| Year |
Citation |
Score |
| 2019 |
Schwake C, Baldwin MR, Bachovchin W, Hegde S, Schiemer J, Okure C, Levin AE, Vannier E, Hanada T, Chishti AH. HIV protease inhibitors block parasite signal peptide peptidases and prevent growth of Babesia microti parasites in erythrocytes. Biochemical and Biophysical Research Communications. PMID 31311649 DOI: 10.1016/J.Bbrc.2019.07.031 |
0.32 |
|
| 2016 |
Coppage AL, Heard KR, DiMare MT, Liu Y, Wu W, Lai JH, Bachovchin WW. Human FGF-21 Is a Substrate of Fibroblast Activation Protein. Plos One. 11: e0151269. PMID 26962859 DOI: 10.1371/journal.pone.0151269 |
0.505 |
|
| 2015 |
Han R, Wang X, Bachovchin W, Zukowska Z, Osborn JW. Inhibition of dipeptidyl peptidase 8/9 impairs preadipocyte differentiation. Scientific Reports. 5: 12348. PMID 26242871 DOI: 10.1038/Srep12348 |
0.351 |
|
| 2015 |
Tomas E, Stanojevic V, McManus K, Khatri A, Everill P, Bachovchin WW, Habener JF. GLP-1(32-36)amide Pentapeptide Increases Basal Energy Expenditure and Inhibits Weight Gain in Obese Mice. Diabetes. 64: 2409-19. PMID 25858562 DOI: 10.2337/Db14-1708 |
0.719 |
|
| 2015 |
Akopian T, Kandror O, Tsu C, Lai JH, Wu W, Liu Y, Zhao P, Park A, Wolf L, Dick LR, Rubin EJ, Bachovchin W, Goldberg AL. Cleavage Specificity of Mycobacterium tuberculosis ClpP1P2 Protease and Identification of Novel Peptide Substrates and Boronate Inhibitors with Anti-bacterial Activity. The Journal of Biological Chemistry. 290: 11008-20. PMID 25759383 DOI: 10.1074/Jbc.M114.625640 |
0.368 |
|
| 2013 |
Heard KR, Wu W, Li Y, Zhao P, Woznica I, Lai JH, Beinborn M, Sanford DG, Dimare MT, Chiluwal AK, Peters DE, Whicher D, Sudmeier JL, Bachovchin WW. A general method for making peptide therapeutics resistant to serine protease degradation: application to dipeptidyl peptidase IV substrates. Journal of Medicinal Chemistry. 56: 8339-51. PMID 24044354 DOI: 10.1021/jm400423p |
0.532 |
|
| 2013 |
Connolly BA, O'Connell DP, Lamon-Fava S, LeBlanc DF, Kuang YL, Schaefer EJ, Coppage AL, Benedict CR, Kiritsy CP, Bachovchin WW. The high-fat high-fructose hamster as an animal model for niacin's biological activities in humans. Metabolism: Clinical and Experimental. 62: 1840-9. PMID 24035454 DOI: 10.1016/J.Metabol.2013.08.001 |
0.476 |
|
| 2012 |
Wu W, Liu Y, Milo LJ, Shu Y, Zhao P, Li Y, Woznica I, Yu G, Sanford DG, Zhou Y, Poplawski SE, Connolly BA, Sudmeier JL, Bachovchin WW, Lai JH. 4-Substituted boro-proline dipeptides: synthesis, characterization, and dipeptidyl peptidase IV, 8, and 9 activities. Bioorganic & Medicinal Chemistry Letters. 22: 5536-40. PMID 22853995 DOI: 10.1016/J.Bmcl.2012.07.033 |
0.704 |
|
| 2012 |
Everill P, Sudmeier JL, Bachovchin WW. Direct NMR observation and pKa determination of the Asp102 side chain in a serine protease. Journal of the American Chemical Society. 134: 2348-54. PMID 22229736 DOI: 10.1021/Ja210091Q |
0.752 |
|
| 2011 |
Milo LJ, Lai JH, Wu W, Liu Y, Maw H, Li Y, Jin Z, Shu Y, Poplawski SE, Wu Y, Sanford DG, Sudmeier JL, Bachovchin WW. Chemical and biological evaluation of dipeptidyl boronic acid proteasome inhibitors for use in prodrugs and pro-soft drugs targeting solid tumors. Journal of Medicinal Chemistry. 54: 4365-77. PMID 21634429 DOI: 10.1021/Jm200460Q |
0.716 |
|
| 2008 |
Connolly BA, Sanford DG, Chiluwal AK, Healey SE, Peters DE, Dimare MT, Wu W, Liu Y, Maw H, Zhou Y, Li Y, Jin Z, Sudmeier JL, Lai JH, Bachovchin WW. Dipeptide boronic acid inhibitors of dipeptidyl peptidase IV: determinants of potency and in vivo efficacy and safety. Journal of Medicinal Chemistry. 51: 6005-13. PMID 18783201 DOI: 10.1021/Jm800390N |
0.598 |
|
| 2007 |
Lai JH, Wu W, Zhou Y, Maw HH, Liu Y, Milo LJ, Poplawski SE, Henry GD, Sudmeier JL, Sanford DG, Bachovchin WW. Synthesis and characterization of constrained peptidomimetic dipeptidyl peptidase IV inhibitors: amino-lactam boroalanines. Journal of Medicinal Chemistry. 50: 2391-8. PMID 17458948 DOI: 10.1021/Jm061321+ |
0.716 |
|
| 2002 |
Ivanov D, Bachovchin WW, Redfield AG. Boron-11 pure quadrupole resonance investigation of peptide boronic acid inhibitors bound to alpha-lytic protease. Biochemistry. 41: 1587-90. PMID 11814352 DOI: 10.1021/Bi011783J |
0.312 |
|
| 1996 |
Tsilikounas E, Rao T, Gutheil WG, Bachovchin WW. 15N and 1H NMR spectroscopy of the catalytic histidine in chloromethyl ketone-inhibited complexes of serine proteases Biochemistry. 35: 2437-2444. PMID 8652587 DOI: 10.1021/Bi9513968 |
0.649 |
|
| 1996 |
Coutts SJ, Kelly TA, Snow RJ, Kennedy CA, Barton RW, Adams J, Krolikowski DA, Freeman DM, Campbell SJ, Ksiazek JF, Bachovchin WW. Structure-activity relationships of boronic acid inhibitors of dipeptidyl peptidase IV. 1. Variation of the P2 position of Xaa-boroPro dipeptides Journal of Medicinal Chemistry. 39: 2087-2094. PMID 8642568 |
0.309 |
|
| 1994 |
Sudmeier JL, Günther UL, Gutheil WG, Coutts SJ, Snow RJ, Barton RW, Bachovchin WW. Solution structures of active and inactive forms of the DP IV (CD26) inhibitor Pro-boroPro determined by NMR spectroscopy Biochemistry. 33: 12427-12438. PMID 7918465 DOI: 10.1021/Bi00207A009 |
0.681 |
|
| 1994 |
Gutheil WG, Subramanyam M, Flentke GR, Sanford DG, Munoz E, Huber BT, Bachovchin WW. Human immunodeficiency virus 1 Tat binds to dipeptidyl aminopeptidase IV (CD26): a possible mechanism for Tat's immunosuppressive activity. Proceedings of the National Academy of Sciences of the United States of America. 91: 6594-8. PMID 7912830 DOI: 10.1073/Pnas.91.14.6594 |
0.607 |
|
| 1994 |
Gutheil WG, Kettner CA, Bachovchin WW. Kinlsq: A program for fitting kinetics data with numerically integrated rate equations and its application to the analysis of slow, tight-binding inhibition data Analytical Biochemistry. 223: 13-20. PMID 7695087 DOI: 10.1006/Abio.1994.1539 |
0.595 |
|
| 1994 |
Snow RJ, Bachovchin WW, Barton RW, Campbell SJ, Coutts SJ, Freeman DM, Gutheil WG, Kelly TA, Kennedy CA, Krolikowski DA, Leonard SF, Pargellis CA, Tong L, Adams J. Studies on proline boronic acid dipeptide inhibitors of dipeptidyl peptidase IV: Identification of a cyclic species containing a B-N bond Journal of the American Chemical Society. 116: 10860-10869. DOI: 10.1021/Ja00103A002 |
0.685 |
|
| 1993 |
Gutheil WG, Bachovchin WW. Separation of L-Pro-DL-boroPro into its component diastereomers and kinetic analysis of their inhibition of dipeptidyl peptidase IV. A new method for the analysis of slow, tight-binding inhibition Biochemistry. 32: 8723-8731. PMID 8103356 DOI: 10.1021/Bi00085A001 |
0.654 |
|
| 1993 |
Farr-Jones S, Wong WYL, Gutheil WG, Bachovchin WW. Direct observation of the tautomeric forms of histidine in 15N NMR spectra at low temperatures. Comments on intramolecular hydrogen bonding and on tautomeric equilibrium constants Journal of the American Chemical Society. 115: 6813-6819. |
0.625 |
|
| 1992 |
Tsilikounas E, Kettner CA, Bachovchin WW. Identification of serine and histidine adducts in complexes of trypsin and trypsinogen with peptide and nonpeptide boronic acid inhibitors by1H NMR spectroscopy Biochemistry®. 31: 12839-12846. PMID 1463754 |
0.371 |
|
| 1990 |
Bachovchin WW, Plaut AG, Flentke GR, Lynch M, Kettner CA. Inhibition of IgA1 proteinases from Neisseria gonorrhoeae and Hemophilus influenzae by peptide prolyl boronic acids Journal of Biological Chemistry. 265: 3738-3743. PMID 2105953 |
0.306 |
|
| 1988 |
Kettner CA, Bone R, Agard DA, Bachovchin WW. Kinetic properties of the binding of α-lytic protease to peptide boronic acids Biochemistry. 27: 7682-7688. PMID 3207699 DOI: 10.1021/Bi00420A017 |
0.319 |
|
| 1988 |
Bachovchin WW, Wong WYL, Farr-Jones S, Shenvi AB, Kettner CA. Nitrogen-15 NMR spectroscopy of the catalytic-triad histidine of a serine protease in peptide boronic acid inhibitor complexes Biochemistry. 27: 7689-7697. |
0.343 |
|
| 1982 |
Bachovchin WW, Kanamori K, Vallee BL, Roberts JD. Nitrogen-15 nuclear magnetic resonance of arsanilazotyrosine-248 carboxypeptidase A and its complex with β-phenylpropionate. Structure and dynamics in solution Biochemistry. 21: 2885-2892. PMID 7104301 DOI: 10.1021/Bi00541A013 |
0.538 |
|
| 1981 |
Bachovchin WW, Kaiser R, Richards JH, Roberts JD. Catalytic mechanism of serine proteases: Reexamination of the pH dependence of the histidyl 1J13(C2-H) coupling constant in the catalytic triad of α-lytic protease Proceedings of the National Academy of Sciences of the United States of America. 78: 7323-7326. PMID 7038675 DOI: 10.1073/Pnas.78.12.7323 |
0.552 |
|
| 1979 |
Moore KW, Bachovchin WW, Gunter JB, Richards JH. Hydrogen transfer in catalysis by adenosylcobalamin-dependent diol dehydratase. Biochemistry. 18: 2776-82. PMID 383139 DOI: 10.1021/Bi00580A013 |
0.414 |
|
| 1979 |
BACHOVCHIN WW, ROBERTS JD. ChemInform Abstract: NITROGEN-15 NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY. THE STATE OF HISTIDINE IN THE CATALYTIC TRIAD OF α-LYTIC PROTEASE. IMPLICATIONS FOR TH CHARGE-RELAY MECHANISM OF PEPTIDE-BOND CLEAVAGE BY SERINE PROTEASES Chemischer Informationsdienst. 10. DOI: 10.1002/chin.197912386 |
0.365 |
|
| 1978 |
Bachovchin WW, Moore KW, Richards JH. Mechanism of action of adenosylcobalamin: hydrogen transfer in the inactivation of diol dehydratase by glycerol. Biochemistry. 17: 2218-24. PMID 667021 DOI: 10.1021/Bi00604A031 |
0.448 |
|
| 1978 |
Bachovchin WW, Roberts JD. Nitrogen-15 nuclear magnetic resonance spectroscopy. The state of histidine in the catalytic triad of .alpha.-lytic protease. Implications for the charge-relay mechanism of peptide-bond cleavage by serine proteases Journal of the American Chemical Society. 100: 8041-8047. DOI: 10.1021/Ja00494A001 |
0.461 |
|
| 1977 |
Bachovchin WW, Eagar RG, Moore KW, Richards JH. Mechanism of action of adenosylcobalamin: glycerol and other substrate analogues as substrates and inactivators for propanediol dehydratase--kinetics, stereospecificity, and mechanism. Biochemistry. 16: 1082-92. PMID 321014 DOI: 10.1021/Bi00625A009 |
0.492 |
|
| 1975 |
Eagar RG, Bachovchin WW, Richards JH. Mechanism of action of adenosylcobalamin: 3-fluoro-1,2-propanediol as substrate for propanediol dehydrase - Mechanistic implications Biochemistry. 14: 5523-5528. PMID 1201278 DOI: 10.1021/Bi00696A022 |
0.425 |
|
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