Deardorff M, Porter N, Christianson D
Protein Sci. 2016; 25(11):1965-1976.
PMID: 27576763
PMC: 5079251.
DOI: 10.1002/pro.3030.
Lombardi P, Cole K, Dowling D, Christianson D
Curr Opin Struct Biol. 2011; 21(6):735-43.
PMID: 21872466
PMC: 3232309.
DOI: 10.1016/j.sbi.2011.08.004.
Wu S, Zhang C, Xu D, Guo H
J Phys Chem B. 2010; 114(28):9259-67.
PMID: 20583802
PMC: 2920051.
DOI: 10.1021/jp101448j.
Gudmundsson O, Pauletti G, Wang W, Shan D, Zhang H, Wang B
Pharm Res. 1999; 16(1):7-15.
PMID: 9950272
DOI: 10.1023/a:1018828207920.
Camenisch G, Wang W, Wang B, Borchardt R
Pharm Res. 1998; 15(8):1174-81.
PMID: 9706046
DOI: 10.1023/a:1011975404789.
Esterase-sensitive cyclic prodrugs of peptides: evaluation of an acyloxyalkoxy promoiety in a model hexapeptide.
Pauletti G, Gangwar S, Okumu F, Siahaan T, Stella V, Borchardt R
Pharm Res. 1996; 13(11):1615-23.
PMID: 8956324
DOI: 10.1023/a:1016472119387.
Fluxionate Lewis acidity of the Zn2+ ion in carboxypeptidase A.
Mock W, Freeman D, Aksamawati M
Biochem J. 1993; 289 ( Pt 1):185-93.
PMID: 8424757
PMC: 1132148.
DOI: 10.1042/bj2890185.
Binding of ligands to the active site of carboxypeptidase A.
Rees D, Lipscomb W
Proc Natl Acad Sci U S A. 1981; 78(9):5455-9.
PMID: 6946483
PMC: 348764.
DOI: 10.1073/pnas.78.9.5455.
Carboxypeptidase A mechanisms.
Lipscomb W
Proc Natl Acad Sci U S A. 1980; 77(7):3875-8.
PMID: 6933442
PMC: 349729.
DOI: 10.1073/pnas.77.7.3875.
Structure and function of carboxypeptidase A alpha in supercooled water.
Thompson J, Gehring H, Vallee B
Proc Natl Acad Sci U S A. 1980; 77(1):132-6.
PMID: 6928608
PMC: 348222.
DOI: 10.1073/pnas.77.1.132.
Cryospectrokinetic characterization of intermediates in biochemical reactions: carboxypeptidase A.
Auld D, Galdes A, Geoghegan K, Holmquist B, Martinelli R, Vallee B
Proc Natl Acad Sci U S A. 1984; 81(16):5041-5.
PMID: 6591178
PMC: 391633.
DOI: 10.1073/pnas.81.16.5041.
Crystallographic studies on apocarboxypeptidase A and the complex with glycyl-L-tyrosine.
Rees D, Lipscomb W
Proc Natl Acad Sci U S A. 1983; 80(23):7151-4.
PMID: 6580631
PMC: 390011.
DOI: 10.1073/pnas.80.23.7151.
Direct observation of enzyme substrate complexes by stopped-flow fluorescence: mathematical analyses.
Lobb R, Auld D
Experientia. 1984; 40(11):1197-206.
PMID: 6389173
DOI: 10.1007/BF01946647.
The physical state dependence of carboxypeptidase Aalpha and Agamma kinetics.
Spilburg C, BETHUNE J, Vallee B
Proc Natl Acad Sci U S A. 1974; 71(10):3922-6.
PMID: 4530272
PMC: 434298.
DOI: 10.1073/pnas.71.10.3922.
Complex between carboxypeptidase A and a hydrated ketomethylene substrate analogue.
Shoham G, Christianson D, Oren D
Proc Natl Acad Sci U S A. 1988; 85(3):684-8.
PMID: 3422451
PMC: 279619.
DOI: 10.1073/pnas.85.3.684.
Arginyl residues and anion binding sites in proteins.
Riordan J
Mol Cell Biochem. 1979; 26(2):71-92.
PMID: 388184
DOI: 10.1007/BF00232886.
Determination of enzyme mechanisms by radiationless energy transfer kinetics.
Lobb R, Auld D
Proc Natl Acad Sci U S A. 1979; 76(6):2684-8.
PMID: 288055
PMC: 383672.
DOI: 10.1073/pnas.76.6.2684.
Unified picture of mechanisms of catalysis by carboxypeptidase A.
Breslow R, Wernick D
Proc Natl Acad Sci U S A. 1977; 74(4):1303-7.
PMID: 266172
PMC: 430731.
DOI: 10.1073/pnas.74.4.1303.
Intramolecular arsanilazotyrosine-248-Zn complex of carboxypeptidase A: a monitor of catalytic events.
Harrison L, Auld D, Vallee B
Proc Natl Acad Sci U S A. 1975; 72(10):3930-3.
PMID: 671
PMC: 433110.
DOI: 10.1073/pnas.72.10.3930.