| Year |
Citation |
Score |
| 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 |
0.96 |
|
| 2015 |
Fan MH, Zhu Q, Li HH, Ra HJ, Majumdar S, Gulick DL, Jerome JA, Madsen DH, Christofidou-Solomidou M, Speicher DW, Bachovchin WW, Feghali-Bostwick C, Pur Eacute E. Fibroblast Activation Protein (FAP) Accelerates Collagen Degradation and Clearance from Lung in Mice. The Journal of Biological Chemistry. PMID 26663085 DOI: 10.1074/jbc.M115.701433 |
0.96 |
|
| 2015 |
Wong PF, Gall MG, Bachovchin WW, McCaughan GW, Keane FM, Gorrell MD. Neuropeptide Y is a physiological substrate of fibroblast activation protein: Enzyme kinetics in blood plasma and expression of Y2R and Y5R in human liver cirrhosis and hepatocellular carcinoma. Peptides. PMID 26621486 DOI: 10.1016/j.peptides.2015.11.004 |
0.96 |
|
| 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 |
0.96 |
|
| 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 |
0.96 |
|
| 2015 |
Williams KH, Viera de Ribeiro AJ, Prakoso E, Veillard AS, Shackel NA, Bu Y, Brooks B, Cavanagh E, Raleigh J, McLennan SV, McCaughan GW, Bachovchin WW, Keane FM, Zekry A, Twigg SM, et al. Lower serum fibroblast activation protein shows promise in the exclusion of clinically significant liver fibrosis due to non-alcoholic fatty liver disease in diabetes and obesity. Diabetes Research and Clinical Practice. 108: 466-72. PMID 25836944 DOI: 10.1016/j.diabres.2015.02.024 |
0.96 |
|
| 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 |
0.96 |
|
| 2014 |
Bachovchin DA, Koblan LW, Wu W, Liu Y, Li Y, Zhao P, Woznica I, Shu Y, Lai JH, Poplawski SE, Kiritsy CP, Healey SE, DiMare M, Sanford DG, Munford RS, ... Bachovchin WW, et al. A high-throughput, multiplexed assay for superfamily-wide profiling of enzyme activity. Nature Chemical Biology. 10: 656-63. PMID 24997602 DOI: 10.1038/nchembio.1578 |
0.96 |
|
| 2014 |
Donahue RN, Duncan BB, Fry TJ, Jones B, Bachovchin WW, Kiritsy CP, Lai JH, Wu W, Zhao P, Liu Y, Tsang KY, Hodge JW. A pan inhibitor of DASH family enzymes induces immunogenic modulation and sensitizes murine and human carcinoma cells to antigen-specific cytotoxic T lymphocyte killing: implications for combination therapy with cancer vaccines. Vaccine. 32: 3223-31. PMID 24731809 DOI: 10.1016/j.vaccine.2014.04.008 |
0.96 |
|
| 2013 |
Keane FM, Yao TW, Seelk S, Gall MG, Chowdhury S, Poplawski SE, Lai JH, Li Y, Wu W, Farrell P, Vieira de Ribeiro AJ, Osborne B, Yu DM, Seth D, Rahman K, ... ... Bachovchin WW, et al. Quantitation of fibroblast activation protein (FAP)-specific protease activity in mouse, baboon and human fluids and organs. Febs Open Bio. 4: 43-54. PMID 24371721 DOI: 10.1016/j.fob.2013.12.001 |
0.96 |
|
| 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 |
0.96 |
|
| 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 |
0.96 |
|
| 2013 |
Duncan BB, Highfill SL, Qin H, Bouchkouj N, Larabee S, Zhao P, Woznica I, Liu Y, Li Y, Wu W, Lai JH, Jones B, Mackall CL, Bachovchin WW, Fry TJ. A pan-inhibitor of DASH family enzymes induces immune-mediated regression of murine sarcoma and is a potent adjuvant to dendritic cell vaccination and adoptive T-cell therapy. Journal of Immunotherapy (Hagerstown, Md. : 1997). 36: 400-11. PMID 23994886 DOI: 10.1097/CJI.0b013e3182a80213 |
0.96 |
|
| 2013 |
Poplawski SE, Lai JH, Li Y, Jin Z, Liu Y, Wu W, Wu Y, Zhou Y, Sudmeier JL, Sanford DG, Bachovchin WW. Identification of selective and potent inhibitors of fibroblast activation protein and prolyl oligopeptidase. Journal of Medicinal Chemistry. 56: 3467-77. PMID 23594271 DOI: 10.1021/jm400351a |
0.96 |
|
| 2013 |
Walsh MP, Duncan B, Larabee S, Krauss A, Davis JP, Cui Y, Kim SY, Guimond M, Bachovchin W, Fry TJ. Val-boroPro accelerates T cell priming via modulation of dendritic cell trafficking resulting in complete regression of established murine tumors. Plos One. 8: e58860. PMID 23554941 DOI: 10.1371/journal.pone.0058860 |
0.96 |
|
| 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 |
0.96 |
|
| 2012 |
Qin S, Kamanna VS, Lai JH, Liu T, Ganji SH, Zhang L, Bachovchin WW, Kashyap ML. Reverse D4F, an apolipoprotein-AI mimetic peptide, inhibits atherosclerosis in ApoE-null mice. Journal of Cardiovascular Pharmacology and Therapeutics. 17: 334-43. PMID 22308547 DOI: 10.1177/1074248411434598 |
0.96 |
|
| 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 |
0.96 |
|
| 2012 |
O'Connell DP, LeBlanc DF, Cromley D, Billheimer J, Rader DJ, Bachovchin WW. Design and synthesis of boronic acid inhibitors of endothelial lipase. Bioorganic & Medicinal Chemistry Letters. 22: 1397-401. PMID 22225633 DOI: 10.1016/j.bmcl.2011.12.043 |
0.96 |
|
| 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 |
0.96 |
|
| 2011 |
Poplawski SE, Lai JH, Sanford DG, Sudmeier JL, Wu W, Bachovchin WW. Pro-soft Val-boroPro: a strategy for enhancing in vivo performance of boronic acid inhibitors of serine proteases. Journal of Medicinal Chemistry. 54: 2022-8. PMID 21388136 DOI: 10.1021/jm100972f |
0.96 |
|
| 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 |
0.96 |
|
| 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+ |
0.96 |
|
| 2006 |
Reese DK, Meinke G, Kumar A, Moine S, Chen K, Sudmeier JL, Bachovchin W, Bohm A, Bullock PA. Analyses of the interaction between the origin binding domain from simian virus 40 T antigen and single-stranded DNA provide insights into DNA unwinding and initiation of DNA replication. Journal of Virology. 80: 12248-59. PMID 17005644 DOI: 10.1128/JVI.01201-06 |
0.96 |
|
| 2006 |
Lai JH, Liu Y, Wu W, Zhou Y, Maw HH, Bachovchin WW, Bhat KL, Bock CW. Synthesis and structural investigation of internally coordinated alpha-amidoboronic acids. The Journal of Organic Chemistry. 71: 512-9. PMID 16408958 DOI: 10.1021/jo051757h |
0.96 |
|
| 2005 |
Sudmeier JL, Zhou Y, Lai JH, Maw HH, Wu W, Bachovchin WW. Autochelation in dipeptide boronic acids: pH-dependent structures and equilibria of Asp-boroPro and His-boroPro by NMR spectroscopy. Journal of the American Chemical Society. 127: 8112-9. PMID 15926838 DOI: 10.1021/ja050215e |
0.96 |
|
| 2005 |
Cheng JD, Valianou M, Canutescu AA, Jaffe EK, Lee HO, Wang H, Lai JH, Bachovchin WW, Weiner LM. Abrogation of fibroblast activation protein enzymatic activity attenuates tumor growth. Molecular Cancer Therapeutics. 4: 351-60. PMID 15767544 DOI: 10.1158/1535-7163.MCT-04-0269 |
0.96 |
|
| 2005 |
Haddad KC, Sudmeier JL, Bachovchin DA, Bachovchin WW. alpha-lytic protease can exist in two separately stable conformations with different His57 mobilities and catalytic activities. Proceedings of the National Academy of Sciences of the United States of America. 102: 1006-11. PMID 15657134 DOI: 10.1073/pnas.0409279102 |
0.96 |
|
| 2004 |
Bradshaw EM, Sanford DG, Luo X, Sudmeier JL, Gurard-Levin ZA, Bullock PA, Bachovchin WW. T antigen origin-binding domain of simian virus 40: determinants of specific DNA binding. Biochemistry. 43: 6928-36. PMID 15170330 DOI: 10.1021/bi030228+ |
0.96 |
|
| 2003 |
Rosay M, Lansing JC, Haddad KC, Bachovchin WW, Herzfeld J, Temkin RJ, Griffin RG. High-frequency dynamic nuclear polarization in MAS spectra of membrane and soluble proteins. Journal of the American Chemical Society. 125: 13626-7. PMID 14599177 DOI: 10.1021/ja036898k |
0.96 |
|
| 2003 |
Sudmeier JL, Bradshaw EM, Haddad KE, Day RM, Thalhauser CJ, Bullock PA, Bachovchin WW. Identification of histidine tautomers in proteins by 2D 1H/13C(delta2) one-bond correlated NMR. Journal of the American Chemical Society. 125: 8430-1. PMID 12848537 DOI: 10.1021/ja034072c |
0.96 |
|
| 2003 |
Lai JH, Zhou Y, Sudmeier JL, Wu W, Sanford DG, Hliang M, Poplawski S, Bachovchin WW. Microscopic acid-base equilibra of alanyl-boroAlanine. Advances in Experimental Medicine and Biology. 524: 333-8. PMID 12675255 DOI: 10.1007/0-306-47920-6_39 |
0.96 |
|
| 2003 |
Day RM, Thalhauser CJ, Sudmeier JL, Vincent MP, Torchilin EV, Sanford DG, Bachovchin CW, Bachovchin WW. Tautomerism, acid-base equilibria, and H-bonding of the six histidines in subtilisin BPN' by NMR. Protein Science : a Publication of the Protein Society. 12: 794-810. PMID 12649438 DOI: 10.1110/ps.0235203 |
0.96 |
|
| 2003 |
Krishnaswamy S, Duan SX, Von Moltke LL, Greenblatt DJ, Sudmeier JL, Bachovchin WW, Court MH. Serotonin (5-hydroxytryptamine) glucuronidation in vitro: Assay development, human liver microsome activities and species differences Xenobiotica. 33: 169-180. PMID 12623759 DOI: 10.1080/0049825021000048809 |
0.96 |
|
| 2001 |
Zhao X, Sudmeier JL, Bachovchin WW, Levitt MH. Measurement of NH bond lengths by fast magic-angle spinning solid-state NMR spectroscopy: A new method for the quantification of hydrogen bonds [1] Journal of the American Chemical Society. 123: 11097-11098. PMID 11686729 DOI: 10.1021/ja016328p |
0.96 |
|
| 2001 |
Bachovchin WW. Contributions of NMR spectroscopy to the study of hydrogen bonds in serine protease active sites Magnetic Resonance in Chemistry. 39. |
0.96 |
|
| 2000 |
Ash EL, Sudmeier JL, Day RM, Vincent M, Torchilin EV, Haddad KC, Bradshaw EM, Sanford DG, Bachovchin WW. Unusual 1H NMR chemical shifts support (His) C(epsilon) 1...O==C H-bond: proposal for reaction-driven ring flip mechanism in serine protease catalysis. Proceedings of the National Academy of Sciences of the United States of America. 97: 10371-6. PMID 10984533 |
0.96 |
|
| 1997 |
Ash EL, Sudmeier JL, De Fabo EC, Bachovchin WW. A low-barrier hydrogen bond in the catalytic triad of serine proteases? Theory versus experiment Science. 278: 1128-1132. PMID 9353195 DOI: 10.1126/science.278.5340.1128 |
0.96 |
|
| 1997 |
O'connell TP, Day RM, Torchilin EV, Bachovchin WW, Malthouse JG. A 13C-NMR study of the role of Asn-155 in stabilizing the oxyanion of a subtilisin tetrahedral adduct The Biochemical Journal. 326. PMID 9307038 |
0.96 |
|
| 1996 |
Sudmeier JL, Ash EL, Günther UL, Luo X, Bullock PA, Bachovchin WW. HCN, a triple-resonance NMR technique for selective observation of histidine and tryptophan side chains in 13C/15N-labeled proteins Journal of Magnetic Resonance - Series B. 113: 236-247. PMID 8995843 |
0.96 |
|
| 1996 |
Günther UL, Liu Y, Sanford D, Bachovchin WW, Schaffhausen B. NMR analysis of interactions of a phosphatidylinositol 3'-kinase SH2 domain with phosphotyrosine peptides reveals interdependence of major binding sites. Biochemistry. 35: 15570-81. PMID 8952511 DOI: 10.1021/bi961783x |
0.96 |
|
| 1996 |
Luo X, Sanford DG, Bullock PA, Bachovchin WW. Solution structure of the origin DNA-binding domain of SV40 T-antigen. Nature Structural Biology. 3: 1034-9. PMID 8946857 DOI: 10.1038/nsb1296-1034 |
0.96 |
|
| 1996 |
Freedman SJ, Sanford DG, Bachovchin WW, Furie BC, Baleja JD, Furie B. Structure and function of the epidermal growth factor domain of P-selectin. Biochemistry. 35: 13733-44. PMID 8901515 DOI: 10.1021/bi9610257 |
0.96 |
|
| 1996 |
Yamaguchi N, Plant C, Biancone L, Bachovchin W, Mccluskey R, Andres G. In vivo modulation of CD26 (dipeptidyl peptidase IV) in the mouse: Effects of polyreactive and monoreactive antibodies Transplantation. 62: 973-985. PMID 8878393 DOI: 10.1097/00007890-199610150-00017 |
0.96 |
|
| 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 |
0.96 |
|
| 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 |
0.96 |
|
| 1996 |
Schmitz T, Underwood R, Khiroya R, Bachovchin WW, Huber BT. Potentiation of the immune response in HIV-1+ individuals Journal of Clinical Investigation. 97: 1545-1549. PMID 8617888 |
0.96 |
|
| 1996 |
Sudmeier JL, Günther UL, Albert K, Bachovchin WW. Sensitivity optimization in continuous-flow FTNMR Journal of Magnetic Resonance - Series A. 118: 145-156. |
0.96 |
|
| 1995 |
Bristol LA, Bachovchin W, Takacs L. Inhibition of CD26 enzyme activity with Pro-boropro stimulates rat granulocyte/macrophage colony formation and thymocyte proliferation in vitro Blood. 85: 3602-3609. PMID 7780144 |
0.96 |
|
| 1995 |
Snow RJ, Bachovchin WW. Boronic acid inhibitors of dipeptidyl peptidase IV. A new class of immunosuppressive agents Advances in Medicinal Chemistry. 3: 149-177. DOI: 10.1016/S1067-5698(06)80006-4 |
0.96 |
|
| 1995 |
GÜNTHER UL, SUDMEIER JL, ALBERT K, BACHOVCHIN WW. NOE Enhancement in Continuous-Flow13C and15N FT NMR Using Upstream1H Preirradiation Journal of Magnetic Resonance, Series A. 117: 73-77. DOI: 10.1006/jmra.1995.9970 |
0.96 |
|
| 1995 |
Silks LA, Dunkle E, Unkefer CJ, Sudmeier JL, Butler M, Bachovchin WW. A reinvestigation of the synthesis of [15N2]hydroxymethylimidazole: Useful in an improved synthesis of (D,L)-[τ,π-15N2]histidine Journal of Labelled Compounds and Radiopharmaceuticals. 36: 947-951. DOI: 10.1002/jlcr.2580361006 |
0.96 |
|
| 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 |
0.96 |
|
| 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 |
0.96 |
|
| 1994 |
Kubota T, Iizuka H, Bachovchin WW, Stollar BD. Dipeptidyl peptidase IV (DP IV) activity in serum and on lymphocytes of MRL/Mp-lpr/lpr mice correlates with disease onset Clinical and Experimental Immunology. 96: 292-296. PMID 7910536 |
0.96 |
|
| 1994 |
Plaut AG, Bachovchin WW. IgA-specific prolyl endopeptidases: Serine type Methods in Enzymology. 244: 137-151. PMID 7845203 DOI: 10.1016/0076-6879(94)44012-3 |
0.96 |
|
| 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 |
0.96 |
|
| 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 |
0.96 |
|
| 1993 |
Tsilikounas E, Kettner CA, Bachovchin WW. 11B NMR spectroscopy of peptide boronic acid inhibitor complexes of α- lytic protease. Direct evidence for tetrahedral boron in both boron-histidine and boron-serine adduct complexes Biochemistry. 32: 12651-12655. PMID 8251483 DOI: 10.1021/bi00210a013 |
0.96 |
|
| 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 |
0.96 |
|
| 1993 |
Subramanyam M, Gutheil WG, Bachovchin WW, Huber BT. Mechanism of HIV-1 tat induced inhibition of antigen-specific T cell responsiveness Journal of Immunology. 150: 2544-2553. PMID 8095514 |
0.96 |
|
| 1993 |
Bachovchin WW. 11B NMR spectroscopy of peptide boronic acid inhibitor complexes of α-lytic protease. direct evidence for tetrahedral boron in both boron-histidine and boron-serine adduct complexes Biochemistry®. 12651-12655. |
0.96 |
|
| 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. |
0.96 |
|
| 1993 |
Kelly TA, Adams J, Bachovchin WW, Barton RW, Campbell SJ, Coutts SJ, Kennedy CA, Snow RJ. Immunosuppressive boronic acid dipeptides: Correlation between conformation and activity Journal of the American Chemical Society. 115: 12637-12638. |
0.96 |
|
| 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 |
0.96 |
|
| 1992 |
Valle Blazquez M, Madueño JA, Gonzalez R, Jurado R, Bachovchin WW, Peña J, Muñoz E. Selective decrease of CD26 expression in T cells from HIV-1-infected individuals Journal of Immunology. 149: 3073-3077. PMID 1357035 |
0.96 |
|
| 1992 |
Kubota T, Flentke GR, Bachovchin WW, Stollar BD. Involvement of dipeptidyl peptidase IV in an in vivo immune response Clinical and Experimental Immunology. 89: 192-197. PMID 1353423 |
0.96 |
|
| 1992 |
Pies R, Renshaw P, Goff DC, Metz A, Bachovchin W, Hotz R, Shader RI. Water-suppressed proton nuclear magnetic resonance spectroscopy of plasma from schizophrenics and normal controls: A preliminary report Research Communications in Psychology, Psychiatry and Behavior. 17: 25-32. |
0.96 |
|
| 1991 |
Sanford DG, Kanagy C, Sudmeier JL, Furie BC, Furie B, Bachovchin WW. Structure of the propeptide of prothrombin containing the gamma-carboxylation recognition site determined by two-dimensional NMR spectroscopy. Biochemistry. 30: 9835-41. PMID 1911775 |
0.96 |
|
| 1991 |
Flentke GR, Munoz E, Huber BT, Plaut AG, Kettner CA, Bachovchin WW. Inhibition of dipeptidyl aminopeptidase IV (DP-IV) by Xaa-boroPro dipeptides and use of these inhibitors to examine the role of DP-IV in T-cell function Proceedings of the National Academy of Sciences of the United States of America. 88: 1556-1559. PMID 1671716 |
0.96 |
|
| 1990 |
van Dijk AA, de Lange LC, Bachovchin WW, Robillard GT. Effect of phosphorylation on hydrogen-bonding interactions of the active site histidine of the phosphocarrier protein HPr of the phosphoenolpyruvate-dependent phosphotransferase system determined by 15N NMR spectroscopy. Biochemistry. 29: 8164-71. PMID 2261470 |
0.96 |
|
| 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 |
0.96 |
|
| 1989 |
Farr-Jones S, Smith SO, Kettner CA, Griffin RG, Bachovchin WW. Crystal versus solution structure of enzymes: NMR spectroscopy of a peptide boronic acid-serine protease complex in the crystalline state Proceedings of the National Academy of Sciences of the United States of America. 86: 6922-6924. PMID 2780549 DOI: 10.1073/pnas.86.18.6922 |
0.96 |
|
| 1989 |
Albert K, Sudmeier JL, Anwer MS, Bachovchin WW. Continuous flow 13C-filtered 1H NMR spectroscopy of ethanol metabolism in rat liver perfusate Magnetic Resonance in Medicine. 11: 309-315. PMID 2779419 |
0.96 |
|
| 1989 |
Smith SO, Farr-Jones S, Griffin RG, Bachovchin WW. Crystal versus solution structures of enzymes: NMR spectroscopy of a crystalline serine protease Science. 244: 961-964. PMID 2499045 DOI: 10.1126/science.2499045 |
0.96 |
|
| 1989 |
Burke PA, Smith SO, Bachovchin WW, Klibanov AM. Demonstration of structural integrity of an enzyme in organic solvents by solid-state NMR Journal of the American Chemical Society. 111: 8290-8291. |
0.96 |
|
| 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 |
0.96 |
|
| 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. |
0.96 |
|
| 1987 |
Lin PS, Blumenstein M, Mikkelsen RB, Schmidt-Ullrich R, Bachovchin WW. Perfusion of cell spheroids for study by NMR spectroscopy Journal of Magnetic Resonance (1969). 73: 399-404. DOI: 10.1016/0022-2364(87)90002-3 |
0.96 |
|
| 1987 |
Levitt MH, Sudmeier JL, Bachovchin WW. NMR solvent peak suppression with a soft-pulse nonlinear excitation sequence Journal of the American Chemical Society. 109: 6540-6541. |
0.96 |
|
| 1986 |
Tan SL, Kopczynski MG, Bachovchin WW, Orme-Johnson WH, Babior BM. Electron spin-echo studies of the composition of the paramagnetic intermediate formed during the deamination of propanolamine by ethanolamine ammonia-lyase, and AdoCbl-dependent enzyme. The Journal of Biological Chemistry. 261: 3483-5. PMID 3949775 |
0.96 |
|
| 1986 |
Bachovchin WW. 15N NMR spectroscopy of hydrogen-bonding interactions in the active site of serine proteases: evidence for a moving histidine mechanism Biochemistry. 25: 7751-7759. PMID 3542033 |
0.96 |
|
| 1985 |
Bachovchin WW. Confirmation of the assignment of the low-field proton resonance of serine proteases by using specifically nitrogen-15 labeled enzyme Proceedings of the National Academy of Sciences of the United States of America. 82: 7948-7951. PMID 3934665 |
0.96 |
|
| 1984 |
Huang TH, Bachovchin WW, Griffin RG, Dobson CM. High-resolution nitrogen-15 nuclear magnetic resonance studies of α-lytic protease in solid state. Direct comparison of enzyme structure in solution and in the solid state Biochemistry. 23: 5933-5937. PMID 6395886 DOI: 10.1021/bi00320a007 |
0.96 |
|
| 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 |
0.96 |
|
| 1982 |
Westler WM, Markley JL, Bachovchin WW. Proton NRM spectroscopy of the active site histidine of α-lytic proteinase. Effects of adjacent 13C and 15N labels Febs Letters. 138: 233-235. PMID 7040114 DOI: 10.1016/0014-5793(82)80449-3 |
0.96 |
|
| 1982 |
Munowitz M, Bachovchin WW, Herzfeld J, Dobson CM, Griffin RG. Acid-base and tautomeric equilibria in the solid state: 15N NMR spectroscopy of histidine and imidazole Journal of the American Chemical Society. 104: 1192-1196. |
0.96 |
|
| 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 |
0.96 |
|
| 1979 |
Moore KW, Bachovchin WW, Gunter JB, Richards JH. Hydrogen transfer in catalysis by adenosylcobalamin-dependent diol dehydratase. Biochemistry. 18: 2776-82. PMID 383139 |
0.96 |
|
| 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 |
0.96 |
|
| 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 |
0.96 |
|
| 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 |
0.96 |
|
| 1978 |
Bachovchin WW, Roberts JD. Nitrogen-15 nuclear magnetic resonance spectroscopy. The state of histidine in the catalytic triad of α-lytic protease. Implications for the charge-relay mechanism of peptide-bond cleavage by serine proteases Journal of the American Chemical Society. 100: 8041-8047. |
0.96 |
|
| 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 |
0.96 |
|
| 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 |
0.96 |
|
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