavoenzyme mercuric ion reductase from Bacillus sp. strain RC607. Journal of Biological Chemistry 1989, 264, (24), 14386-8. 

8. Walsh, C.; Distefano, M. D.; Moore, M., Mutagenesis of paired cysteine residues in the disulphide-containing flavoprotein mercuric ion reductase from mercury-resistant bacteria. Biochemical Society Transactions 1988, 16, (2), 90-1. 

7. Walsh, C. T.; Distefano, M. D.; Moore, M. J.; Shewchuk, L. M.; Verdine, G. L., Molecular basis of bacterial resistance to organomercurial and inorganic mercuric salts. FASEB Journal 1988, 2, (2), 124-30. 

6. Massey, V.; Miller, S.; Ballou, D. P.; Williams, C. H.; Moore, M. J.; Distefano, M. D.; Walsh, C. T., Studies of the Active Site of Mercuric Reductase Employing Site Directed Mutants and the Thiol-Reactive Flavin, 6-SCN-FAD. In Flavins and Flavoproteins 1987, ed.; Edmondson, D. E.; McCormick, D. B., Walter de Gruyter & Co.: Berlin, 1987; p 41-44. 

5. Moore, M. J.; Distefano, M. D.; Walsh, C. T.; Miller, S.; Massey, V.; Williams, C. H.; Ballou, D. P., The Penultimate Cysteines in Mercuric Reductase Aid in the Reduction of Mercury. In Flavins and Flavoproteins 1987, ed.; Edmondson, D. E.; McCormick, D. B., Walter de Gruyter & Co.: Berlin, 1987; p 37-40. 

4. Neidhard, D. J.; Distefano, M. D.; Tanizawa, K.; Soda, K.; Walsh, C. T.; Petsko, G. A., X-ray crystallographic studies of the alanine-specific racemase from Bacillus stearothermophilus. Overproduction, crystallization, and preliminary characterization. Journal of Biological Chemistry 1987, 262, (32), 15323-6. 

3. Walsh, C.; Distefano, M. D.; Moore, M., Catalytic effects of mutagenesis of paired cysteine residues in the bacterial enzyme mercuric ion reductase. UCLA Symposia on Molecular and Cellular Biology, New Series 1987, 69, (Protein Struct., Folding, Des. 2), p 283-92. 

2. Walsh, C. T.; Moore, M. J.; Distefano, M. D., Conserved Cysteine Pairs of Mercuric Ion Reductase: An Investigation of Function Via Site-Directed Mutagenesis. In Flavins and Flavoproteins 1987, ed.; Edmondson, D. E.; McCormick, D. B.,Walter de Gruyter & Co.: Berlin, 1987; p 13-28. 

 

MDD Undergraduate Research

1. Kanazawa, T.; Distefano, M. D.; Bassham, J. A., Ammonia regulation of intermediary metabolism in photosynthesizing and respiring Chlorella pyrenoidosa: comparative effects of methylamine. Plant and Cell Physiology 1983, 24, (6), 979-86.