Detalles de la búsqueda
1.
A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases.
FEBS Lett
; 296(3): 263-6, 1992 Jan 27.
Artículo
en Inglés
| MEDLINE | ID: mdl-1537400
2.
The second zinc atom in the matrix metalloproteinase catalytic domain is absent in the full-length enzymes: a possible role for the C-terminal domain.
FEBS Lett
; 358(2): 189-92, 1995 Jan 23.
Artículo
en Inglés
| MEDLINE | ID: mdl-7828734
3.
Engineering and the national science foundation.
Science
; 223(4634): 345, 1984 Jan 27.
Artículo
en Inglés
| MEDLINE | ID: mdl-17829874
4.
NBS: Problems and Needs.
Science
; 198(4312): 8, 1977 Oct 07.
Artículo
en Inglés
| MEDLINE | ID: mdl-17741874
5.
Tissue inhibitors of matrix metalloendopeptidases.
Methods Enzymol
; 248: 496-510, 1995.
Artículo
en Inglés
| MEDLINE | ID: mdl-7674941
6.
Regulation of matrix metalloproteinase activity.
Ann N Y Acad Sci
; 732: 31-41, 1994 Sep 06.
Artículo
en Inglés
| MEDLINE | ID: mdl-7978800
7.
Analysis of the interaction of TIMP-2 and MMPs: engineering the changes.
Ann N Y Acad Sci
; 878: 524-7, 1999 Jun 30.
Artículo
en Inglés
| MEDLINE | ID: mdl-10415762
8.
Kinetic analysis of the inhibition of matrix metalloproteinases by tissue inhibitor of metalloproteinases (TIMP).
Methods Mol Biol
; 151: 519-32, 2001.
Artículo
en Inglés
| MEDLINE | ID: mdl-11217325
9.
Chemical evidence for the pH-dependent control of ion-pair geometry in cathepsin B. Benzofuroxan as a reactivity probe sensitive to differences in the mutual disposition of the thiolate and imidazolium components of cysteine proteinase catalytic sites.
Biochem J
; 238(1): 103-7, 1986 Aug 15.
Artículo
en Inglés
| MEDLINE | ID: mdl-3800926
10.
Structure-function relationships in the tissue inhibitors of metalloproteinases.
Am J Respir Crit Care Med
; 150(6 Pt 2): S165-70, 1994 Dec.
Artículo
en Inglés
| MEDLINE | ID: mdl-7952654
11.
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).
Biochem J
; 222(3): 805-14, 1984 Sep 15.
Artículo
en Inglés
| MEDLINE | ID: mdl-6534384
12.
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.
Biochem J
; 227(2): 521-8, 1985 Apr 15.
Artículo
en Inglés
| MEDLINE | ID: mdl-3890831
13.
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.
Biochem J
; 227(2): 511-9, 1985 Apr 15.
Artículo
en Inglés
| MEDLINE | ID: mdl-4004778
14.
A marked gradation in active-centre properties in the cysteine proteinases revealed by neutral and anionic reactivity probes. Reactivity characteristics of the thiol groups of actinidin, ficin, papain and papaya peptidase A towards 4,4'-dipyridyl disulphide and 5,5'-dithiobis-(2-nitrobenzoate) dianion.
Biochem J
; 209(3): 873-9, 1983 Mar 01.
Artículo
en Inglés
| MEDLINE | ID: mdl-6347181
15.
Evidence for a close similarity in the catalytic sites of papain and ficin in near-neutral media despite differences in acidic and alkaline media. Kinetics of the reactions of papain and ficin with chloroacetate.
Biochem J
; 201(1): 101-4, 1982 Jan 01.
Artículo
en Inglés
| MEDLINE | ID: mdl-7044370
16.
Kinetic analysis of the mechanism of interaction of full-length TIMP-2 and gelatinase A: evidence for the existence of a low-affinity intermediate.
Biochemistry
; 37(28): 10094-8, 1998 Jul 14.
Artículo
en Inglés
| MEDLINE | ID: mdl-9665714
17.
Evidence for the importance of weakly bound water for matrix metalloproteinase activity.
Biochemistry
; 34(37): 12012-8, 1995 Sep 19.
Artículo
en Inglés
| MEDLINE | ID: mdl-7547939
18.
Human tissue inhibitor of metalloproteinases 3 interacts with both the N- and C-terminal domains of gelatinases A and B. Regulation by polyanions.
J Biol Chem
; 274(16): 10846-51, 1999 Apr 16.
Artículo
en Inglés
| MEDLINE | ID: mdl-10196161
19.
The use of HPLC-pulsed amperometry for the characterization and assay of glycosidases and glycosyltransferases.
Glycobiology
; 1(2): 223-7, 1991 Mar.
Artículo
en Inglés
| MEDLINE | ID: mdl-1823165
20.
Analysis of the role of the COOH-terminal domain in the activation, proteolytic activity, and tissue inhibitor of metalloproteinase interactions of gelatinase B.
J Biol Chem
; 269(21): 14967-73, 1994 May 27.
Artículo
en Inglés
| MEDLINE | ID: mdl-8195131