| Year |
Citation |
Score |
| 2022 |
Johnson CM, Fast W. On the kinetic mechanism of dimethylarginine dimethylaminohydrolase. Bioorganic & Medicinal Chemistry. 66: 116816. PMID 35598478 DOI: 10.1016/j.bmc.2022.116816 |
0.809 |
|
| 2022 |
Thomas PW, Cho EJ, Bethel CR, Smisek T, Ahn YC, Schroeder JM, Thomas CA, Dalby KN, Beckham JT, Crowder MW, Bonomo RA, Fast W. Discovery of an Effective Small-Molecule Allosteric Inhibitor of New Delhi Metallo-β-lactamase (NDM). Acs Infectious Diseases. PMID 35353502 DOI: 10.1021/acsinfecdis.1c00577 |
0.726 |
|
| 2021 |
Reidl CT, Mascarenhas R, Mohammad TSH, Lutz MR, Thomas PW, Fast W, Liu D, Becker DP. Cyclobutanone Inhibitor of Cobalt-Functionalized Metallo-γ-Lactonase AiiA with Cyclobutanone Ring Opening in the Active Site. Acs Omega. 6: 13567-13578. PMID 34095651 DOI: 10.1021/acsomega.0c06348 |
0.341 |
|
| 2021 |
Mehta R, Rivera DD, Reilley DJ, Tan D, Thomas PW, Hinojosa A, Stewart AC, Cheng Z, Thomas CA, Crowder MW, Alexandrova AN, Fast W, Que EL. Visualizing the Dynamic Metalation State of New Delhi Metallo-β-lactamase-1 in Bacteria Using a Reversible Fluorescent Probe. Journal of the American Chemical Society. PMID 34038127 DOI: 10.1021/jacs.1c00290 |
0.663 |
|
| 2021 |
Ahn YC, May VK, Bedford GC, Tuley AA, Fast W. Discovery of 4,4'-Dipyridylsulfide Analogs as "Switchable Electrophiles" for Covalent Inhibition. Acs Chemical Biology. PMID 33492128 DOI: 10.1021/acschembio.0c00890 |
0.809 |
|
| 2021 |
Cheng Z, Bethel CR, Thomas PW, Shurina BA, Alao JP, Thomas CA, Yang K, Zhang H, Sturgill AM, Kravats AN, Page RC, Fast W, Bonomo RA, Crowder MW. Carbapenem use is driving the evolution of IMiPenemase (IMP)-1 variants. Antimicrobial Agents and Chemotherapy. PMID 33468463 DOI: 10.1128/AAC.01714-20 |
0.521 |
|
| 2020 |
Mehaffey MR, Ahn YC, Rivera DD, Thomas PW, Cheng Z, Crowder MW, Pratt RF, Fast W, Brodbelt JS. Elusive structural changes of New Delhi metallo-β-lactamase revealed by ultraviolet photodissociation mass spectrometry. Chemical Science. 11: 8999-9010. PMID 34123154 DOI: 10.1039/d0sc02503h |
0.721 |
|
| 2020 |
Chen AY, Thomas C, Thomas PW, Yang K, Cheng Z, Fast W, Crowder MW, Cohen SM. Iminodiacetic Acid as a Novel Metal-binding Pharmacophore for New Delhi Metallo-β-lactamase Inhibitor Development . Chemmedchem. PMID 32315115 DOI: 10.1002/Cmdc.202000123 |
0.632 |
|
| 2020 |
Cheng Z, Thomas CA, Joyner AR, Kimble RL, Sturgill AM, Tran NY, Vulcan MR, Klinsky SA, Orea DJ, Platt CR, Cao F, Li B, Yang Q, Yurkiewicz CJ, Fast W, et al. MBLinhibitors.com, a Website Resource Offering Information and Expertise for the Continued Development of Metallo--Lactamase Inhibitors. Biomolecules. 10. PMID 32188106 DOI: 10.3390/biom10030459 |
0.566 |
|
| 2020 |
Mehaffey MR, Ahn Y-C, Rivera DD, Thomas PW, Cheng Z, Crowder MW, Pratt RF, Fast W, Brodbelt JS. Elusive structural changes of New Delhi metallo-β-lactamase revealed by ultraviolet photodissociation mass spectrometry Chemical Science. 11: 8999-9010. DOI: 10.1039/D0Sc02503H |
0.738 |
|
| 2019 |
Mehaffey MR, Schardon CL, Novelli ET, Cammarata MB, Webb LJ, Fast W, Brodbelt JS. Investigation of GTP-dependent dimerization of G12X K-Ras variants using ultraviolet photodissociation mass spectrometry. Chemical Science. 10: 8025-8034. PMID 31853358 DOI: 10.1039/C9Sc01032G |
0.776 |
|
| 2019 |
Cheng Z, Shurina BA, Bethel CR, Thomas PW, Marshall SH, Thomas CA, Yang K, Kimble RL, Montgomery JS, Orischak MG, Miller CM, Tennenbaum JL, Nix JC, Tierney DL, Fast W, et al. A Single Salt Bridge in VIM-20 Increases Protein Stability and Antibiotic Resistance under Low-Zinc Conditions. Mbio. 10. PMID 31744917 DOI: 10.1128/Mbio.02412-19 |
0.581 |
|
| 2019 |
Thomas PW, Cammarata MB, Brodbelt JS, Monzingo AF, Pratt RF, Fast W. A Lysine-Targeted Affinity Label for Serine β-Lactamase Also Covalently Modifies New Delhi Metallo-β-Lactamase-1 (NDM-1). Biochemistry. PMID 31145588 DOI: 10.1021/Acs.Biochem.9B00393 |
0.475 |
|
| 2019 |
Chen AY, Thomas PW, Cheng Z, Xu NY, Tierney DL, Crowder MW, Fast W, Cohen SM. Investigation of Dipicolinic Acid Isosteres for the Inhibition of Metallo-β-Lactamases. Chemmedchem. PMID 31124602 DOI: 10.1002/Cmdc.201900172 |
0.63 |
|
| 2019 |
Sen S, Mondal S, Zheng L, Salinger AJ, Fast W, Weerapana E, Thompson PR. Development of a Suicide Inhibition Based Protein Labeling (SIBLing) Strategy for Nicotinamide N-methyltransferase. Acs Chemical Biology. PMID 30933557 DOI: 10.1021/Acschembio.9B00211 |
0.442 |
|
| 2018 |
Chen AY, Thomas PW, Stewart AC, Bergstrom A, Cheng Z, Miller C, Bethel CR, Marshall SH, Credille CV, Riley CL, Page RC, Bonomo RA, Crowder MW, Tierney DL, Fast W, et al. Correction to Dipicolinic Acid Derivatives as Inhibitors of New Delhi Metallo-β-lactamase-1. Journal of Medicinal Chemistry. PMID 30019584 DOI: 10.1021/Acs.Jmedchem.8B01057 |
0.678 |
|
| 2018 |
Burstein-Teitelbaum G, Er J, Monzingo AF, Tuley A, Fast W. Dissection, Optimization and Structural Analysis of a Covalent Irreversible DDAH1 Inhibitor. Biochemistry. PMID 29983043 DOI: 10.1021/Acs.Biochem.8B00554 |
0.794 |
|
| 2018 |
Cheng Z, Thomas PW, Ju L, Bergstrom A, Mason K, Clayton D, Miller C, Bethel CR, VanPelt J, Tierney DL, Page RC, Bonomo RA, Fast W, Crowder MW. Evolution of New Delhi metallo-β-lactamase (NDM) in the clinic: effects of NDM mutations on stability, zinc affinity, mono-zinc activity. The Journal of Biological Chemistry. PMID 29909397 DOI: 10.1074/Jbc.Ra118.003835 |
0.628 |
|
| 2018 |
Tuley A, Fast W. The Taxonomy of Covalent Inhibitors. Biochemistry. PMID 29689165 DOI: 10.1021/Acs.Biochem.8B00315 |
0.816 |
|
| 2018 |
Ju LC, Cheng Z, Fast W, Bonomo RA, Crowder MW. The Continuing Challenge of Metallo-β-Lactamase Inhibition: Mechanism Matters. Trends in Pharmacological Sciences. PMID 29680579 DOI: 10.1016/J.Tips.2018.03.007 |
0.613 |
|
| 2017 |
Bergstrom A, Katko A, Adkins ZB, Hill JE, Cheng Z, Burnett ML, Yang H, Aitha M, Mehaffey MR, Brodbelt JS, Tehrani KHME, Martin NI, Bonomo RA, Page RC, Tierney DL, ... Fast W, et al. Probing the interaction of Aspergillomarasmine A (AMA) with metallo-β-lactamases NDM-1, VIM-2, and IMP-7. Acs Infectious Diseases. PMID 29091730 DOI: 10.1021/Acsinfecdis.7B00106 |
0.581 |
|
| 2017 |
Stweart AC, Bethel CR, VanPelt J, Bergstrom A, Cheng Z, Miller CG, Williams C, Poth R, Morris M, Lahey O, Nix JC, Tierney DL, Page RC, Crowder MW, Bonomo RA, ... Fast W, et al. Clinical Variants of New Delhi Metallo-β-Lactamase Are Evolving to Overcome Zinc Scarcity. Acs Infectious Diseases. PMID 28965402 DOI: 10.1021/Acsinfecdis.7B00128 |
0.569 |
|
| 2017 |
Chen AY, Thomas PW, Stewart AC, Bergstrom A, Cheng Z, Miller C, Bethel CR, Marshall SH, Credille CV, Riley CL, Page RC, Bonomo RA, Crowder MW, Tierney DL, Fast W, et al. Dipicolinic Acid Derivatives as Inhibitors of New Delhi Metallo-β-lactamase-1. Journal of Medicinal Chemistry. PMID 28809565 DOI: 10.1021/Acs.Jmedchem.7B00407 |
0.706 |
|
| 2017 |
Schardon C, Tuley A, Er J, Swartzel J, Fast W. Selective Covalent Protein Modification by 4-Halopyridines Through Catalysis. Chembiochem : a European Journal of Chemical Biology. PMID 28470883 DOI: 10.1002/Cbic.201700104 |
0.746 |
|
| 2017 |
Clevenger KD, Mascarenhas R, Catlin D, Wu R, Kelleher NL, Drake EJ, Gulick AM, Liu D, Fast W. Substrate Trapping in the Siderophore Tailoring Enzyme PvdQ. Acs Chemical Biology. PMID 28186406 DOI: 10.1021/Acschembio.7B00031 |
0.804 |
|
| 2016 |
Cammarata M, Schardon CL, Mehaffey MR, Rosenberg J, Singleton J, Fast W, Brodbelt JS. Impact of G12 Mutations on the Structure of K-Ras Probed by Ultraviolet Photodissociation Mass Spectrometry. Journal of the American Chemical Society. PMID 27665622 DOI: 10.1021/Jacs.6B04474 |
0.769 |
|
| 2016 |
Mojica MF, Bonomo RA, Fast W. B1-Metallo-β-Lactamases: Where Do We Stand? Current Drug Targets. 17: 1029-50. PMID 26424398 DOI: 10.2174/1389450116666151001105622 |
0.358 |
|
| 2015 |
Mascarenhas R, Thomas PW, Wu CX, Nocek BP, Hoang QQ, Liu D, Fast W. Structural and Biochemical Characterization of AidC, a Quorum-Quenching Lactonase With Atypical Selectivity. Biochemistry. PMID 26115006 DOI: 10.1021/Acs.Biochem.5B00499 |
0.656 |
|
| 2014 |
Thomas PW, Cammarata M, Brodbelt JS, Fast W. Covalent inhibition of New Delhi metallo-β-lactamase-1 (NDM-1) by cefaclor. Chembiochem : a European Journal of Chemical Biology. 15: 2541-8. PMID 25302694 DOI: 10.1002/Cbic.201402268 |
0.316 |
|
| 2014 |
Clevenger KD, Wu R, Liu D, Fast W. n-Alkylboronic acid inhibitors reveal determinants of ligand specificity in the quorum-quenching and siderophore biosynthetic enzyme PvdQ. Biochemistry. 53: 6679-86. PMID 25290020 DOI: 10.1021/Bi501086S |
0.82 |
|
| 2014 |
Wang Y, Hu S, Gabisi AM, Er JA, Pope A, Burstein G, Schardon CL, Cardounel AJ, Ekmekcioglu S, Fast W. Developing an irreversible inhibitor of human DDAH-1, an enzyme upregulated in melanoma. Chemmedchem. 9: 792-7. PMID 24574257 DOI: 10.1002/Cmdc.201300557 |
0.745 |
|
| 2013 |
Clevenger KD, Wu R, Er JA, Liu D, Fast W. Rational design of a transition state analogue with picomolar affinity for Pseudomonas aeruginosa PvdQ, a siderophore biosynthetic enzyme. Acs Chemical Biology. 8: 2192-200. PMID 23883096 DOI: 10.1021/Cb400345H |
0.79 |
|
| 2013 |
Thomas PW, Spicer T, Cammarata M, Brodbelt JS, Hodder P, Fast W. An altered zinc-binding site confers resistance to a covalent inactivator of New Delhi metallo-beta-lactamase-1 (NDM-1) discovered by high-throughput screening. Bioorganic & Medicinal Chemistry. 21: 3138-46. PMID 23591260 DOI: 10.1016/J.Bmc.2013.03.031 |
0.303 |
|
| 2013 |
Liu CF, Liu D, Momb J, Thomas PW, Lajoie A, Petsko GA, Fast W, Ringe D. A phenylalanine clamp controls substrate specificity in the quorum-quenching metallo-γ-lactonase from Bacillus thuringiensis Biochemistry. 52: 1603-1610. PMID 23387521 DOI: 10.1021/Bi400050J |
0.818 |
|
| 2012 |
Linsky TW, Fast W. Discovery of structurally-diverse inhibitor scaffolds by high-throughput screening of a fragment library with dimethylarginine dimethylaminohydrolase. Bioorganic & Medicinal Chemistry. 20: 5550-8. PMID 22921743 DOI: 10.1016/j.bmc.2012.07.022 |
0.818 |
|
| 2012 |
Clevenger KD, Fast W. "Clicking" on the lights to reveal bacterial social networking. Chembiochem : a European Journal of Chemical Biology. 13: 508-10. PMID 22262670 DOI: 10.1002/Cbic.201100767 |
0.762 |
|
| 2011 |
Thomas PW, Zheng M, Wu S, Guo H, Liu D, Xu D, Fast W. Characterization of purified New Delhi metallo-β-lactamase-1. Biochemistry. 50: 10102-13. PMID 22029287 DOI: 10.1021/Bi201449R |
0.614 |
|
| 2011 |
Linsky T, Wang Y, Fast W. Screening for dimethylarginine dimethylaminohydrolase inhibitors reveals ebselen as a bioavailable inactivator. Acs Medicinal Chemistry Letters. 2: 592-596. PMID 21927644 DOI: 10.1021/Ml2000824 |
0.804 |
|
| 2011 |
Linsky T, Fast W. A continuous, fluorescent, high-throughput assay for human dimethylarginine dimethylaminohydrolase-1. Journal of Biomolecular Screening. 16: 1089-97. PMID 21921133 DOI: 10.1177/1087057111417712 |
0.801 |
|
| 2011 |
Johnson CM, Monzingo AF, Ke Z, Yoon DW, Linsky TW, Guo H, Robertus JD, Fast W. On the mechanism of dimethylarginine dimethylaminohydrolase inactivation by 4-halopyridines. Journal of the American Chemical Society. 133: 10951-9. PMID 21630706 DOI: 10.1021/Ja2033684 |
0.808 |
|
| 2011 |
Guo Q, Bedford MT, Fast W. Discovery of peptidylarginine deiminase-4 substrates by protein array: antagonistic citrullination and methylation of human ribosomal protein S2. Molecular Biosystems. 7: 2286-95. PMID 21584310 DOI: 10.1039/C1Mb05089C |
0.583 |
|
| 2011 |
Guo Q, Fast W. Citrullination of inhibitor of growth 4 (ING4) by peptidylarginine deminase 4 (PAD4) disrupts the interaction between ING4 and p53. The Journal of Biological Chemistry. 286: 17069-78. PMID 21454715 DOI: 10.1074/Jbc.M111.230961 |
0.538 |
|
| 2011 |
Johnson CM, Linsky TW, Yoon DW, Person MD, Fast W. Discovery of halopyridines as quiescent affinity labels: inactivation of dimethylarginine dimethylaminohydrolase. Journal of the American Chemical Society. 133: 1553-62. PMID 21222447 DOI: 10.1021/Ja109207M |
0.805 |
|
| 2011 |
Thomas PW, Fast W. Heterologous overexpression, purification, and in vitro characterization of AHL lactonases. Methods in Molecular Biology (Clifton, N.J.). 692: 275-90. PMID 21031319 DOI: 10.1007/978-1-60761-971-0_20 |
0.364 |
|
| 2011 |
Lluis M, Wang Y, Monzingo AF, Fast W, Robertus JD. Characterization of C-alkyl amidines as bioavailable covalent reversible inhibitors of human DDAH-1. Chemmedchem. 6: 81-8. PMID 20979083 DOI: 10.1002/Cmdc.201000392 |
0.502 |
|
| 2010 |
Linsky T, Fast W. Mechanistic similarity and diversity among the guanidine-modifying members of the pentein superfamily. Biochimica Et Biophysica Acta. 1804: 1943-53. PMID 20654741 DOI: 10.1016/J.Bbapap.2010.07.016 |
0.814 |
|
| 2010 |
Momb J, Yoon DW, Fast W. Enzymic disruption of N-aroyl-L-homoserine lactone-based quorum sensing. Chembiochem : a European Journal of Chemical Biology. 11: 1535-7. PMID 20544776 DOI: 10.1002/Cbic.201000191 |
0.795 |
|
| 2010 |
Lluis M, Wang Y, Monzingo AF, Fast W, Robertus JD. Cover Picture: Characterization of C-Alkyl Amidines as Bioavailable Covalent Reversible Inhibitors of Human DDAH-1 (ChemMedChem 1/2011) Chemmedchem. 6: 1-1. DOI: 10.1002/Cmdc.201090059 |
0.402 |
|
| 2010 |
Momb J, Yoon D, Fast W. Inside Cover: Enzymic Disruption of N-Aroyl-L-homoserine Lactone-Based Quorum Sensing (ChemBioChem 11/2010) Chembiochem. 11: 1474-1474. DOI: 10.1002/Cbic.201090049 |
0.795 |
|
| 2009 |
Wang Y, Hu S, Fast W. A click chemistry mediated in vivo activity probe for dimethylarginine dimethylaminohydrolase. Journal of the American Chemical Society. 131: 15096-7. PMID 19919155 DOI: 10.1021/Ja906432E |
0.524 |
|
| 2009 |
Limphong P, Nimako G, Thomas PW, Fast W, Makaroff CA, Crowder MW. Arabidopsis thaliana mitochondrial glyoxalase 2-1 exhibits β-lactamase activity Biochemistry. 48: 8491-8493. PMID 19735113 DOI: 10.1021/Bi9010539 |
0.534 |
|
| 2009 |
Wang Y, Monzingo AF, Hu S, Schaller TH, Robertus JD, Fast W. Developing dual and specific inhibitors of dimethylarginine dimethylaminohydrolase-1 and nitric oxide synthase: toward a targeted polypharmacology to control nitric oxide. Biochemistry. 48: 8624-35. PMID 19663506 DOI: 10.1021/Bi9007098 |
0.424 |
|
| 2009 |
Li H, Fast W, Benkovic SJ. Structural and functional modularity of proteins in the de novo purine biosynthetic pathway. Protein Science : a Publication of the Protein Society. 18: 881-92. PMID 19384989 DOI: 10.1002/Pro.95 |
0.453 |
|
| 2008 |
Momb J, Wang C, Liu D, Thomas PW, Petsko GA, Guo H, Ringe D, Fast W. Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 2. Substrate modeling and active site mutations. Biochemistry. 47: 7715-25. PMID 18627130 DOI: 10.1021/Bi8003704 |
0.814 |
|
| 2008 |
Liu D, Momb J, Thomas PW, Moulin A, Petsko GA, Fast W, Ringe D. Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures. Biochemistry. 47: 7706-14. PMID 18627129 DOI: 10.1021/Bi800368Y |
0.815 |
|
| 2008 |
Linsky TW, Monzingo AF, Stone EM, Robertus JD, Fast W. Promiscuous partitioning of a covalent intermediate common in the pentein superfamily. Chemistry & Biology. 15: 467-75. PMID 18482699 DOI: 10.1016/J.Chembiol.2008.03.012 |
0.804 |
|
| 2007 |
Liu D, Thomas PW, Momb J, Hoang QQ, Petsko GA, Ringe D, Fast W. Structure and specificity of a quorum-quenching lactonase (AiiB) from Agrobacterium tumefaciens. Biochemistry. 46: 11789-99. PMID 17900178 DOI: 10.1021/Bi7012849 |
0.823 |
|
| 2007 |
Hong L, Fast W. Inhibition of human dimethylarginine dimethylaminohydrolase-1 by S-nitroso-L-homocysteine and hydrogen peroxide. Analysis, quantification, and implications for hyperhomocysteinemia. The Journal of Biological Chemistry. 282: 34684-92. PMID 17895252 DOI: 10.1074/Jbc.M707231200 |
0.675 |
|
| 2006 |
Momb J, Thomas PW, Breece RM, Tierney DL, Fast W. The quorum-quenching metallo-gamma-lactonase from Bacillus thuringiensis exhibits a leaving group thio effect. Biochemistry. 45: 13385-93. PMID 17073460 DOI: 10.1021/Bi061238O |
0.8 |
|
| 2006 |
Stone EM, Costello AL, Tierney DL, Fast W. Substrate-assisted cysteine deprotonation in the mechanism of dimethylargininase (DDAH) from Pseudomonas aeruginosa. Biochemistry. 45: 5618-30. PMID 16634643 DOI: 10.1021/Bi052595M |
0.734 |
|
| 2005 |
Stone EM, Schaller TH, Bianchi H, Person MD, Fast W. Inactivation of two diverse enzymes in the amidinotransferase superfamily by 2-chloroacetamidine: dimethylargininase and peptidylarginine deiminase. Biochemistry. 44: 13744-52. PMID 16229464 DOI: 10.1021/Bi051341Y |
0.745 |
|
| 2005 |
Liu D, Lepore BW, Petsko GA, Thomas PW, Stone EM, Fast W, Ringe D. Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis. Proceedings of the National Academy of Sciences of the United States of America. 102: 11882-7. PMID 16087890 DOI: 10.1073/Pnas.0505255102 |
0.769 |
|
| 2005 |
Stone EM, Fast W. A continuous spectrophotometric assay for dimethylarginine dimethylaminohydrolase. Analytical Biochemistry. 343: 335-7. PMID 15992759 DOI: 10.1016/J.Ab.2005.05.006 |
0.587 |
|
| 2005 |
Thomas PW, Stone EM, Costello AL, Tierney DL, Fast W. The quorum-quenching lactonase from Bacillus thuringiensis is a metalloprotein. Biochemistry. 44: 7559-69. PMID 15895999 DOI: 10.1021/Bi050050M |
0.654 |
|
| 2005 |
Stone EM, Person MD, Costello NJ, Fast W. Characterization of a transient covalent adduct formed during dimethylarginine dimethylaminohydrolase catalysis. Biochemistry. 44: 7069-78. PMID 15865451 DOI: 10.1021/Bi047407R |
0.719 |
|
| 2003 |
Huntley JJ, Fast W, Benkovic SJ, Wright PE, Dyson HJ. Role of a solvent-exposed tryptophan in the recognition and binding of antibiotic substrates for a metallo-beta-lactamase. Protein Science : a Publication of the Protein Society. 12: 1368-75. PMID 12824483 DOI: 10.1110/Ps.0305303 |
0.468 |
|
| 2002 |
Lutz S, Fast W, Benkovic SJ. A universal, vector-based system for nucleic acid reading-frame selection. Protein Engineering. 15: 1025-30. PMID 12601143 DOI: 10.1093/Protein/15.12.1025 |
0.622 |
|
| 2001 |
Fast W, Wang Z, Benkovic SJ. Familial mutations and zinc stoichiometry determine the rate-limiting step of nitrocefin hydrolysis by metallo-β-lactamase from Bacteroides fragilis Biochemistry. 40: 1640-1650. PMID 11327823 DOI: 10.1021/Bi001860V |
0.524 |
|
| 1999 |
Wang Z, Fast W, Valentine AM, Benkovic SJ. Metallo-beta-lactamase: structure and mechanism. Current Opinion in Chemical Biology. 3: 614-22. PMID 10508665 DOI: 10.1016/S1367-5931(99)00017-4 |
0.691 |
|
| 1999 |
Wang Z, Fast W, Benkovic SJ. On the mechanism of the metallo-beta-lactamase from Bacteroides fragilis. Biochemistry. 38: 10013-23. PMID 10433708 DOI: 10.1021/Bi990356R |
0.542 |
|
| 1999 |
Fast W, Nikolic D, Van Breemen RB, Silverman RB. Mechanistic studies of the inactivation of inducible nitric oxide synthase by N5-(1-iminoethyl)-L-ornithine (L-NIO) Journal of the American Chemical Society. 121: 903-916. DOI: 10.1021/Ja982318L |
0.509 |
|
| 1998 |
Wang Z, Fast W, Benkovic SJ. Direct Observation of an Enzyme-Bound Intermediate in the Catalytic Cycle of the Metallo-β-Lactamase fromBacteroides fragilis Journal of the American Chemical Society. 120: 10788-10789. DOI: 10.1021/Ja982621M |
0.526 |
|
| 1997 |
Zhang HQ, Fast W, Marletta MA, Martasek P, Silverman RB. Potent and selective inhibition of neuronal nitric oxide synthase by N omega-propyl-L-arginine. Journal of Medicinal Chemistry. 40: 3869-70. PMID 9397167 DOI: 10.1021/Jm970550G |
0.465 |
|
| 1997 |
Fast W, Levsky ME, Marletta MA, Silverman RB. N omega-propargyl-L-arginine and N omega-hydroxy-N omega-propargyl-L-arginine are inhibitors, but not inactivators, of neuronal and macrophage nitric oxide synthases. Bioorganic & Medicinal Chemistry. 5: 1601-8. PMID 9313865 DOI: 10.1016/S0968-0896(97)00109-0 |
0.514 |
|
| 1997 |
Fast W, Huff ME, Silverman RB. Time-dependent inhibition of neuronal nitric oxide synthase by N-propargylguanidine Bioorganic and Medicinal Chemistry Letters. 7: 1449-1454. DOI: 10.1016/S0960-894X(97)00241-2 |
0.519 |
|
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