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Table representation of search results timeline featuring number of search results per year.

Year Number of Results
1930 1
1935 2
1938 1
1940 2
1942 1
1957 1
1958 2
1961 1
1964 4
1965 7
1966 3
1967 4
1968 4
1969 6
1970 4
1971 5
1972 5
1973 13
1974 14
1975 11
1976 23
1977 13
1978 16
1979 15
1980 26
1981 21
1982 24
1983 25
1984 24
1985 25
1986 18
1987 23
1988 24
1989 17
1990 14
1991 23
1992 28
1993 11
1994 18
1995 14
1996 12
1997 15
1998 14
1999 11
2000 10
2001 11
2002 5
2003 11
2004 6
2005 1
2006 1
2007 4
2008 5
2009 6
2010 2
2011 2
2012 1
2015 2
2016 2
2017 1
2018 2
2019 2
2020 6
2021 4
2022 4
2024 0

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Similar articles for PMID: 3890831

624 results

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Page 1
A general framework of cysteine-proteinase mechanism deduced from studies on enzymes with structurally different analogous catalytic-site residues Asp-158 and -161 (papain and actinidin), Gly-196 (cathepsin B) and Asn-165 (cathepsin H). Kinetic studies up to pH 8 of the hydrolysis of N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide catalysed by cathepsin B and of L-arginine 2-naphthylamide catalysed by cathepsin H.
Willenbrock F, Brocklehurst K. Willenbrock F, et al. Biochem J. 1985 Apr 15;227(2):521-8. doi: 10.1042/bj2270521. Biochem J. 1985. PMID: 3890831 Free PMC article.
Natural structural variation in enzymes as a tool in the study of mechanism exemplified by a comparison of the catalytic-site structure and characteristics of cathepsin B and papain. pH-dependent kinetics of the reactions of cathepsin B from bovine spleen and from rat liver with a thiol-specific two-protonic-state probe (2,2'-dipyridyl disulphide) and with a specific synthetic substrate (N-alpha-benzyloxycarbonyl-L-arginyl-L-arginine 2-naphthylamide).
Willenbrock F, Brocklehurst K. Willenbrock F, et al. Biochem J. 1984 Sep 15;222(3):805-14. doi: 10.1042/bj2220805. Biochem J. 1984. PMID: 6534384 Free PMC article.
Preparation of cathepsins B and H by covalent chromatography and characterization of their catalytic sites by reaction with a thiol-specific two-protonic-state reactivity probe. Kinetic study of cathepsins B and H extending into alkaline media and a rapid spectroscopic titration of cathepsin H at pH 3-4.
Willenbrock F, Brocklehurst K. Willenbrock F, et al. Biochem J. 1985 Apr 15;227(2):511-9. doi: 10.1042/bj2270511. Biochem J. 1985. PMID: 4004778 Free PMC article.
Differences in the chemical and catalytic characteristics of two crystallographically 'identical' enzyme catalytic sites. Characterization of actinidin and papain by a combination of pH-dependent substrate catalysis kinetics and reactivity probe studies targeted on the catalytic-site thiol group and its immediate microenvironment.
Salih E, Malthouse JP, Kowlessur D, Jarvis M, O'Driscoll M, Brocklehurst K. Salih E, et al. Biochem J. 1987 Oct 1;247(1):181-93. doi: 10.1042/bj2470181. Biochem J. 1987. PMID: 2825655 Free PMC article.
Investigation of the catalytic site of actinidin by using benzofuroxan as a reactivity probe with selectivity for the thiolate-imidazolium ion-pair systems of cysteine proteinases. Evidence that the reaction of the ion-pair of actinidin (pKI 3.0, pKII 9.6) is modulated by the state of ionization of a group associated with a molecular pKa of 5.5.
Salih E, Brocklehurst K. Salih E, et al. Biochem J. 1983 Sep 1;213(3):713-8. doi: 10.1042/bj2130713. Biochem J. 1983. PMID: 6311173 Free PMC article.
624 results