| Year |
Citation |
Score |
| 2023 |
Thomas CA, Cheng Z, Bethel CR, Hujer AM, Sturgill AM, Onuoha K, Page RC, Bonomo RA, Crowder MW. The directed evolution of NDM-1. Antimicrobial Agents and Chemotherapy. e0071423. PMID 37874296 DOI: 10.1128/aac.00714-23 |
0.716 |
|
| 2022 |
Legru A, Verdirosa F, Vo-Hoang Y, Tassone G, Vascon F, Thomas CA, Sannio F, Corsica G, Benvenuti M, Feller G, Coulon R, Marcoccia F, Devente SR, Bouajila E, Piveteau C, ... ... Crowder MW, et al. Optimization of 1,2,4-Triazole-3-thiones toward Broad-Spectrum Metallo-β-lactamase Inhibitors Showing Potent Synergistic Activity on VIM- and NDM-1-Producing Clinical Isolates. Journal of Medicinal Chemistry. PMID 36450011 DOI: 10.1021/acs.jmedchem.2c01257 |
0.301 |
|
| 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 |
0.644 |
|
| 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 |
0.798 |
|
| 2021 |
Zhang H, Yang K, Cheng Z, Thomas C, Steinbrunner A, Pryor C, Vulcan M, Kemp C, Orea D, Paththamperuma C, Chen AY, Cohen SM, Page RC, Tierney DL, Crowder MW. Spectroscopic and biochemical characterization of metallo-β-lactamase IMP-1 with dicarboxylic, sulfonyl, and thiol inhibitors. Bioorganic & Medicinal Chemistry. 40: 116183. PMID 33965839 DOI: 10.1016/j.bmc.2021.116183 |
0.815 |
|
| 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 |
0.777 |
|
| 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 |
0.803 |
|
| 2020 |
Thomas CA, Cheng Z, Yang K, Hellwarth E, Yurkiewicz CJ, Baxter FM, Fullington SA, Klinsky SA, Otto JL, Chen AY, Cohen SM, Crowder MW. Probing the mechanisms of inhibition for various inhibitors of metallo-β-lactamases VIM-2 and NDM-1. Journal of Inorganic Biochemistry. 210: 111123. PMID 32622213 DOI: 10.1016/J.Jinorgbio.2020.111123 |
0.754 |
|
| 2020 |
Fullington S, Cheng Z, Thomas C, Miller C, Yang K, Ju LC, Bergstrom A, Shurina BA, Bretz SL, Page RC, Tierney DL, Crowder MW. An integrated biophysical approach to discovering mechanisms of NDM-1 inhibition for several thiol-containing drugs. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 32500360 DOI: 10.1007/S00775-020-01794-Z |
0.802 |
|
| 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 |
0.815 |
|
| 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, ... Crowder MW, 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 |
0.776 |
|
| 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 |
0.811 |
|
| 2020 |
Yang K, Somogyi A, Thomas C, Zhang H, Cheng Z, Xu S, Miller C, Spivey D, Blake C, Smith C, Dafoe D, Danielson ND, Crowder MW. Analysis of Barrel-Aged Kentucky Bourbon Whiskey by Ultrahigh Resolution Mass Spectrometry Food Analytical Methods. DOI: 10.1007/S12161-020-01850-Z |
0.655 |
|
| 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, ... ... Crowder MW, 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 |
0.797 |
|
| 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 |
0.825 |
|
| 2019 |
Montgomery J, Orischak M, Morris M, Shurina BA, Cheng Z, Bethel C, Fast W, Bonomo R, Nix J, Crowder M, Page RC. Probing the thermal stability and X-ray crystal structures of select members of the Verona integron-encoded metallo-β-lactamase 2 family Acta Crystallographica Section a Foundations and Advances. 75: a436-a436. DOI: 10.1107/S0108767319095758 |
0.682 |
|
| 2018 |
Cheng Z, VanPelt J, Bergstrom A, Bethel C, Katko A, Miller C, Mason K, Cumming E, Zhang H, Kimble R, Fullington S, Bretz SL, Nix JC, Bonomo RA, Tierney D, ... ... Crowder MW, et al. A non-canonical metal center drives activity of the Sediminispirochaeta smaragdinae metallo-β-lactamase SPS-1. Biochemistry. PMID 30106565 DOI: 10.1021/Acs.Biochem.8B00728 |
0.821 |
|
| 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 |
0.788 |
|
| 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 |
0.816 |
|
| 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 |
0.809 |
|
| 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, ... ... Crowder MW, 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 |
0.83 |
|
| 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, 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 |
0.823 |
|
| 2017 |
Lisa MN, Palacios AR, Aitha M, González MM, Moreno DM, Crowder MW, Bonomo RA, Spencer J, Tierney DL, Llarrull LI, Vila AJ. A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases. Nature Communications. 8: 538. PMID 28912448 DOI: 10.1038/S41467-017-00601-9 |
0.677 |
|
| 2017 |
Craig WR, Baker TW, Marts AR, DeGenova DT, Martin DP, Reed GC, McCarrick RM, Crowder MW, Cohen SM, Tierney DL. Substituent Effects on the Coordination Chemistry of Metal-Binding Pharmacophores. Inorganic Chemistry. PMID 28898098 DOI: 10.1021/Acs.Inorgchem.7B01661 |
0.628 |
|
| 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 |
0.825 |
|
| 2017 |
Muthyala R, Shin WS, Sham YY, Bergstrom A, Crowder MW, Bonomo RA. Discovery of 1-hydroxypyridine-2(1H)-thione-6-carboxylic acid as a first-in-class low-cytotoxic nanomolar metallo -lactamase inhibitor. Chemmedchem. PMID 28482143 DOI: 10.1002/Cmdc.201700182 |
0.371 |
|
| 2016 |
Meng F, Yang H, Jack C, Zhang H, Moller A, Spivey D, Page RC, Tierney DL, Crowder MW. Biochemical characterization and zinc binding group (ZBGs) inhibition studies on the catalytic domain of MMP7 (cdMMP7). Journal of Inorganic Biochemistry. 165: 7-17. PMID 27755977 DOI: 10.1016/J.Jinorgbio.2016.10.005 |
0.653 |
|
| 2016 |
Meng F, Yang H, Aitha M, George S, Tierney DL, Crowder MW. Biochemical and spectroscopic characterization of the catalytic domain of MMP16 (cdMMP16). Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. PMID 27229514 DOI: 10.1007/S00775-016-1362-Y |
0.59 |
|
| 2016 |
Aitha M, Al-Adbul-Wahid S, Tierney DL, Crowder MW. Probing substrate binding to the metal binding sites in metallo-β-lactamase L1 during catalysis. Medchemcomm. 7: 194-201. PMID 27087914 DOI: 10.1039/C5Md00358J |
0.678 |
|
| 2016 |
Aitha M, Al-Abdul-Wahid S, Tierney DL, Crowder MW. Correction: Probing substrate binding to the metal binding sites in metallo-β-lactamase L1 during catalysis Medchemcomm. 7: 734-734. DOI: 10.1039/C6Md90019D |
0.663 |
|
| 2016 |
Aitha M, Al-Adbul-Wahid S, Tierney DL, Crowder MW. Probing substrate binding to the metal binding sites in metallo-β-lactamase L1 during catalysis Medchemcomm. 7: 194-201. DOI: 10.1039/c5md00358j |
0.628 |
|
| 2015 |
Aitha M, Moller AJ, Sahu ID, Horitani M, Tierney DL, Crowder MW. Investigating the position of the hairpin loop in New Delhi metallo-β-lactamase, NDM-1, during catalysis and inhibitor binding. Journal of Inorganic Biochemistry. 156: 35-39. PMID 26717260 DOI: 10.1016/J.Jinorgbio.2015.10.011 |
0.621 |
|
| 2015 |
Yang H, Makaroff K, Paz N, Aitha M, Crowder MW, Tierney DL. Metal Ion Dependence of the Matrix Metalloproteinase-1 Mechanism. Biochemistry. 54: 3631-9. PMID 26018933 DOI: 10.1021/Acs.Biochem.5B00379 |
0.648 |
|
| 2015 |
Oelschlaeger P, Aitha M, Yang H, Kang JS, Zhang AL, Liu EM, Buynak JD, Crowder MW. Meropenem and Chromacef Intermediates Observed in IMP-25 Metallo-β-Lactamase-Catalyzed Hydrolysis. Antimicrobial Agents and Chemotherapy. 59: 4326-30. PMID 25918145 DOI: 10.1128/Aac.04409-14 |
0.419 |
|
| 2015 |
Aitha M, Moritz L, Sahu ID, Sanyurah O, Roche Z, McCarrick R, Lorigan GA, Bennett B, Crowder MW. Conformational dynamics of metallo-β-lactamase CcrA during catalysis investigated by using DEER spectroscopy. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 20: 585-94. PMID 25827593 DOI: 10.1007/S00775-015-1244-8 |
0.329 |
|
| 2014 |
Aitha M, Marts AR, Bergstrom A, Møller AJ, Moritz L, Turner L, Nix JC, Bonomo RA, Page RC, Tierney DL, Crowder MW. Biochemical, mechanistic, and spectroscopic characterization of metallo-β-lactamase VIM-2. Biochemistry. 53: 7321-31. PMID 25356958 DOI: 10.1021/Bi500916Y |
0.716 |
|
| 2014 |
Yang H, Young H, Yu S, Sutton L, Crowder MW. Targeting metallo-carbapenemases via modulation of electronic properties of cephalosporins. The Biochemical Journal. 464: 271-9. PMID 25220027 DOI: 10.1042/Bj20140364 |
0.376 |
|
| 2014 |
Zhang YL, Yang KW, Zhou YJ, LaCuran AE, Oelschlaeger P, Crowder MW. Diaryl-substituted azolylthioacetamides: Inhibitor discovery of New Delhi metallo-β-lactamase-1 (NDM-1) Chemmedchem. 9: 2445-2448. PMID 25048031 DOI: 10.1002/Cmdc.201402249 |
0.452 |
|
| 2014 |
Yang H, Aitha M, Marts AR, Hetrick A, Bennett B, Crowder MW, Tierney DL. Spectroscopic and mechanistic studies of heterodimetallic forms of metallo-β-lactamase NDM-1. Journal of the American Chemical Society. 136: 7273-85. PMID 24754678 DOI: 10.1021/Ja410376S |
0.68 |
|
| 2014 |
Aitha M, Richmond TK, Hu Z, Hetrick A, Reese R, Gunther A, McCarrick R, Bennett B, Crowder MW. Dilution of dipolar interactions in a spin-labeled, multimeric metalloenzyme for DEER studies. Journal of Inorganic Biochemistry. 136: 40-6. PMID 24742748 DOI: 10.1016/J.Jinorgbio.2014.03.010 |
0.318 |
|
| 2013 |
Yang KW, Feng L, Yang SK, Aitha M, Lacuran AE, Oelschlaeger P, Crowder MW. New β-phospholactam as a carbapenem transition state analog: Synthesis of a broad-spectrum inhibitor of metallo-β-lactamases Bioorganic and Medicinal Chemistry Letters. 23: 5855-5859. PMID 24064498 DOI: 10.1016/J.Bmcl.2013.08.098 |
0.425 |
|
| 2013 |
Zhang YL, Xiao JM, Feng JL, Yang KW, Feng L, Zhou LS, Crowder MW. A novel fluorogenic substrate for dinuclear Zn(II)-containing metallo-β-lactamases Bioorganic and Medicinal Chemistry Letters. 23: 1676-1679. PMID 23411077 DOI: 10.1016/J.Bmcl.2013.01.071 |
0.361 |
|
| 2013 |
Heidari Torkabadi H, Che T, Shou J, Shanmugam S, Crowder MW, Bonomo RA, Pusztai-Carey M, Carey PR. Raman spectra of interchanging β-lactamase inhibitor intermediates on the millisecond time scale Journal of the American Chemical Society. 135: 2895-2898. PMID 23406484 DOI: 10.1021/Ja311440P |
0.348 |
|
| 2013 |
Zhang Y, Xiao J, Feng J, Yang K, Feng L, Zhou L, Crowder MW. Corrigendum to “A novel fluorogenic substrate for dinuclear Zn(II)-containing metallo-β-lactamases” [Bioorg. Med. Chem. Lett. 23 (2013) 1676–1679] Bioorganic & Medicinal Chemistry Letters. 23: 2813. DOI: 10.1016/J.Bmcl.2013.03.001 |
0.443 |
|
| 2012 |
Feng L, Yang KW, Zhou LS, Xiao JM, Yang X, Zhai L, Zhang YL, Crowder MW. N-Heterocyclic dicarboxylic acids: Broad-spectrum inhibitors of metallo-β-lactamases with co-antibacterial effect against antibiotic-resistant bacteria Bioorganic and Medicinal Chemistry Letters. 22: 5185-5189. PMID 22796180 DOI: 10.1016/J.Bmcl.2012.06.074 |
0.38 |
|
| 2012 |
Yang H, Aitha M, Hetrick AM, Richmond TK, Tierney DL, Crowder MW. Mechanistic and spectroscopic studies of metallo-β-lactamase NDM-1. Biochemistry. 51: 3839-47. PMID 22482529 DOI: 10.1021/Bi300056Y |
0.701 |
|
| 2012 |
Hensley MP, Gunasekera TS, Easton JA, Sigdel TK, Sugarbaker SA, Klingbeil L, Breece RM, Tierney DL, Crowder MW. Characterization of Zn(II)-responsive ribosomal proteins YkgM and L31 in E. coli. Journal of Inorganic Biochemistry. 111: 164-72. PMID 22196016 DOI: 10.1016/J.Jinorgbio.2011.11.022 |
0.816 |
|
| 2011 |
Hensley MP, Tierney DL, Crowder MW. Zn(II) binding to Escherichia coli 70S ribosomes. Biochemistry. 50: 9937-9. PMID 22026583 DOI: 10.1021/Bi200619W |
0.667 |
|
| 2011 |
Griffin DH, Richmond TK, Sanchez C, Moller AJ, Breece RM, Tierney DL, Bennett B, Crowder MW. Structural and kinetic studies on metallo-β-lactamase IMP-1. Biochemistry. 50: 9125-34. PMID 21928807 DOI: 10.1021/Bi200839H |
0.833 |
|
| 2011 |
Linenberger K, Bretz SL, Crowder MW, McCarrick R, Lorigan GA, Tierney DL. What is the true color of fresh meat? A biophysical undergraduate laboratory experiment investigating the effects of ligand binding on myoglobin using optical, EPR, and NMR spectroscopy Journal of Chemical Education. 88: 223-225. DOI: 10.1021/Ed100585T |
0.559 |
|
| 2010 |
Limphong P, Adams NE, Rouhier MF, McKinney RM, Naylor M, Bennett B, Makaroff CA, Crowder MW. Converting GLX2-1 into an active glyoxalase II. Biochemistry. 49: 8228-36. PMID 20715794 DOI: 10.1021/Bi1010865 |
0.488 |
|
| 2010 |
Limphong P, McKinney RM, Adams NE, Makaroff CA, Bennett B, Crowder MW. The metal ion requirements of Arabidopsis thaliana Glx2-2 for catalytic activity Journal of Biological Inorganic Chemistry. 15: 249-258. PMID 19834746 DOI: 10.1007/S00775-009-0593-6 |
0.419 |
|
| 2009 |
Gunasekera TS, Herre AH, Crowder MW. Absence of ZnuABC-mediated zinc uptake affects virulence-associated phenotypes of uropathogenic Escherichia coli CFT073 under Zn(II)-depleted conditions Fems Microbiology Letters. 300: 36-41. PMID 19765083 DOI: 10.1111/J.1574-6968.2009.01762.X |
0.383 |
|
| 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 |
0.636 |
|
| 2009 |
Breece RM, Hu Z, Bennett B, Crowder MW, Tierney DL. Motion of the zinc ions in catalysis by a dizinc metallo-beta-lactamase. Journal of the American Chemical Society. 131: 11642-3. PMID 19653676 DOI: 10.1021/Ja902534B |
0.81 |
|
| 2009 |
Hawk MJ, Breece RM, Hajdin CE, Bender KM, Hu Z, Costello AL, Bennett B, Tierney DL, Crowder MW. Differential binding of Co(II) and Zn(II) to metallo-beta-lactamase Bla2 from Bacillus anthracis. Journal of the American Chemical Society. 131: 10753-62. PMID 19588962 DOI: 10.1021/Ja900296U |
0.832 |
|
| 2009 |
Limphong P, McKinney RM, Adams NE, Bennett B, Makaroff CA, Gunasekera T, Crowder MW. Human glyoxalase II contains an Fe(II)Zn(II) center but is active as a mononuclear Zn(II) enzyme Biochemistry. 48: 5426-5434. PMID 19413286 DOI: 10.1021/Bi9001375 |
0.466 |
|
| 2009 |
Hu Z, Spadafora LJ, Hajdin CE, Bennett B, Crowder MW. Structure and mechanism of copper- and nickel-substituted analogues of metallo-β-lactamase L1 Biochemistry. 48: 2981-2989. PMID 19228020 DOI: 10.1021/Bi802295Z |
0.415 |
|
| 2009 |
Limphong P, Crowder MW, Bennett B, Makaroff CA. Arabidopsis thaliana GLX2-1 contains a dinuclear metal binding site, but is not a glyoxalase 2 Biochemical Journal. 417: 323-330. PMID 18782082 DOI: 10.1042/Bj20081151 |
0.459 |
|
| 2008 |
Hu Z, Periyannan G, Bennett B, Crowder MW. Role of the Zn1 and Zn2 sites in metallo-β- lactamase L1 Journal of the American Chemical Society. 130: 14207-14216. PMID 18831550 DOI: 10.1021/Ja8035916 |
0.499 |
|
| 2008 |
Holdorf MM, Bennett B, Crowder MW, Makaroff CA. Spectroscopic studies on Arabidopsis ETHE1, a glyoxalase II-like protein Journal of Inorganic Biochemistry. 102: 1825-1830. PMID 18656261 DOI: 10.1016/J.Jinorgbio.2008.06.003 |
0.38 |
|
| 2008 |
Hu Z, Gunasekera TS, Spadafora L, Bennett B, Crowder MW. Metal content of metallo-β-lactamase L1 is determined by the bioavailability of metal ions Biochemistry. 47: 7947-7953. PMID 18597493 DOI: 10.1021/Bi8004768 |
0.435 |
|
| 2008 |
Sharma N, Hu Z, Crowder MW, Bennett B. Conformational changes in the metallo-β-lactamase ImiS during the catalytic reaction: An EPR spectrokinetic study of Co(II)-spin label interactions Journal of the American Chemical Society. 130: 8215-8222. PMID 18528987 DOI: 10.1021/Ja0774562 |
0.459 |
|
| 2008 |
Hu Z, Periyannan GR, Crowder MW. Folding strategy to prepare Co(II)-substituted metallo-β-lactamase L1 Analytical Biochemistry. 378: 177-183. PMID 18445468 DOI: 10.1016/J.Ab.2008.04.007 |
0.826 |
|
| 2008 |
Hu Z, Periyannan GR, Crowder MW. Folding strategy to prepare Co(II)-substituted metallo-β-lactamase L1 Analytical Biochemistry. 378: 177-183. PMID 18445468 DOI: 10.1016/j.ab.2008.04.007 |
0.3 |
|
| 2008 |
Yatsunyk LA, Easton JA, Kim LR, Sugarbaker SA, Bennett B, Breece RM, Vorontsov II, Tierney DL, Crowder MW, Rosenzweig AC. Structure and metal binding properties of ZnuA, a periplasmic zinc transporter from Escherichia coli. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 13: 271-88. PMID 18027003 DOI: 10.1007/S00775-007-0320-0 |
0.817 |
|
| 2008 |
Yatsunyk LA, Easton JA, Kim LR, Sugarbaker SA, Bennett B, Breece RM, Vorontsov II, Tierney DL, Crowder MW, Rosenzweig AC. Structure and metal binding properties of ZnuA, a periplasmic zinc transporter from Escherichia coli. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 13: 271-88. PMID 18027003 DOI: 10.1007/S00775-007-0320-0 |
0.817 |
|
| 2007 |
Crisp J, Conners R, Garrity JD, Carenbauer AL, Crowder MW, Spencer J. Structural basis for the role of Asp-120 in metallo-β-lactamases Biochemistry. 46: 10664-10674. PMID 17715946 DOI: 10.1021/Bi700707U |
0.433 |
|
| 2006 |
Costello AL, Sharma NP, Yang KW, Crowder MW, Tierney DL. X-ray absorption spectroscopy of the zinc-binding sites in the class B2 metallo-beta-lactamase ImiS from Aeromonas veronii bv. sobria. Biochemistry. 45: 13650-8. PMID 17087519 DOI: 10.1021/Bi061547E |
0.632 |
|
| 2006 |
Costello AL, Sharma NP, Yang KW, Crowder MW, Tierney DL. X-ray absorption spectroscopy of the zinc-binding sites in the class B2 metallo-beta-lactamase ImiS from Aeromonas veronii bv. sobria. Biochemistry. 45: 13650-8. PMID 17087519 DOI: 10.1021/Bi061547E |
0.632 |
|
| 2006 |
Crowder MW, Spencer J, Vila AJ. Metallo-β-lactamases: Novel weaponry for antibiotic resistance in bacteria Accounts of Chemical Research. 39: 721-728. PMID 17042472 DOI: 10.1021/Ar0400241 |
0.459 |
|
| 2006 |
Matthews ML, Periyannan G, Hajdin C, Sidgel TK, Bennett B, Crowder MW. Probing the reaction mechanism of the D-ala-D-ala dipeptidase, VanX, by using stopped-flow kinetic and rapid-freeze quench EPR studies on the Co(II)-substituted enzyme Journal of the American Chemical Society. 128: 13050-13051. PMID 17017774 DOI: 10.1021/Ja0627343 |
0.415 |
|
| 2006 |
Sigdel TK, Easton JA, Crowder MW. Transcriptional response of Escherichia coli to TPEN Journal of Bacteriology. 188: 6709-6713. PMID 16952965 DOI: 10.1128/Jb.00680-06 |
0.543 |
|
| 2006 |
Sharma NP, Hajdin C, Chandrasekar S, Bennett B, Yang KW, Crowder MW. Mechanistic studies on the mononuclear ZnII-containing metallo-β-lactamase ImiS from Aeromonas sobria Biochemistry. 45: 10729-10738. PMID 16939225 DOI: 10.1021/Bi060893T |
0.377 |
|
| 2006 |
Sigdel TK, Cilliers R, Gursahaney PR, Thompson P, Easton JA, Crowder MW. Probing the adaptive response of Escherichia coli to extracellular Zn(II) Biometals. 19: 461-471. PMID 16937252 DOI: 10.1007/S10534-005-4962-5 |
0.647 |
|
| 2006 |
Sun Q, Law A, Crowder MW, Geysen HM. Homo-cysteinyl peptide inhibitors of the L1 metallo-β-lactamase, and SAR as determined by combinatorial library synthesis Bioorganic and Medicinal Chemistry Letters. 16: 5169-5175. PMID 16875814 DOI: 10.1016/J.Bmcl.2006.07.001 |
0.356 |
|
| 2006 |
Costello A, Periyannan G, Yang KW, Crowder MW, Tierney DL. Site-selective binding of Zn(II) to metallo-beta-lactamase L1 from Stenotrophomonas maltophilia. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 11: 351-8. PMID 16489411 DOI: 10.1007/S00775-006-0083-Z |
0.651 |
|
| 2006 |
Costello A, Periyannan G, Yang KW, Crowder MW, Tierney DL. Site-selective binding of Zn(II) to metallo-beta-lactamase L1 from Stenotrophomonas maltophilia. Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry. 11: 351-8. PMID 16489411 DOI: 10.1007/S00775-006-0083-Z |
0.651 |
|
| 2006 |
Periyannan GR, Costello AL, Tierney DL, Yang KW, Bennett B, Crowder MW. Sequential binding of cobalt(II) to metallo-beta-lactamase CcrA. Biochemistry. 45: 1313-20. PMID 16430228 DOI: 10.1021/Bi051105N |
0.806 |
|
| 2006 |
Golich FC, Han M, Crowder MW. Over-expression, purification, and characterization of aminopeptidase N from Escherichia coli Protein Expression and Purification. 47: 634-639. PMID 16380266 DOI: 10.1016/J.Pep.2005.11.012 |
0.815 |
|
| 2005 |
Marasinghe GPK, Sander IM, Bennett B, Periyannan G, Yang KW, Makaroff CA, Crowder MW. Structural studies on a mitochondrial glyoxalase II Journal of Biological Chemistry. 280: 40668-40675. PMID 16227621 DOI: 10.1074/Jbc.M509748200 |
0.443 |
|
| 2005 |
Yang KW, Golich FC, Sigdel TK, Crowder MW. Phosphinate, sulfonate, and sulfonamidate dipeptides as potential inhibitors of Escherichia coli aminopeptidase N Bioorganic and Medicinal Chemistry Letters. 15: 5150-5153. PMID 16168644 DOI: 10.1016/J.Bmcl.2005.08.055 |
0.773 |
|
| 2005 |
Crawford PA, Yang KW, Sharma N, Bennett B, Crowder MW. Spectroscopic studies on cobalt(II)-substituted metallo-β-lactamase ImiS from Aeromonas veronii bv. sobria Biochemistry. 44: 5168-5176. PMID 15794654 DOI: 10.1021/Bi047463S |
0.833 |
|
| 2005 |
Breece RM, Costello A, Bennett B, Sigdel TK, Matthews ML, Tierney DL, Crowder MW. A five-coordinate metal center in Co(II)-substituted VanX. The Journal of Biological Chemistry. 280: 11074-81. PMID 15657055 DOI: 10.1074/Jbc.M412582200 |
0.821 |
|
| 2005 |
Breece RM, Costello A, Bennett B, Sigdel TK, Matthews ML, Tierney DL, Crowder MW. A five-coordinate metal center in Co(II)-substituted VanX. The Journal of Biological Chemistry. 280: 11074-81. PMID 15657055 DOI: 10.1074/Jbc.M412582200 |
0.821 |
|
| 2005 |
Garrity JD, Bennett B, Crowder MW. Direct evidence that the reaction intermediate of metallo-β-lactamase L1 is metal bound Biochemistry. 44: 1078-1087. PMID 15654764 DOI: 10.1021/Bi048385B |
0.497 |
|
| 2004 |
Sigdel TK, Cilliers R, Gursahaney PR, Crowder MW. Fractionation of soluble proteins in Escherichia coli using DEAE-, SP-, and phenyl sepharose chromatographies Journal of Biomolecular Techniques. 15: 199-207. PMID 15331586 |
0.522 |
|
| 2004 |
Garrity JD, Pauff JM, Crowder MW. Probing the dynamics of a mobile loop above the active site of L1, metallo-β-lactamase from Stenotrophomonas maltophilia, via site-directed mutagenesis and stopped-flow fluorescence spectroscopy Journal of Biological Chemistry. 279: 39663-39670. PMID 15271998 DOI: 10.1074/Jbc.M406826200 |
0.384 |
|
| 2004 |
Golich FC, Sigdel T, Breece RM, Detar L, Herron LR, Crowder MW. L-Alanine-p-nitroanilide is not a substrate for VanX Analytical Biochemistry. 331: 398-400. PMID 15265748 DOI: 10.1016/J.Ab.2004.05.026 |
0.748 |
|
| 2004 |
Crawford PA, Sharma N, Chandrasekar S, Sigdel T, Walsh TR, Spencer J, Crowder MW. Over-expression, purification, and characterization of metallo-β- lactamase ImiS from Aeromonas veronii bv. sobria Protein Expression and Purification. 36: 272-279. PMID 15249050 DOI: 10.1016/J.Pep.2004.04.017 |
0.817 |
|
| 2004 |
Periyannan G, Shaw PJ, Sigdel T, Crowder MW. In vivo folding of recombinant metallo-β-lactamase L1 requires the presence of Zn(II) Protein Science. 13: 2236-2243. PMID 15238636 DOI: 10.1110/Ps.04742704 |
0.711 |
|
| 2004 |
Periyannan G, Shaw PJ, Sigdel T, Crowder MW. In vivo folding of recombinant metallo-β-lactamase L1 requires the presence of Zn(II) Protein Science. 13: 2236-2243. PMID 15238636 DOI: 10.1110/ps.04742704 |
0.327 |
|
| 2004 |
Wenzel NF, Carenbauer AL, Pfiester MP, Schilling O, Meyer-Klaucke W, Makaroff CA, Crowder MW. The binding of iron and zinc to glyoxalase II occurs exclusively as di-metal centers and is unique within the metallo-β-lactamase family Journal of Biological Inorganic Chemistry. 9: 429-438. PMID 15067523 DOI: 10.1007/S00775-004-0535-2 |
0.435 |
|
| 2004 |
Wenzel NF, Carenbauer AL, Pfiester MP, Schilling O, Meyer-Klaucke W, Makaroff CA, Crowder MW. The binding of iron and zinc to glyoxalase II occurs exclusively as di-metal centers and is unique within the metallo-β-lactamase family Journal of Biological Inorganic Chemistry. 9: 429-438. PMID 15067523 DOI: 10.1007/s00775-004-0535-2 |
0.317 |
|
| 2004 |
Garrity JD, Carenbauer AL, Herron LR, Crowder MW. Metal Binding Asp-120 in Metallo-β-lactamase L1 from Stenotrophomonas maltophilia Plays a Crucial Role in Catalysis Journal of Biological Chemistry. 279: 920-927. PMID 14573595 DOI: 10.1074/Jbc.M309852200 |
0.499 |
|
| 2004 |
Garrity JD, Carenbauer AL, Herron LR, Crowder MW. Metal Binding Asp-120 in Metallo-β-lactamase L1 from Stenotrophomonas maltophilia Plays a Crucial Role in Catalysis Journal of Biological Chemistry. 279: 920-927. PMID 14573595 DOI: 10.1074/jbc.M309852200 |
0.306 |
|
| 2003 |
Cao X, Iqbal A, Patel A, Gretz P, Huang G, Crowder M, Day RA. 3-alkoxy-5-isoxazolidinones mimic beta-lactams. Biochemical and Biophysical Research Communications. 311: 267-71. PMID 14592409 DOI: 10.1016/J.Bbrc.2003.09.210 |
0.327 |
|
| 2003 |
Schilling O, Wenzel N, Naylor M, Vogel A, Crowder M, Makaroff C, Meyer-Klaucke W. Flexible metal binding of the metallo-β-lactamase domain: Glyoxalase II incorporates iron, manganese, and zinc in vivo Biochemistry. 42: 11777-11786. PMID 14529289 DOI: 10.1021/Bi034672O |
0.497 |
|
| 2003 |
Yang KW, Sobieski DN, Carenbauer AL, Crawford PA, Makaroff CA, Crowder MW. Explaining the inhibition of glyoxalase II by 9-fluorenylmethoxycarbonyl-protected glutathione derivatives Archives of Biochemistry and Biophysics. 414: 271-278. PMID 12781779 DOI: 10.1016/S0003-9861(03)00193-0 |
0.81 |
|
| 2003 |
Jacquamet L, Sun Y, Hatfield J, Gu W, Cramer SP, Crowder MW, Lorigan GA, Vincent JB, Latour JM. Characterization of chromodulin by X-ray absorption and electron paramagnetic resonance spectroscopies and magnetic susceptibility measurements Journal of the American Chemical Society. 125: 774-780. PMID 12526678 DOI: 10.1021/Ja0202661 |
0.305 |
|
| 2002 |
Simm AM, Higgins CS, Carenbauer AL, Crowder MW, Bateson JH, Bennett PM, Clarke AR, Halford SE, Walsh TR. Characterization of monomeric L1 metallo-β-lactamase and the role of the N-terminal extension in negative cooperativity and antibiotic hydrolysis Journal of Biological Chemistry. 277: 24744-24752. PMID 11940588 DOI: 10.1074/Jbc.M201524200 |
0.377 |
|
| 2002 |
Carenbauer AL, Garrity JD, Periyannan G, Yates RB, Crowder MW. Probing substrate binding to metallo-beta-lactamase L1 from Stenotrophomonas maltophilia by using site-directed mutagenesis. Bmc Biochemistry [Electronic Resource]. 3: 4. PMID 11876827 DOI: 10.1186/1471-2091-3-4 |
0.813 |
|
| 2001 |
Crowder MW, Yang KW, Carenbauer AL, Periyannan G, Seifert ME, Rude NE, Walsh TR. The problem of a solvent exposable disulfide when preparing Co(II)-substituted metallo-β-lactamase L1 from Stenotrophomonas maltophilia Journal of Biological Inorganic Chemistry. 6: 91-99. PMID 11191226 DOI: 10.1007/S007750000173 |
0.826 |
|
| 2001 |
Zang TM, Hollman DA, Crawford PA, Crowder MW, Makaroff CA. Arabidopsis Glyoxalase II Contains a Zinc/Iron Binuclear Metal Center That Is Essential for Substrate Binding and Catalysis Journal of Biological Chemistry. 276: 4788-4795. PMID 11085979 DOI: 10.1074/Jbc.M005090200 |
0.828 |
|
| 2001 |
Zang TM, Hollman DA, Crawford PA, Crowder MW, Makaroff CA. Arabidopsis Glyoxalase II Contains a Zinc/Iron Binuclear Metal Center That Is Essential for Substrate Binding and Catalysis Journal of Biological Chemistry. 276: 4788-4795. PMID 11085979 DOI: 10.1074/jbc.M005090200 |
0.317 |
|
| 2000 |
Brandt JJ, Chatwood LL, Crowder MW. Analysis of three overexpression systems for VanX, the zinc(II) dipeptidase required for high-level vancomycin resistance in bacteria Protein Expression and Purification. 20: 300-307. PMID 11049753 DOI: 10.1006/Prep.2000.1303 |
0.79 |
|
| 2000 |
Yanchak MP, Taylor RA, Crowder MW. Mutational analysis of metallo-β-lactamase CcrA from Bacteroides fragilis Biochemistry. 39: 11330-11339. PMID 10985778 DOI: 10.1021/Bi0010524 |
0.4 |
|
| 2000 |
Yang KW, Brandt JJ, Chatwood LL, Crowder MW. Phosphonamidate and phosphothioate dipeptides as potential inhibitors of VanX Bioorganic and Medicinal Chemistry Letters. 10: 1085-1087. PMID 10843223 DOI: 10.1016/S0960-894X(00)00186-4 |
0.778 |
|
| 1999 |
Yang KW, Crowder MW. Inhibition studies on the metallo-β-lactamase L1 from Stenotrophomonas maltophilia Archives of Biochemistry and Biophysics. 368: 1-6. PMID 10415104 DOI: 10.1006/Abbi.1999.1293 |
0.402 |
|
| 1999 |
Brandt JJ, Chatwood LL, Yang KW, Crowder MW. Continuous assay for VanX, the D-alanyl-D-alanine dipeptidase required for high-level vancomycin resistance Analytical Biochemistry. 272: 94-99. PMID 10405298 DOI: 10.1006/Abio.1999.4166 |
0.809 |
|
| 1999 |
McManus-Munoz S, Crowder MW. Kinetic mechanism of metallo-β-lactamase L1 from stenotrophomonas maltophilia Biochemistry. 38: 1547-1553. PMID 9931021 DOI: 10.1021/Bi9826512 |
0.317 |
|
| 1998 |
Crowder MW, Walsh TR, Banovic L, Pettit M, Spencer J. Overexpression, purification, and characterization of the cloned metallo-β-lactamase L1 from Stenotrophomonas maltophilia Antimicrobial Agents and Chemotherapy. 42: 921-926. PMID 9559809 DOI: 10.1128/Aac.42.4.921 |
0.427 |
|
| 1997 |
Crowder MW, Maiti MK, Banovic L, Makaroff CA. Glyoxalase II from A. thialana requires Zn(II) for catalytic activity Febs Letters. 418: 351-354. PMID 9428743 DOI: 10.1016/S0014-5793(97)01416-6 |
0.49 |
|
| 1996 |
Crowder MW, Wang Z, Franklin SL, Zovinka EP, Benkovic SJ. Characterization of the metal-binding sites of the beta-lactamase from Bacteroides fragilis. Biochemistry. 35: 12126-32. PMID 8810919 DOI: 10.1021/Bi960976H |
0.587 |
|
| 1996 |
Crowder MW, Wang Z, Franklin SL, Zovinka EP, Benkovic SJ. Characterization of the metal-binding sites of the beta-lactamase from Bacteroides fragilis. Biochemistry. 35: 12126-32. PMID 8810919 DOI: 10.1021/Bi960976H |
0.587 |
|
| 1995 |
Crowder MW, Stewart JD, Roberts VA, Bender CJ, Tevelrakh E, Peisach J, Getzoff ED, Gaffney BJ, Benkovic SJ. Spectroscopic Studies on the Designed Metal-Binding Sites of the 43C9 Single Chain Antibody Journal of the American Chemical Society. 117: 5627-5634. DOI: 10.1021/Ja00126A003 |
0.579 |
|
| 1994 |
Stewart JD, Roberts VA, Crowder MW, Getzoff ED, Benkovic SJ. Creation of a novel biosensor for zinc(II) Journal of the American Chemical Society. 116: 415-416. DOI: 10.1021/Ja00080A065 |
0.545 |
|
| 1993 |
Mueller EG, Crowder MW, Averill BA, Knowles JR. Purple acid phosphatase: a diiron enzyme that catalyzes a direct phospho group transfer to water Journal of the American Chemical Society. 115: 2974-2975. DOI: 10.1021/Ja00060A055 |
0.599 |
|
| 1993 |
Mueller EG, Crowder MW, Averill BA, Knowles JR. Purple acid phosphatase catalyzes the direct transfer of a phospho group from substrate to water. Journal of Inorganic Biochemistry. 51: 106. DOI: 10.1016/0162-0134(93)85142-U |
0.54 |
|
| 1993 |
Crowder M, Stewart J, Roberts V, Getzoff E, Benkovic S. Design, preparation and characterization of a de novo metal binding site in single chain catalytic antibody 43C9. Journal of Inorganic Biochemistry. 51: 76. DOI: 10.1016/0162-0134(93)85112-L |
0.506 |
|
| 1992 |
Wang Z, Ming LJ, Que L, Vincent JB, Crowder MW, Averill BA. 1H NMR and NOE studies of the purple acid phosphatases from porcine uterus and bovine spleen. Biochemistry. 31: 5263-8. PMID 1606150 DOI: 10.1021/Bi00138A004 |
0.602 |
|
| 1992 |
Vincent JB, Crowder MW, Averill BA. Hydrolysis of phosphate monoesters: a biological problem with multiple chemical solutions. Trends in Biochemical Sciences. 17: 105-10. PMID 1412693 DOI: 10.1016/0968-0004(92)90246-6 |
0.559 |
|
| 1992 |
Vincent JB, Crowder MW, Averill BA. Multiple binding sites for tetrahedral oxyanion inhibitors of bovine spleen purple acid phosphatase. Biochemistry. 31: 3033-7. PMID 1372824 DOI: 10.1021/Bi00127A001 |
0.597 |
|
| 1992 |
Vincent JB, Crowder MW, Averill BA. Multiple binding sites for tetrahedral oxyanion inhibitors of bovine spleen purple acid phosphatase. Biochemistry. 31: 3033-7. PMID 1372824 DOI: 10.1021/Bi00127A001 |
0.597 |
|
| 1992 |
Crowder MW, Vincent JB, Averill BA. Electron paramagnetic resonance studies on the high-salt form of bovine spleen purple acid phosphatase. Biochemistry. 31: 9603-8. PMID 1327121 DOI: 10.1021/Bi00155A012 |
0.56 |
|
| 1992 |
Crowder MW, Vincent JB, Averill BA. Electron paramagnetic resonance studies on the high-salt form of bovine spleen purple acid phosphatase. Biochemistry. 31: 9603-8. PMID 1327121 DOI: 10.1021/Bi00155A012 |
0.56 |
|
| 1991 |
Vincent JB, Crowder MW, Averill BA. Evidence for a phosphoryl-enzyme intermediate in phosphate ester hydrolysis by purple acid phosphatase from bovine spleen. The Journal of Biological Chemistry. 266: 17737-40. PMID 1917918 |
0.539 |
|
| 1991 |
Vincent JB, Crowder MW, Averill BA. Evidence for a phosphoryl-enzyme intermediate in phosphate ester hydrolysis by purple acid phosphatase from bovine spleen. The Journal of Biological Chemistry. 266: 17737-40. PMID 1917918 |
0.539 |
|
| 1991 |
Vincent JB, Crowder MW, Averill BA. Spectroscopic and kinetics studies of a high-salt-stabilized form of the purple acid phosphatase from bovine spleen. Biochemistry. 30: 3025-34. PMID 1848783 DOI: 10.1021/Bi00226A007 |
0.599 |
|
| 1991 |
Vincent JB, Crowder MW, Averill BA. Spectroscopic and kinetics studies of a high-salt-stabilized form of the purple acid phosphatase from bovine spleen. Biochemistry. 30: 3025-34. PMID 1848783 DOI: 10.1021/Bi00226A007 |
0.599 |
|
| 1991 |
Vincent JB, Crowder MW, Averill BA. The high-salt stabilized form of bovine spleen purple acid phosphatase. Journal of Inorganic Biochemistry. 43: 542. DOI: 10.1016/0162-0134(91)84517-D |
0.529 |
|
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