V. Schramm

发表

Azetidine based transition state analogue inhibitors of N-ribosyl hydrolases and phosphorylases.

G. Evans, R. Furneaux, B. Greatrex, 2008, Journal of medicinal chemistry.

Synthesis of 5'-methylthio coformycins: specific inhibitors for malarial adenosine deaminase.

V. Schramm, P. Tyler, E. Taylor, 2007, Journal of the American Chemical Society.

Transition-state analogs as inhibitors of human and malarial hypoxanthine-guanine phosphoribosyltransferases

R. Furneaux, V. Schramm, P. Tyler, 1999, Nature Structural Biology.

Purine-less Death in Plasmodium falciparumInduced by Immucillin-H, a Transition State Analogue of Purine Nucleoside Phosphorylase*

G. Evans, R. Furneaux, V. Schramm, 2002, The Journal of Biological Chemistry.

Enzymatic transition states and transition state analog design.

V. Schramm, 1998, Annual review of biochemistry.

The biochemistry of sirtuins.

J. Boeke, V. Schramm, C. Wolberger, 2006, Annual review of biochemistry.

Enzymatic transition states and dynamic motion in barrier crossing.

V. Schramm, S. Schwartz, 2009, Nature chemical biology.

Insight into catalytically relevant correlated motions in human purine nucleoside phosphorylase.

V. Schramm, S. Schwartz, S. Núñez, 2006, The journal of physical chemistry. A.

Stabilization of allosteric adenosine monophosphate nucleosidase by inorganic salts, substrate, and essential activator.

V. Schramm, L. Hochstein, 1971, Biochemistry.

Transition state structure of 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase from Escherichia coli and its similarity to transition state analogues.

V. Schramm, P. Howell, Jeffrey E. Lee, 2005, Biochemistry.

Recycling nicotinamide. The transition-state structure of human nicotinamide phosphoribosyltransferase.

V. Schramm, E. Burgos, Mathew J. Vetticatt, 2013, Journal of the American Chemical Society.

Achieving the Ultimate Physiological Goal in Transition State Analogue Inhibitors for Purine Nucleoside Phosphorylase*

G. Evans, R. Furneaux, V. Schramm, 2003, Journal of Biological Chemistry.

Binding Isotope Effects for para-Aminobenzoic Acid with Dihydropteroate Synthase from Staphylococcus aureus and Plasmodium falciparum.

Christopher F Stratton, V. Schramm, S. Cameron, 2015, ACS chemical biology.

Transition State Structure of RNA Depurination by Saporin L3.

Christopher F Stratton, V. Schramm, Hongling Yuan, 2016, ACS chemical biology.

Supplemental Data Ribocation Transition State Capture and Rebound in Human Purine Nucleoside Phosphorylase

A. S. Murkin, V. Schramm, Mahmoud Ghanem, 2009 .

Ribocation transition state capture and rebound in human purine nucleoside phosphorylase.

A. S. Murkin, V. Schramm, Mahmoud Ghanem, 2009, Chemistry & biology.

Transition state structure for ADP-ribosylation of eukaryotic elongation factor 2 catalyzed by diphtheria toxin.

V. Schramm, S. Parikh, 2004, Biochemistry.

Sir2 regulation by nicotinamide results from switching between base exchange and deacetylation chemistry.

V. Schramm, A. Sauve, 2003, Biochemistry.

A picomolar transition state analogue inhibitor of MTAN as a specific antibiotic for Helicobacter pylori.

G. Evans, V. Schramm, P. Tyler, 2012, Biochemistry.

A Transition State Analogue of 5′-Methylthioadenosine Phosphorylase Induces Apoptosis in Head and Neck Cancers*

V. Schramm, C. Guha, T. Belbin, 2007, Journal of Biological Chemistry.

The effect of a novel transition state inhibitor of methylthioadenosine phosphorylase on pemetrexed activity

V. Schramm, I. Goldman, R. Zhao, 2006, Molecular Cancer Therapeutics.

Prediction of inhibitor binding free energies by quantum neural networks. Nucleoside analogues binding to trypanosomal nucleoside hydrolase.

V. Schramm, S. Schwartz, B. B. Braunheim, 1999, Biochemistry.

Immucillin‐H binding to purine nucleoside phosphorylase reduces dynamic solvent exchange

R. Angeletti, V. Schramm, G. Kicska, 2000, Protein science : a publication of the Protein Society.

Vinyldeoxyadenosine in a sarcin-ricin RNA loop and its binding to ricin toxin a-chain.

V. Schramm, Suwipa Saen-oon, Setu Roday, 2007, Biochemistry.

Transition-state structure of neisseria meningitides 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase.

V. Schramm, M. Luo, G. Norris, 2007, Journal of the American Chemical Society.

Salmonella enterica MTAN at 1.36 Å resolution. Structure-based design of new transition state analogues

G. Evans, V. Schramm, P. Tyler, 2013 .

Mechanism-based inhibitors of CD38: a mammalian cyclic ADP-ribose synthetase.

V. Schramm, A. Sauve, 2002, Biochemistry.

Synthesis and Characterization of Transition-State Analogue Inhibitors against Human DNA Methyltransferase 1.

V. Schramm, P. Tyler, A. D. Woolhouse, 2022, Journal of medicinal chemistry.

Small molecule inhibitors targeting the interaction of ricin toxin A subunit with ribosomes.

V. Schramm, N. Tumer, Xiao-Ping Li, 2020, ACS infectious diseases.

Enzymatic transition state poise and transition state analogues.

V. Schramm, 2003, Accounts of chemical research.

Evaluation of the relationship between the intra- and extramitochondrial [ATP]/[ADP] ratios using phosphoenolpyruvate carboxykinase.

V. Schramm, M. Erecińska, D. Wilson, 1983, The Journal of biological chemistry.

Mn2(+)-binding properties of a recombinant protein-tyrosine kinase derived from the human insulin receptor.

V. Schramm, O. Rosen, S. Wente, 1990, Proceedings of the National Academy of Sciences of the United States of America.

Crystal structures of Giardia lamblia guanine phosphoribosyltransferase at 1.75 A(,).

R. Furneaux, V. Schramm, P. Tyler, 2000, Biochemistry.

A β -Fluoroamine Inhibitor of Purine Nucleoside Phosphorylase

A. S. Murkin, V. Schramm, B. Skelton, 2015 .

Intracellular rebinding of transition-state analogues provides extended in vivo inhibition lifetimes on human purine nucleoside phosphorylase

V. Schramm, Lei Li, Y. Babu, 2017, The Journal of Biological Chemistry.

Transition state analysis of thymidine hydrolysis by human thymidine phosphorylase.

V. Schramm, Phillip A. Schwartz, Mathew J. Vetticatt, 2010, Journal of the American Chemical Society.

Chemoenzymatic Synthesis of (36)S Isotopologues of Methionine and S-Adenosyl-L-methionine.

V. Schramm, M. Poulin, Quan Du, 2015, The Journal of organic chemistry.

Conformational states of human purine nucleoside phosphorylase at rest, at work, and with transition state analogues.

G. Evans, V. Schramm, P. Tyler, 2010, Biochemistry.

Mechanism and Inhibition of Human Methionine Adenosyltransferase 2A.

V. Schramm, S. Cahill, C. Niland, 2021, Biochemistry.

Transition state analogue of MTAP extends lifespan of APCMin/+ mice

V. Schramm, L. Augenlicht, I. Basu, 2020, Scientific Reports.

Entropy-driven binding of picomolar transition state analogue inhibitors to human 5'-methylthioadenosine phosphorylase.

G. Evans, V. Schramm, P. Tyler, 2011, Biochemistry.

Ricin A-chain inhibitors resembling the oxacarbenium ion transition state.

R. Furneaux, V. Schramm, P. Tyler, 2001, Biochemistry.

Clostridioides difficile TcdB Toxin Glucosylates Rho GTPase by an SNi Mechanism and Ion Pair Transition State

V. Schramm, S. Cahill, A. Paparella, 2022, ACS chemical biology.

Nucleosome Binding Alters the Substrate Bonding Environment of Histone H3 Lysine 36 Methyltransferase NSD2.

V. Schramm, Marc A. Holbert, R. Matico, 2016, Journal of the American Chemical Society.

Kinetic Characterization and Inhibition of Trypanosoma cruzi Hypoxanthine–Guanine Phosphoribosyltransferases

V. Schramm, P. Tyler, T. Meek, 2022, Biochemistry.

Transition State Analogue Inhibitors of 5'-Deoxyadenosine/5'-Methylthioadenosine Nucleosidase from Mycobacterium tuberculosis.

G. Evans, V. Schramm, P. Tyler, 2017, Biochemistry.

Transition state for the NSD2-catalyzed methylation of histone H3 lysine 36

V. Schramm, S. Thrall, M. Huddleston, 2016, Proceedings of the National Academy of Sciences.

Pyrophosphate activation in hypoxanthine--guanine phosphoribosyltransferase with transition state analogue.

V. Schramm, C. Grubmeyer, R. Callender, 2010, Biochemistry.

Tight binding enantiomers of pre-clinical drug candidates.

G. Evans, V. Schramm, P. Tyler, 2015, Bioorganic & medicinal chemistry.

Tryptophan-free human PNP reveals catalytic site interactions.

V. Schramm, S. Cahill, R. Callender, 2008, Biochemistry.

Weak coupling of ATP hydrolysis to the chemical equilibrium of human nicotinamide phosphoribosyltransferase.

V. Schramm, E. Burgos, Emmanuel S. Burgos, 2008, Biochemistry.

Binding isotope effects: boon and bane.

V. Schramm, 2007, Current opinion in chemical biology.

Antibacterial Strategy against H. pylori: Inhibition of the Radical SAM Enzyme MqnE in Menaquinone Biosynthesis.

V. Schramm, T. Begley, Sumedh Joshi, 2019, ACS medicinal chemistry letters.

Uridine phosphorylase from Trypanosoma cruzi: kinetic and chemical mechanisms.

V. Schramm, R. G. Silva, 2011, Biochemistry.

[33] Adenosine monophosphate nucleosidase from Azotobacter vinelandii and Escherichia coli

V. Schramm, H. Leung, 1978 .

Structural and kinetic characterization of Escherichia coli TadA, the wobble-specific tRNA deaminase.

V. Schramm, V. Malashkevich, S. Almo, 2006, Biochemistry.

The reaction mechanism for CD38. A single intermediate is responsible for cyclization, hydrolysis, and base-exchange chemistries.

V. Schramm, A. Sauve, H. C. Lee, 1998, Biochemistry.

Mn2+-sensitive and -insensitive forms of phosphoenolpyruvate carboxykinase (GTP).

V. Schramm, R. Hanson, R. Brinkworth, 1981, The Journal of biological chemistry.

Studies on an aged preparation of nucleoside diphosphatase. Kinetics and reaction mechanism.

V. Schramm, J. Morrison, 1970, Biochemistry.

Protein dynamics by hydrogen/deuterium exchange coupled to mass spectrometry: Purine nucleoside phosphorylase

R. Angeletti, V. Schramm, F. Wang, 2002 .

Kinetic mechanism of phosphoenolpyruvate carboxykinase (GTP) from rat liver cytosol. Product inhibition, isotope exchange at equilibrium, and partial reactions.

V. Schramm, V. Schramm, M. Jomain-Baum, 1978, The Journal of biological chemistry.

Characterizing DNA methyltransferases with an ultrasensitive luciferase-linked continuous assay.

V. Schramm, I. Hemeon, M. Ho, 2011, Analytical chemistry.

Studies on the allosteric modification of nucleoside diphosphatase activity by magnesium nucleoside triphosphates and inosine diphosphate.

V. Schramm, J. Morrison, 1971, Biochemistry.

Trypanosomal nucleoside hydrolase. A novel mechanism from the structure with a transition-state inhibitor.

V. Schramm, S. Almo, J. Sacchettini, 1998, Biochemistry.

Circular DNA and DNA/RNA hybrid molecules as scaffolds for ricin inhibitor design.

V. Schramm, Matthew B. Sturm, Setu Roday, 2007, Journal of the American Chemical Society.

Binding Isotope Effects for Interrogating Enzyme-Substrate Interactions.

Christopher F Stratton, V. Schramm, M. Poulin, 2017, Methods in enzymology.

Transition state structure of E. coli tRNA-specific adenosine deaminase.

V. Schramm, M. Luo, 2008, Journal of the American Chemical Society.

Mammalian and avian liver phosphoenolpyruvate carboxykinase. Alternate substrates and inhibition by analogues of oxaloacetate.

V. Schramm, Y. Satoh, D. Ash, 1990, The Journal of biological chemistry.

Inhibition and Mechanism of Plasmodium falciparum Hypoxanthine-Guanine-Xanthine Phosphoribosyltransferase.

V. Schramm, P. Tyler, S. Cahill, 2022, ACS chemical biology.

Detection of an abasic site in RNA with stem-loop DNA beacons: application to an activity assay for Ricin Toxin A-Chain.

V. Schramm, D. Blakaj, Matthew B. Sturm, 2008, Journal of biochemical and biophysical methods.

Addition of lithiated 9-deazapurine derivatives to a carbohydrate cyclic imine: convergent synthesis of the aza-C-nucleoside immucillins.

G. Evans, R. Furneaux, V. Schramm, 2001, The Journal of organic chemistry.

Exploring structure-activity relationships of transition state analogues of human purine nucleoside phosphorylase.

G. Evans, R. Furneaux, V. Schramm, 2003, Journal of medicinal chemistry.

Femtosecond dynamics coupled to chemical barrier crossing in a Born-Oppenheimer enzyme

A. S. Murkin, V. Schramm, R. G. Silva, 2011, Proceedings of the National Academy of Sciences.

Arsenate and phosphate as nucleophiles at the transition states of human purine nucleoside phosphorylase.

A. S. Murkin, V. Schramm, R. G. Silva, 2011, Biochemistry.

Second generation transition state analogue inhibitors of human 5'-methylthioadenosine phosphorylase.

G. Evans, R. Furneaux, V. Schramm, 2005, Journal of medicinal chemistry.

Synthesis of second-generation transition state analogues of human purine nucleoside phosphorylase.

G. Evans, R. Furneaux, V. Schramm, 2003, Journal of medicinal chemistry.

8-Aza-immucillins as transition-state analogue inhibitors of purine nucleoside phosphorylase and nucleoside hydrolases.

J. Hanson, G. Evans, R. Furneaux, 2003, Journal of medicinal chemistry.

Transition state structure of purine nucleoside phosphorylase and principles of atomic motion in enzymatic catalysis.

J. Hanson, R. Furneaux, V. Schramm, 2001, Biochemistry.

Transition state analogue inhibitors of protozoan nucleoside hydrolases.

R. Furneaux, V. Schramm, P. Tyler, 1999, Bioorganic & medicinal chemistry.

Iminoribitol transition state analogue inhibitors of protozoan nucleoside hydrolases.

G. Evans, R. Furneaux, V. Schramm, 1999, Biochemistry.

A new class of C-nucleoside analogues. 1-(S)-aryl-1,4-dideoxy-1,4-imino-D-ribitols, transition state analogue inhibitors of nucleoside hydrolase

V. Schramm, B. Horenstein, R. Zabinski, 1993 .

Electronic nature of the transition state for nucleoside hydrolase. A blueprint for inhibitor design.

V. Schramm, B. Horenstein, 1993, Biochemistry.

Transition-state analysis of nucleoside hydrolase from Crithidia fasciculata.

V. Schramm, B. Horenstein, D. Parkin, 1991, Biochemistry.

Nucleoside hydrolase from Crithidia fasciculata. Metabolic role, purification, specificity, and kinetic mechanism.

V. Schramm, B. Horenstein, D. Parkin, 1991, The Journal of biological chemistry.

Inhibition of Clostridium difficile TcdA and TcdB toxins with transition state analogues

V. Schramm, P. Tyler, R. Harijan, 2021, Nature Communications.

Synthesis of a transition state analogue inhibitor of purine nucleoside phosphorylase via the Mannich reaction.

G. Evans, R. Furneaux, V. Schramm, 2003, Organic letters.

Third-generation immucillins: syntheses and bioactivities of acyclic immucillin inhibitors of human purine nucleoside phosphorylase.

Andrew S Murkin, G. Evans, R. Furneaux, 2009, Journal of medicinal chemistry.

Transition-State Analogues of Phenylethanolamine N-methyltransferase.

V. Schramm, R. Harijan, N. Mahmoodi, 2020, Journal of the American Chemical Society.

Energetic Mapping of Transition State Analogue Interactions with Human and Plasmodium falciparum Purine Nucleoside Phosphorylases*♦

G. Evans, R. Furneaux, V. Schramm, 2005, Journal of Biological Chemistry.

Structural Rationale for the Affinity of Pico- and Femtomolar Transition State Analogues of Escherichia coli 5′-Methylthioadenosine/S-Adenosylhomocysteine Nucleosidase*♦

G. Evans, R. Furneaux, V. Schramm, 2005, Journal of Biological Chemistry.

Assignment of downfield proton resonances in purine nucleoside phosphorylase immucillin-H complex by saturation-transferred NOEs.

R. Furneaux, V. Schramm, P. Tyler, 2004, Biochemistry.

Enzymatic Transition States and Drug Design.

V. Schramm, 2018, Chemical reviews.

The transition to magic bullets - transition state analogue drug design.

G. Evans, V. Schramm, P. Tyler, 2018, MedChemComm.

Development of transition state analogues of purine nucleoside phosphorylase as anti-T-cell agents.

V. Schramm, 2002, Biochimica et biophysica acta.

Synthesis of transition state inhibitors for N-riboside hydrolases and transferases

R. Furneaux, V. Schramm, P. Tyler, 1997 .

Correlation of the molecular electrostatic potential surface of an enzymatic transition state with novel transition-state inhibitors.

V. Schramm, B. Horenstein, 1993, Biochemistry.

Isozyme-specific transition state inhibitors for the trypanosomal nucleoside hydrolases.

R. Furneaux, V. Schramm, P. Tyler, 1997, Biochemistry.

Selective Inhibitors of Helicobacter pylori Methylthioadenosine Nucleosidase and Human Methylthioadenosine Phosphorylase.

G. Evans, V. Schramm, P. Tyler, 2019, Journal of medicinal chemistry.

Transition-State Analogues of Campylobacter jejuni 5'-Methylthioadenosine Nucleosidase.

G. Evans, V. Schramm, P. Tyler, 2018, ACS Chemical Biology.

The Transition-State Structure for Human MAT2A from Isotope Effects.

V. Schramm, Ross S. Firestone, 2017, Journal of the American Chemical Society.

Heat Capacity Changes for Transition-State Analogue Binding and Catalysis with Human 5'-Methylthioadenosine Phosphorylase.

V. Schramm, V. Arcus, S. Cameron, 2017, ACS chemical biology.

Continuous Fluorescence Assays for Reactions Involving Adenine.

V. Schramm, P. Tyler, S. Cameron, 2016, Analytical chemistry.

New Antibiotic Candidates against Helicobacter pylori.

G. Evans, V. Schramm, P. Tyler, 2015, Journal of the American Chemical Society.

Active site and remote contributions to catalysis in methylthioadenosine nucleosidases.

V. Schramm, S. Almo, E. Burgos, 2015, Biochemistry.

Thermodynamic analysis of transition-state features in picomolar inhibitors of human 5'-methylthioadenosine phosphorylase.

G. Evans, V. Schramm, P. Tyler, 2013, Biochemistry.

Salmonella enterica MTAN at 1.36 Å resolution: a structure-based design of tailored transition state analogs.

G. Evans, V. Schramm, P. Tyler, 2013, Structure.

Femtomolar inhibitors bind to 5'-methylthioadenosine nucleosidases with favorable enthalpy and entropy.

G. Evans, V. Schramm, P. Tyler, 2012, Biochemistry.

Transition state analogue inhibitors of human methylthioadenosine phosphorylase and bacterial methylthioadenosine/S-adenosylhomocysteine nucleosidase incorporating acyclic ribooxacarbenium ion mimics.

G. Evans, V. Schramm, P. Tyler, 2012, Bioorganic & medicinal chemistry.

Enzymatic transition states, transition-state analogs, dynamics, thermodynamics, and lifetimes.

V. Schramm, Vern L Schramm, 2011, Annual review of biochemistry.

Growth and Metastases of Human Lung Cancer Are Inhibited in Mouse Xenografts by a Transition State Analogue of 5′-Methylthioadenosine Phosphorylase*

G. Evans, V. Schramm, M. Cassera, 2010, The Journal of Biological Chemistry.

Design and synthesis of potent "sulfur-free" transition state analogue inhibitors of 5'-methylthioadenosine nucleosidase and 5'-methylthioadenosine phosphorylase.

G. Evans, V. Schramm, P. Tyler, 2010, Journal of medicinal chemistry.

Transition state analogues of 5′-methylthioadenosine nucleosidase disrupt quorum sensing

V. Schramm, S. Almo, M. Ho, 2009, Nature chemical biology.

Picomolar inhibitors as transition-state probes of 5'-methylthioadenosine nucleosidases.

G. Evans, R. Furneaux, V. Schramm, 2007, ACS chemical biology.

Structure and inhibition of a quorum sensing target from Streptococcus pneumoniae.

G. Evans, R. Furneaux, V. Schramm, 2006, Biochemistry.

Enzymatic transition states and transition state analogues.

V. Schramm, Vern L Schramm, 2005, Current opinion in structural biology.

Synthesis of bis-Phosphate Iminoaltritol Enantiomers and Structural Characterization with Adenine Phosphoribosyltransferase.

G. Evans, V. Schramm, R. Harijan, 2017, ACS chemical biology.

Immucillins ImmA and ImmH Are Effective and Non-toxic in the Treatment of Experimental Visceral Leishmaniasis

G. Evans, V. Schramm, P. Tyler, 2015, PLoS neglected tropical diseases.

Transition State Analogues of Plasmodium falciparum and Human Orotate Phosphoribosyltransferases*

G. Evans, V. Schramm, P. Tyler, 2013, The Journal of Biological Chemistry.

Leaving group activation and pyrophosphate ionic state at the catalytic site of Plasmodium falciparum orotate phosphoribosyltransferase.

V. Schramm, H. Deng, Yong Zhang, 2010, Journal of the American Chemical Society.

Synthesis of transition state analogue inhibitors for purine nucleoside phosphorylase and N-riboside hydrolases

G. Evans, R. Furneaux, V. Schramm, 2000 .

Inosine-uridine nucleoside hydrolase from Crithidia fasciculata. Genetic characterization, crystallization, and identification of histidine 241 as a catalytic site residue.

V. Schramm, J. Sacchettini, M. Degano, 1996, Biochemistry.

Mechanistic Diagnoses of N-Ribohydrolases and Purine Nucleoside Phosphorylase

R. Furneaux, V. Schramm, P. Tyler, 1996 .

Guanosine-inosine-preferring nucleoside N-glycohydrolase from Crithidia fasciculata.

V. Schramm, B. Estupiñán, 1994, The Journal of biological chemistry.

Syntheses of 5-Chlorouracils/Thymines with 1-[Phosphono(Methyl/Difluoromethyl)]-1,2-Unsaturated-Moiety-Substituted Methyl Groups at N(1) and Human Thymidine Phosphorylase Inhibitory Activity

V. Schramm, P. Tyler, G. Gainsford, 2009 .

The mechanism of soluble peptidoglycan hydrolysis by an autolytic muramidase. A processive exodisaccharidase.

V. Schramm, G. Shockman, J. Barrett, 1984, The Journal of biological chemistry.

Transition State Analogue Inhibitors of N‐Ribosyltransferases

V. Schramm, P. Tyler, 2008 .

The 2.0 A structure of malarial purine phosphoribosyltransferase in complex with a transition-state analogue inhibitor.

R. Furneaux, V. Schramm, P. Tyler, 1999, Biochemistry.

Inhibition of ricin by an rna stem-loop containing a ribo-oxycarbonium mimic

V. Schramm, T. Link, Xiangyang Chen, 1996 .

Transition states and inhibitors of the purine nucleoside phosphorylase family.

V. Schramm, Erika A Taylor Ringia, 2005, Current topics in medicinal chemistry.

Immucillins as Antibiotics for T‐Cell Proliferation and Malaria

V. Schramm, 2004, Nucleosides, nucleotides & nucleic acids.

Imino-sugar-based nucleosides.

V. Schramm, P. Tyler, 2003, Current topics in medicinal chemistry.

Immucillin H, a powerful transition-state analog inhibitor of purine nucleoside phosphorylase, selectively inhibits human T lymphocytes

R. Furneaux, V. Schramm, P. Tyler, 2001, Proceedings of the National Academy of Sciences of the United States of America.

One-third-the-sites transition-state inhibitors for purine nucleoside phosphorylase.

R. Furneaux, V. Schramm, P. Tyler, 1998, Biochemistry.

Purine nucleoside phosphorylase. Catalytic mechanism and transition-state analysis of the arsenolysis reaction.

V. Schramm, P C Kline, V L Schramm, 1993, Biochemistry.

Syntheses and bio-activities of the L-enantiomers of two potent transition state analogue inhibitors of purine nucleoside phosphorylases.

G. Evans, R. Furneaux, V. Schramm, 2006, Organic & biomolecular chemistry.

Electrostatic potential surfaces of the transition state for AMP deaminase and for (R)-coformycin, a transition state inhibitor.

V. Schramm, P. Kline, 1994, The Journal of biological chemistry.

Transition state analysis and inhibitor design for enzymatic reactions.

V. Schramm, B. Horenstein, P. Kline, 1994, The Journal of biological chemistry.

Ground-state destabilization in orotate phosphoribosyltransferases by binding isotope effects.

V. Schramm, Yong Zhang, 2011, Biochemistry.

Pyrophosphate interactions at the transition states of Plasmodium falciparum and human orotate phosphoribosyltransferases.

V. Schramm, Yong Zhang, 2010, Journal of the American Chemical Society.

The 2.0 Å structure of human hypoxanthine-guanine phosphoribosyltransferase in complex with a transition-state analog inhibitor

R. Furneaux, V. Schramm, P. Tyler, 1999, Nature Structural Biology.

Purification, properties, and allosteric activation of nucleoside diphosphatase.

V. Schramm, J. Morrison, 1968, Biochemistry.

Enzymatic N-riboside scission in RNA and RNA precursors.

V. Schramm, 1997, Current opinion in chemical biology.

Determination of free and bound manganese(II) in hepatocytes from fed and fasted rats.

V. Schramm, D. Ash, V. Schramm, 1982, The Journal of biological chemistry.

Catalytic mechanism of yeast adenosine 5'-monophosphate deaminase. Zinc content, substrate specificity, pH studies, and solvent isotope effects.

V. Schramm, D. Merkler, 1993, Biochemistry.

Action of magnesium ion on diphosphopyridine nucleotide-linked isocitrate dehydrogenase from bovine heart. Characterization of the forms of the substrate and the modifier of the reaction.

V. Schramm, G. Plaut, V L Schramm, 1974, The Journal of biological chemistry.

Hydride Transfer in DHFR by Transition Path Sampling, Kinetic Isotope Effects, and Heavy Enzyme Studies.

V. Schramm, Zhen Wang, S. Schwartz, 2016, Biochemistry.

Kinetic studies of the interaction of substrates, Mn2+, and Mg2+ with the Mn2+-sensitive and -insensitive forms of phosphoenolpyruvate carboxykinase.

V. Schramm, F. A. Fullin, M. Zimmerman, 1981, The Journal of biological chemistry.

Transition-state inhibitors of purine salvage and other prospective enzyme targets in malaria.

V. Schramm, Hilda A. Namanja-Magliano, R. G. Ducati, 2013, Future medicinal chemistry.

Inverse enzyme isotope effects in human purine nucleoside phosphorylase with heavy asparagine labels

V. Schramm, S. Schwartz, D. Antoniou, 2018, Proceedings of the National Academy of Sciences.

Constrained bonding environment in the Michaelis complex of Trypanosoma cruzi uridine phosphorylase.

V. Schramm, R. G. Silva, D. R. Kipp, 2012, Biochemistry.

Immucillins in Infectious Diseases.

G. Evans, V. Schramm, P. Tyler, 2017, ACS infectious diseases.

5.05 – Deamination of Nucleosides and Nucleotides and Related Reactions

V. Schramm, 1999 .

Molecular Electrostatic Potential Analysis for Enzymatic Substrates, Competitive Inhibitors, and Transition-State Inhibitors

Steven D. Schwartz, Carey K. Bagdassarian, V. Schramm, 1996 .

Catalytic and allosteric mechanism of AMP nucleosidase from primary, beta-secondary, and multiple heavy atom kinetic isotope effects.

V. Schramm, D. Parkin, 1987, Biochemistry.

Transition-state structures for N-glycoside hydrolysis of AMP by acid and by AMP nucleosidase in the presence and absence of allosteric activator.

V. Schramm, F. Mentch, D. Parkin, 1987, Biochemistry.

Protein Mass-Modulated Effects in Alkaline Phosphatase.

V. Schramm, Ananda K Ghosh, 2021, Biochemistry.

Transition state analogues in structures of ricin and saporin ribosome-inactivating proteins

V. Schramm, S. Almo, M. Ho, 2009, Proceedings of the National Academy of Sciences.

Isotope trapping and positional isotope exchange with rat and chicken liver phosphoenolpyruvate carboxykinases.

V. Schramm, Y. Sato, C. Y. Chen, 1991, Biochemistry.

Transition States and transition state analogue interactions with enzymes.

V. Schramm, 2015, Accounts of chemical research.

Amidrazone analogues of D-ribofuranose as transition-state inhibitors of nucleoside hydrolase.

B. Ganem, V. Schramm, B. Horenstein, 1994, Biochemistry.

Transition States, analogues, and drug development.

V. Schramm, Vern L Schramm, 2013, ACS chemical biology.

Electrophilic aromatic selenylation: new OPRT inhibitors.

V. Schramm, S. Knapp, M. Abdo, 2010, Organic letters.

5'-Deoxyadenosine contacts the substrate radical intermediate in the active site of ethanolamine ammonia-lyase: 2H and 13C electron nuclear double resonance studies.

G. H. Reed, O. Magnusson, V. Schramm, 2001, Biochemistry.

Catalytic-site design for inverse heavy-enzyme isotope effects in human purine nucleoside phosphorylase

V. Schramm, S. Schwartz, D. Antoniou, 2017, Proceedings of the National Academy of Sciences.

Triple Isotope Effects Support Concerted Hydride and Proton Transfer and Promoting Vibrations in Human Heart Lactate Dehydrogenase.

V. Schramm, Zhen Wang, Eric P. Chang, 2016, Journal of the American Chemical Society.

Modulating Enzyme Catalysis through Mutations Designed to Alter Rapid Protein Dynamics.

V. Schramm, S. Schwartz, D. Antoniou, 2016, Journal of the American Chemical Society.

Isotope-specific and amino acid-specific heavy atom substitutions alter barrier crossing in human purine nucleoside phosphorylase

V. Schramm, Javier Suárez, 2015, Proceedings of the National Academy of Sciences.

Protein Mass-Modulated Effects in the Catalytic Mechanism of Dihydrofolate Reductase: Beyond Promoting Vibrations

V. Schramm, Zhen Wang, A. Kohen, 2014, Journal of the American Chemical Society.

Mass-dependent bond vibrational dynamics influence catalysis by HIV-1 protease.

V. Schramm, R. G. Silva, D. R. Kipp, 2011, Journal of the American Chemical Society.

Acyclic phosph(on)ate inhibitors of Plasmodium falciparum hypoxanthine-guanine-xanthine phosphoribosyltransferase.

G. Evans, V. Schramm, P. Tyler, 2013, Bioorganic & medicinal chemistry.

Transition-state analysis of AMP deaminase.

V. Schramm, D. Merkler, P. Weiss, 1993, Biochemistry.

Loop-tryptophan human purine nucleoside phosphorylase reveals submillisecond protein dynamics.

V. Schramm, R. Callender, Mahmoud Ghanem, 2009, Biochemistry.

Crystal structure of formycin 5'-phosphate: an explanation for its tight binding to AMP nucleosidase.

H. Berman, V. Schramm, V. Giranda, 1988, Biochemistry.

Neighboring group participation in the transition state of human purine nucleoside phosphorylase.

A. S. Murkin, V. Schramm, S. Almo, 2007, Biochemistry.

Inhibition and Structure of Toxoplasma gondii Purine Nucleoside Phosphorylase

G. Evans, V. Schramm, P. Tyler, 2014, Eukaryotic Cell.

Plasmodium falciparum Purine Nucleoside Phosphorylase

G. Evans, R. Furneaux, V. Schramm, 2004, Journal of Biological Chemistry.

Transition State Analogue Inhibitors of Purine Nucleoside Phosphorylase from Plasmodium falciparum *

Kami Kim, G. Evans, R. Furneaux, 2002, The Journal of Biological Chemistry.

Structures of purine nucleoside phosphorylase from Mycobacterium tuberculosis in complexes with immucillin-H and its pieces.

R. Furneaux, V. Schramm, P. Tyler, 2001, Biochemistry.

Transition state analysis of the arsenolytic depyrimidination of thymidine by human thymidine phosphorylase.

V. Schramm, Phillip A. Schwartz, Mathew J. Vetticatt, 2011, Biochemistry.

Atomic motion in enzymatic reaction coordinates.

V. Schramm, W. Shi, 2001, Current opinion in structural biology.

Closed Site Complexes of Adenine Phosphoribosyltransferase fromGiardia lamblia Reveal a Mechanism of Ribosyl Migration*

Steven C Almo, V. Schramm, S. Almo, 2002, The Journal of Biological Chemistry.

Transition-state analysis of Trypanosoma cruzi uridine phosphorylase-catalyzed arsenolysis of uridine.

V. Schramm, M. Cassera, E. F. Merino, 2011, Journal of the American Chemical Society.

Transport of purines and purine salvage pathway inhibitors by the Plasmodium falciparum equilibrative nucleoside transporter PfENT1.

V. Schramm, Richard F. G. Fröhlich, M. Cassera, 2010, Molecular and biochemical parasitology.

Nucleoside Hydrolase from Leishmania major

V. Schramm, S. Almo, W. Shi, 1999, The Journal of Biological Chemistry.

The design of protozoan phosphoribosyltransferase inhibitors containing non-charged phosphate mimic residues.

V. Schramm, P. Tyler, W. Jiao, 2022, Bioorganic & medicinal chemistry.

Acyclic immucillin phosphonates: second-generation inhibitors of Plasmodium falciparum hypoxanthine-guanine-xanthine phosphoribosyltransferase.

V. Schramm, P. Tyler, S. Almo, 2012, Chemistry & biology.

Spontaneous epimerization of (S)-deoxycoformycin and interaction of (R)-deoxycoformycin, (S)-deoxycoformycin, and 8-ketodeoxycoformycin with adenosine deaminase.

V. Schramm, D. Baker, 1985, Biochemistry.

Transition state analysis for human and Plasmodium falciparum purine nucleoside phosphorylases.

V. Schramm, A. Lewandowicz, 2004, Biochemistry.

Binding causes the remote [5'-3H]thymidine kinetic isotope effect in human thymidine phosphorylase.

V. Schramm, M. Birck, 2004, Journal of the American Chemical Society.

Nucleophilic participation in the transition state for human thymidine phosphorylase.

V. Schramm, M. Birck, 2004, Journal of the American Chemical Society.

Transition state analogues for enzymes of nucleic acid metabolism.

V. Schramm, 2003, Nucleic acids research. Supplement.

Primate genome gain and loss: a bone dysplasia, muscular dystrophy, and bone cancer syndrome resulting from mutated retroviral-derived MTAP transcripts.

V. Schramm, S. Mehta, J. Martignetti, 2012, American journal of human genetics.

Enzymatic transition-state analysis and transition-state analogs.

V. Schramm, 1999, Methods in enzymology.

Enzymatic transition states and inhibitor design from principles of classical and quantum chemistry

V. Schramm, P. Berti, S. Schwartz, 1996 .

Genetic resistance to purine nucleoside phosphorylase inhibition in Plasmodium falciparum

V. Schramm, A. Fiser, J. Daily, 2018, Proceedings of the National Academy of Sciences.

A resistant mutant of Plasmodium falciparum purine nucleoside phosphorylase uses wild-type neighbors to maintain parasite survival

V. Schramm, R. Harijan, Y. V. Minnow, 2021, The Journal of biological chemistry.

Ricin A-chain: kinetics, mechanism, and RNA stem-loop inhibitors.

V. Schramm, T. Link, X. Chen, 1998, Biochemistry.

Detecting ricin: sensitive luminescent assay for ricin A-chain ribosome depurination kinetics.

V. Schramm, Matthew B. Sturm, 2009, Analytical chemistry.

Effect of dietary p-aminobenzoic acid on murine Plasmodium yoelii infection.

V. Schramm, G. Kicska, Kami Kim, 2003, The Journal of infectious diseases.

Soapwort Saporin L3 Expression in Yeast, Mutagenesis, and RNA Substrate Specificity.

V. Schramm, Hongling Yuan, Matthew B. Sturm, 2015, Biochemistry.

A Covalent Intermediate in CD38 Is Responsible for ADP-Ribosylation and Cyclization Reactions

R. Angeletti, V. Schramm, Haixin Deng, 2000 .

Enhanced Antibiotic Discovery by PROSPECTing.

V. Schramm, T. Meek, 2019, Biochemistry.

The catalytic site of AMP nucleosidase. Substrate specificity and pH effects with AMP and formycin 5'-PO4.

V. Schramm, W. deWolf, F. A. Fullin, 1979, The Journal of biological chemistry.

Characterization of AMD, the AMP deaminase gene in yeast. Production of amd strain, cloning, nucleotide sequence, and properties of the protein.

V. Schramm, S. Meyer, K. Kvalnes-Krick, 1989, Biochemistry.

AMP deaminase from yeast. Role in AMP degradation, large scale purification, and properties of the native and proteolyzed enzyme.

V. Schramm, J. Taylor, D. Merkler, 1989, The Journal of biological chemistry.

L-Enantiomers of transition state analogue inhibitors bound to human purine nucleoside phosphorylase.

G. Evans, R. Furneaux, A. S. Murkin, 2008, Journal of the American Chemical Society.

Erythrocytic Adenosine Monophosphate as an Alternative Purine Source in Plasmodium falciparum*

V. Schramm, M. Cassera, E. F. Merino, 2008, Journal of Biological Chemistry.

Kinetic Isotope Effects and Transition State Structure for Hypoxanthine-Guanine-Xanthine Phosphoribosyltransferase from Plasmodium falciparum.

V. Schramm, Ross S. Firestone, R. G. Ducati, 2017, Biochemistry.

Chemistry of gene silencing: the mechanism of NAD+-dependent deacetylation reactions.

J. Boeke, V. Schramm, J. Avalos, 2001, Biochemistry.

Mn 2 +-binding properties of a recombinant protein-tyrosine kinase derived from the human insulin receptor ( conformational change / secondary structure / electron a ge resonance / drcular dichroism )

V. Schramm, O. Rosen, S. Wente, 2022 .

Structural Insights into Intermediate Steps in the Sir 2 Deacetylation Reaction

V. Schramm, K. Hoff, C. Wolberger, 2022 .

Malaria parasite type 4 equilibrative nucleoside transporters (ENT4) are purine transporters with distinct substrate specificity.

V. Schramm, M. Cassera, E. F. Merino, 2012, The Biochemical journal.

Mechanism of 3-mercaptopicolinic acid inhibition of hepatic phosphoenolpyruvate carboxykinase (GTP).

V. Schramm, R. Hanson, V. Schramm, 1976, The Journal of biological chemistry.

Adenylate degradation in Escherichia coli. The role of AMP nucleosidase and properties of the purified enzyme.

V. Schramm, H. Leung, 1980, The Journal of biological chemistry.

The pathway of adenylate catabolism in Azotobacter vinelandii. Evidence for adenosine monophosphate nucleosidase as the regulatory enzyme.

V. Schramm, F. C. Lazorik, 1975, The Journal of biological chemistry.

Inhibition of ricin A-chain with pyrrolidine mimics of the oxacarbenium ion transition state.

G. Evans, R. Furneaux, V. Schramm, 2004, Biochemistry.

Structural analysis of adenine phosphoribosyltransferase from Saccharomyces cerevisiae.

V. Schramm, S. Almo, K. Tanaka, 2001, Biochemistry.

Picomolar transition state analogue inhibitors of human 5'-methylthioadenosine phosphorylase and X-ray structure with MT-immucillin-A.

G. Evans, R. Furneaux, V. Schramm, 2004, Biochemistry.

Methylthioinosine phosphorylase from Pseudomonas aeruginosa. Structure and annotation of a novel enzyme in quorum sensing.

V. Schramm, S. Almo, M. Ho, 2011, Biochemistry.

Chemical activation of Sir2-dependent silencing by relief of nicotinamide inhibition.

V. Schramm, I. Willis, R. Moir, 2005, Molecular cell.

Effects of allosteric activation on the primary and secondary kinetic isotope effects for three AMP nucleosidases.

V. Schramm, D. Parkin, 1984, The Journal of biological chemistry.

Incorporation of extracellular 8-oxodG into DNA and RNA requires purine nucleoside phosphorylase in MCF-7 cells

V. Schramm, S. Hah, P. Henderson, 2007, Nucleic acids research.

A high-affinity adenosine kinase from Anopheles gambiae.

V. Schramm, S. Almo, M. Cassera, 2011, Biochemistry.

Plasmodium falciparum Purine Nucleoside Phosphorylase Is Critical for Viability of Malaria Parasites*

V. Schramm, Kami Kim, L. Ting, 2008, Journal of Biological Chemistry.

Transition State Analysis of Adenosine Triphosphate Phosphoribosyltransferase.

V. Schramm, P. Tyler, E. Parker, 2017, ACS chemical biology.

Promoting Vibrations and the Function of Enzymes. Emerging Theoretical and Experimental Convergence.

V. Schramm, S. Schwartz, 2018, Biochemistry.

Mass Modulation of Protein Dynamics Associated with Barrier Crossing in Purine Nucleoside Phosphorylase.

V. Schramm, S. Schwartz, Xiaoxia Ge, 2012, The journal of physical chemistry letters.

Conformational dynamics in human purine nucleoside phosphorylase with reactants and transition-state analogues.

Karunesh Arora, V. Schramm, C. Brooks, 2010, The journal of physical chemistry. B.

Atomic detail of chemical transformation at the transition state of an enzymatic reaction

V. Schramm, S. Schwartz, Suwipa Saen-oon, 2008, Proceedings of the National Academy of Sciences.

Remote mutations and active site dynamics correlate with catalytic properties of purine nucleoside phosphorylase.

V. Schramm, S. Schwartz, Suwipa Saen-oon, 2008, Biophysical journal.

Promoting vibrations in human purine nucleoside phosphorylase. A molecular dynamics and hybrid quantum mechanical/molecular mechanical study.

V. Schramm, S. Schwartz, S. Núñez, 2004, Journal of the American Chemical Society.

Transition states of Plasmodium falciparum and human orotate phosphoribosyltransferases.

V. Schramm, M. Luo, Yong Zhang, 2009, Journal of the American Chemical Society.

Immucillins Impair Leishmania (L.) infantum chagasi and Leishmania (L.) amazonensis Multiplication In Vitro

G. Evans, V. Schramm, P. Tyler, 2015, PloS one.

Ricin A-chain activity on stem-loop and unstructured DNA substrates.

V. Schramm, Setu Roday, Tim K Amukele, 2005, Biochemistry.

The rate constant describing slow-onset inhibition of yeast AMP deaminase by coformycin analogues is independent of inhibitor structure.

V. Schramm, M. Brenowitz, D. Merkler, 1990, Biochemistry.

Subcellular location of phosphoenolpyruvate carboxykinase in hepatocytes from fed and starved rats.

V. Schramm, N. Cornell, F. Emig, 1986, The Journal of nutrition.

Enzymatic Transition State Theory and Transition State Analogue Design*

V. Schramm, 2007, Journal of Biological Chemistry.

Enzymatic transition states: thermodynamics, dynamics and analogue design.

V. Schramm, 2005, Archives of biochemistry and biophysics.

Transition states of native and drug-resistant HIV-1 protease are the same

V. Schramm, H. Goldstein, D. R. Kipp, 2012, Proceedings of the National Academy of Sciences.

Transition state variation in enzymatic reactions.

V. Schramm, 2001, Current opinion in chemical biology.

Remote mutations alter transition-state structure of human purine nucleoside phosphorylase.

V. Schramm, M. Luo, Lei Li, 2008, Biochemistry.

Catalytic site conformations in human PNP by 19F-NMR and crystallography.

V. Schramm, S. Almo, S. Cahill, 2013, Chemistry & biology.

Regulation of adenosine monophosphate levels as a function of adenosine triphosphate and inorganic phosphate. A proposed metabolic role for adenosine monophosphate nucleosidase from Azotobacter vinelandii.

V. Schramm, V. Schramm, H. Leung, 1973, The Journal of biological chemistry.

Purine and pyrimidine pathways as targets in Plasmodium falciparum.

V. Schramm, M. Cassera, María Belén Cassera, 2011, Current topics in medicinal chemistry.

Structural insights into intermediate steps in the Sir2 deacetylation reaction.

V. Schramm, K. Hoff, C. Wolberger, 2008, Structure.

Phosphoribosyltransferase mechanisms and roles in nucleic acid metabolism.

V. Schramm, C. Grubmeyer, 2004, Progress in nucleic acid research and molecular biology.

A phosphoenzyme mimic, overlapping catalytic sites and reaction coordinate motion for human NAMPT

V. Schramm, S. Almo, M. Ho, 2009, Proceedings of the National Academy of Sciences.

Structural and Biochemical Characterization of Chlamydia trachomatis Hypothetical Protein CT263 Supports That Menaquinone Synthesis Occurs through the Futalosine Pathway*

V. Schramm, K. Battaile, Hongling Yuan, 2014, The Journal of Biological Chemistry.

Pathway Menaquinone Synthesis Occurs through the Hypothetical Protein CT 263 Supports that Chlamydia trachomatis

V. Schramm, K. Battaile, Hongling Yuan, 2014 .

Plasmodium falciparum Parasites Are Killed by a Transition State Analogue of Purine Nucleoside Phosphorylase in a Primate Animal Model

G. Evans, A. S. Murkin, V. Schramm, 2011, PloS one.

Catalytic and regulatory site composition of yeast AMP deaminase by comparative binding and rate studies. Resolution of the cooperative mechanism.

V. Schramm, D. Merkler, V L Schramm, 1990, The Journal of biological chemistry.

Atomic dissection of the hydrogen bond network for transition-state analogue binding to purine nucleoside phosphorylase.

G. Evans, R. Furneaux, V. Schramm, 2002, Biochemistry.

Synthesis of nucleotides with specific radiolabels in ribose. Primary 14C and secondary 3H kinetic isotope effects on acid-catalyzed glycosidic bond hydrolysis of AMP, dAMP, and inosine.

V. Schramm, D. Parkin, H. Leung, 1984, The Journal of biological chemistry.

Yeast AMP deaminase. Catalytic activity in Schizosaccharomyces pombe and chromosomal location in Saccharomyces cerevisiae.

V. Schramm, D. Merkler, P. Sollitti, 1993, The Journal of biological chemistry.

Altered enthalpy-entropy compensation in picomolar transition state analogues of human purine nucleoside phosphorylase.

G. Evans, V. Schramm, P. Tyler, 2009, Biochemistry.

Determinants of sensitivity of human T-cell leukemia CCRF-CEM cells to immucillin-H.

V. Schramm, B. Mitchell, L. Graves, 2008, Leukemia research.

Purine nucleoside phosphorylase. Inosine hydrolysis, tight binding of the hypoxanthine intermediate, and third-the-sites reactivity.

V. Schramm, P. Kline, 1992, Biochemistry.

Comparison of initial velocity and binding data for allosteric adenosine monophosphate nucleosidase.

V. Schramm, 1976, The Journal of biological chemistry.

Phosphate activation in the ground state of purine nucleoside phosphorylase.

A. S. Murkin, V. Schramm, H. Deng, 2006, Journal of the American Chemical Society.

A beta-fluoroamine inhibitor of purine nucleoside phosphorylase.

A. S. Murkin, V. Schramm, Lei Li, 2008, Journal of medicinal chemistry.

Purine nucleoside phosphorylase from Mycobacterium tuberculosis. Analysis of inhibition by a transition-state analogue and dissection by parts.

R. Furneaux, V. Schramm, P. Tyler, 2001, Biochemistry.

Binding modes for substrate and a proposed transition-state analogue of protozoan nucleoside hydrolase.

V. Schramm, D. Parkin, 1995, Biochemistry.

A transition-state analogue reduces protein dynamics in hypoxanthine-guanine phosphoribosyltransferase.

R. Angeletti, V. Schramm, C. Grubmeyer, 2001, Biochemistry.

An enzyme-coupled microplate assay for activity and inhibition of hmdUMP hydrolysis by DNPH1.

V. Schramm, Andrew G. Wagner, Roozbeh Eskandari, 2023, Analytical biochemistry.

Human DNMT1 transition state structure

V. Schramm, Zhen Wang, Quan Du, 2016, Proceedings of the National Academy of Sciences.

A hypothesis to explain the substrate reactivity of ribosomal and stem-loop RNA with ricin A-chain.

V. Schramm, T. Link, X. Chen, 1996, Toxicon : official journal of the International Society on Toxinology.

Three-dimensional structure of the inosine-uridine nucleoside N-ribohydrolase from Crithidia fasciculata.

V. Schramm, J. Sacchettini, M. Degano, 1996, Biochemistry.

Molecular Cloning and Expression of a Purine-specific N-Ribohydrolase from Trypanosoma brucei brucei

V. Schramm, D. Parkin, R. Pelle, 1998, The Journal of Biological Chemistry.

Transition state analogues rescue ribosomes from saporin-L1 ribosome inactivating protein.

G. Evans, V. Schramm, P. Tyler, 2009, Biochemistry.

SIR2: the biochemical mechanism of NAD(+)-dependent protein deacetylation and ADP-ribosyl enzyme intermediates.

V. Schramm, A. Sauve, 2004, Current medicinal chemistry.

Active site contacts in the purine nucleoside phosphorylase--hypoxanthine complex by NMR and ab initio calculations.

Roger A. Jones, V. Schramm, S. Cahill, 2004, Biochemistry.

Methylthioadenosine deaminase in an alternative quorum sensing pathway in Pseudomonas aeruginosa.

V. Schramm, P. Tyler, S. Almo, 2012, Biochemistry.

The Immucillins: Design, Synthesis and Application of Transition- State Analogues.

G. Evans, V. Schramm, P. Tyler, 2015, Current medicinal chemistry.

Inhibition and structure of Trichomonas vaginalis purine nucleoside phosphorylase with picomolar transition state analogues.

G. Evans, R. Furneaux, V. Schramm, 2007, Biochemistry.

Structure and regulation of the AMP nucleosidase gene (amn) from Escherichia coli.

V. Schramm, S. Meyer, K. Kvalnes-Krick, 1989, Biochemistry.

Pre-steady-state transition-state analysis of the hydrolytic reaction catalyzed by purine nucleoside phosphorylase.

V. Schramm, P C Kline, V L Schramm, 1995, Biochemistry.

The structural gene for AMP nucleosidase. Mapping, cloning, and overproduction of the enzyme.

V. Schramm, H. Leung, 1984, The Journal of biological chemistry.

Transition-state analysis of a Vmax mutant of AMP nucleosidase by the application of heavy-atom kinetic isotope effects.

V. Schramm, F. Mentch, B. Horenstein, 1991, Biochemistry.

Ricin A-Chain: Kinetic Isotope Effects and Transition State Structure with Stem-Loop RNA†

V. Schramm, A. Berti, Xiangyang Chen, 2000 .

Targeting a Novel Plasmodium falciparum Purine Recycling Pathway with Specific Immucillins*

G. Evans, R. Furneaux, V. Schramm, 2005, Journal of Biological Chemistry.

Four generations of transition-state analogues for human purine nucleoside phosphorylase

Steven C. Almo, G. Evans, V. Schramm, 2010, Proceedings of the National Academy of Sciences.

Transition-State Analysis of 2-O-Acetyl-ADP-Ribose Hydrolysis by Human Macrodomain 1

V. Schramm, E. Burgos, Brett M. Hirsch, 2014, ACS chemical biology.

AMP nucleosidase: kinetic mechanism and thermodynamics.

V. Schramm, W. deWolf, F. Emig, 1986, Biochemistry.

Adenosine monophosphate nucleosidase from Azotobacter vinelandii and Escherichia coli.

V. Schramm, H. Leung, 1978, Methods in enzymology.

Inverse heavy enzyme isotope effects in methylthioadenosine nucleosidases

V. Schramm, S. Schwartz, D. Antoniou, 2021, Proceedings of the National Academy of Sciences.

Transition state analogue discrimination by related purine nucleoside phosphorylases.

G. Evans, R. Furneaux, A. S. Murkin, 2006, Journal of the American Chemical Society.

Ionic states of substrates and transition state analogues at the catalytic sites of N-ribosyltransferases.

G. Evans, R. Furneaux, V. Schramm, 2003, Biochemistry.

Femtomolar Transition State Analogue Inhibitors of 5′-Methylthioadenosine/S-Adenosylhomocysteine Nucleosidase from Escherichia coli*

G. Evans, R. Furneaux, V. Schramm, 2005, Journal of Biological Chemistry.

Kinetic Isotope Effects and Transition State Structure for Human Phenylethanolamine N-Methyltransferase.

Christopher F Stratton, V. Schramm, M. Poulin, 2017, ACS chemical biology.

Hydrolysis of soluble, linear, un-cross-linked peptidoglycans by endogenous bacterial N-acetylmuramoylhydrolases

V. Schramm, G. Shockman, J. Barrett, 1984, Journal of Bacteriology.

Conformational freedom in tight binding enzymatic transition-state analogues.

V. Schramm, S. Schwartz, Matthew W. Motley, 2013, The journal of physical chemistry. B.

MAT Gain of Activity Mutation in Helicobacter pylori Is Associated with Resistance to MTAN Transition State Analogues.

V. Schramm, A. Fiser, W. Jacobs, 2023, ACS infectious diseases.

The role of adenosine monophosphate nucleosidase in the regulation of adenine nucleotide levels in Azotobacter vinelandii during aerobic-anaerobic transitions.

V. Schramm, H. Leung, 1978, Archives of biochemistry and biophysics.

Residence Times for Femtomolar and Picomolar Inhibitors of MTANs.

V. Schramm, P. Tyler, Morais Brown, 2023, Biochemistry.

Targeting the polyamine pathway with transition-state analogue inhibitors of 5'-methylthioadenosine phosphorylase.

G. Evans, R. Furneaux, V. Schramm, 2004, Journal of medicinal chemistry.

Synthesis of a transition state analogue inhibitor of purine nucleoside phosphorylase via the Mannich reaction.

G. Evans, R. Furneaux, V. Schramm, 2003, Organic letters.

Acyclic ribooxacarbenium ion mimics as transition state analogues of human and malarial purine nucleoside phosphorylases.

G. Evans, V. Schramm, P. Tyler, 2007, Journal of the American Chemical Society.

Inactivation of chicken mitochondrial phosphoenolpyruvate carboxykinase by o-phthalaldehyde.

V. Schramm, D. Ash, F. Emig, 1991, The Journal of biological chemistry.

Anopheles gambiae purine nucleoside phosphorylase: catalysis, structure, and inhibition.

V. Schramm, S. Almo, E. Taylor, 2007, Biochemistry.

Quantum neural networks can predict binding free energies for enzymatic inhibitors

V. Schramm, S. Schwartz, B. B. Braunheim, 2000 .

Electrostatic potential surface analysis of the transition state for AMP nucleosidase and for formycin 5'-phosphate, a transition-state inhibitor.

V. Schramm, J. Ehrlich, 1994, Biochemistry.

Kinetic studies of the mechanism and allosteric activation of the reaction catalyzed by nucleoside diphosphatase.

V. Schramm, J. Morrison, 1969, Biochemistry.

Altered thermodynamics from remote mutations altering human toward bovine purine nucleoside phosphorylase.

V. Schramm, Lei Li, C. Wing, 2008, Biochemistry.

Second-sphere amino acids contribute to transition-state structure in bovine purine nucleoside phosphorylase.

V. Schramm, E. Taylor, M. Luo, 2008, Biochemistry.

Transition States

V. Schramm, 2009, The Journal of Biological Chemistry.

Transition state analogs enhanced by fragment-based structural analysis: Bacterial methylthioadenosine nucleosidases.

G. Evans, V. Schramm, P. Tyler, 2020, Biochemistry.

Transition state structure of the solvolytic hydrolysis of NAD

V. Schramm, P. Berti, Paul J. Berti, 1997 .

Transition State Structure for the Hydrolysis of NAD Catalyzed by Diphtheria Toxin.

V. Schramm, P. Berti, S. Blanke, 1997, Journal of the American Chemical Society.

Transition State Structure and Inhibition of Rv0091, a 5'-Deoxyadenosine/5'-methylthioadenosine Nucleosidase from Mycobacterium tuberculosis.

Christopher F Stratton, V. Schramm, Hilda A. Namanja-Magliano, 2016, ACS chemical biology.

Transport of purines and purine salvage pathway inhibitors by the Plasmodium falciparum equilibrative nucleoside transporter PfENT1.

V. Schramm, Richard F. G. Fröhlich, M. Cassera, 2010, Molecular and biochemical parasitology.

Enzymatic Transition States and Drug Design.

V. Schramm, 2018, Chemical reviews.

Immucillins in Infectious Diseases.

G. Evans, V. Schramm, P. Tyler, 2017, ACS infectious diseases.

Oligonucleotide transition state analogues of saporin L3.

G. Evans, V. Schramm, P. Tyler, 2017, European journal of medicinal chemistry.

Active site and remote contributions to catalysis in methylthioadenosine nucleosidases.

V. Schramm, S. Almo, S. Cameron, 2015, Biochemistry.

Distortional binding of transition state analogs to human purine nucleoside phosphorylase probed by magic angle spinning solid-state NMR

G. Evans, V. Schramm, Mathew J. Vetticatt, 2013, Proceedings of the National Academy of Sciences.

Conformational freedom in tight binding enzymatic transition-state analogues.

V. Schramm, S. Schwartz, Matthew W. Motley, 2013, The journal of physical chemistry. B.

A complex of methylthioadenosine/S-adenosylhomocysteine nucleosidase, transition state analogue, and nucleophilic water identified by mass spectrometry.

R. Angeletti, V. Schramm, Jihyeon Lim, 2012, Journal of the American Chemical Society.

Leaving group activation and pyrophosphate ionic state at the catalytic site of Plasmodium falciparum orotate phosphoribosyltransferase.

V. Schramm, H. Deng, Yong Zhang, 2010, Journal of the American Chemical Society.

Structural and metabolic specificity of methylthiocoformycin for malarial adenosine deaminases.

V. Schramm, P. Tyler, S. Almo, 2009, Biochemistry.

Transition Path Sampling Study of the Reaction Catalyzed by Purine Nucleoside Phosphorylase

V. Schramm, S. Schwartz, Suwipa Saen-oon, 2008, Zeitschrift fur physikalische Chemie.

Remote mutations alter transition-state structure of human purine nucleoside phosphorylase.

V. Schramm, M. Luo, Lei Li, 2008, Biochemistry.

Transition-state variation in human, bovine, and Plasmodium falciparum adenosine deaminases.

V. Schramm, E. Taylor, M. Luo, 2007, Journal of the American Chemical Society.

Transition-state analysis of S. pneumoniae 5'-methylthioadenosine nucleosidase.

V. Schramm, Vipender Singh, 2007, Journal of the American Chemical Society.

Transition-state analysis for depurination of DNA by Ricin A-chain

V. Schramm, A. Berti, Xiangyang Chen, 2000 .

Pertussis toxin: transition state analysis for ADP-ribosylation of G-protein peptide alphai3C20.

V. Schramm, J. Scheuring, 1997, Biochemistry.

Kinetic isotope effect characterization of the transition state for oxidized nicotinamide adenine dinucleotide hydrolysis by pertussis toxin.

V. Schramm, Johannes Scheuring, 1997, Biochemistry.

Trypanosomal nucleoside hydrolase. Resonance Raman spectroscopy of a transition-state inhibitor complex.

B. Ganem, V. Schramm, R. Callender, 1996, Biochemistry.

A kinetic isotope effect study and transition state analysis of the S-adenosylmethionine synthetase reaction.

V. Schramm, F. Mentch, G. D. Markham, 1987, The Journal of biological chemistry.

Kinetic properties of allosteric adenosine monophosphate nucleosidase from Azotobacter vinelandii.

V. Schramm, 1974, The Journal of biological chemistry.

Enzymatic transition states, transition-state analogs, dynamics, thermodynamics, and lifetimes.

V. Schramm, 2011, Annual review of biochemistry.

Transition-state interactions revealed in purine nucleoside phosphorylase by binding isotope effects.

A. S. Murkin, V. Schramm, P. Tyler, 2008, Journal of the American Chemical Society.

Conformational equilibrium isotope effects in glucose by (13)C NMR spectroscopy and computational studies.

V. Schramm, V. Schramm, B. E. Lewis, 2001, Journal of the American Chemical Society.

Ribocation transition state capture and rebound in human purine nucleoside phosphorylase.

A. S. Murkin, V. Schramm, Mahmoud Ghanem, 2009, Chemistry & biology.

Mutagenic analysis of AMP nucleosidase from Escherichia coli. Deletion of a region similar to AMP deaminase and peptide characterization by mass spectrometry.

V. Schramm, Xin Ma, E. Nieves, 1993, The Journal of biological chemistry.

Immucillins in custom catalytic-site cavities.

A. S. Murkin, V. Schramm, P. Tyler, 2008, Bioorganic & medicinal chemistry letters.

Over-the-barrier transition state analogues and crystal structure with Mycobacterium tuberculosis purine nucleoside phosphorylase.

G. Evans, R. Furneaux, V. Schramm, 2003, Biochemistry.

Design and Synthesis of D-Ribofuranoamidrazones as Inhibitors of Nucleoside Processing Enzymes

B. Ganem, V. Schramm, B. Horenstein, 1995 .

Exploring structure-activity relationships of transition state analogues of human purine nucleoside phosphorylase.

G. Evans, R. Furneaux, V. Schramm, 2003, Journal of medicinal chemistry.

Crystallization and preliminary X-ray study of AMP nucleosidase.

V. Schramm, Helen M. Berman, Vincent L. Giranda, 1986, The Journal of biological chemistry.

Uridine phosphorylase from Trypanosoma cruzi: kinetic and chemical mechanisms.

V. Schramm, R. G. Silva, 2011, Biochemistry.

Combined inhibition of MTAP and MAT2a mimics synthetic lethality in tumor models via PRMT5 inhibition

V. Schramm, L. Augenlicht, E. Tosti, 2023, The Journal of biological chemistry.