132 related articles for article (PubMed ID: 1310615)
1. Higher-order complex formation between the 72-kilodalton type IV collagenase and tissue inhibitor of metalloproteinases-2.
Kleiner DE; Unsworth EJ; Krutzsch HC; Stetler-Stevenson WG
Biochemistry; 1992 Feb; 31(6):1665-72. PubMed ID: 1310615
[TBL] [Abstract][Full Text] [Related]
2. Interaction of 92-kDa type IV collagenase with the tissue inhibitor of metalloproteinases prevents dimerization, complex formation with interstitial collagenase, and activation of the proenzyme with stromelysin.
Goldberg GI; Strongin A; Collier IE; Genrich LT; Marmer BL
J Biol Chem; 1992 Mar; 267(7):4583-91. PubMed ID: 1311314
[TBL] [Abstract][Full Text] [Related]
3. Inhibition of autoproteolytic activation of interstitial procollagenase by recombinant metalloproteinase inhibitor MI/TIMP-2.
DeClerck YA; Yean TD; Lu HS; Ting J; Langley KE
J Biol Chem; 1991 Feb; 266(6):3893-9. PubMed ID: 1847392
[TBL] [Abstract][Full Text] [Related]
4. Human 72-kilodalton type IV collagenase forms a complex with a tissue inhibitor of metalloproteases designated TIMP-2.
Goldberg GI; Marmer BL; Grant GA; Eisen AZ; Wilhelm S; He CS
Proc Natl Acad Sci U S A; 1989 Nov; 86(21):8207-11. PubMed ID: 2554304
[TBL] [Abstract][Full Text] [Related]
5. Stability analysis of latent and active 72-kDa type IV collagenase: the role of tissue inhibitor of metalloproteinases-2 (TIMP-2).
Kleiner DE; Tuuttila A; Tryggvason K; Stetler-Stevenson WG
Biochemistry; 1993 Feb; 32(6):1583-92. PubMed ID: 8431437
[TBL] [Abstract][Full Text] [Related]
6. Domain structure of human 72-kDa gelatinase/type IV collagenase. Characterization of proteolytic activity and identification of the tissue inhibitor of metalloproteinase-2 (TIMP-2) binding regions.
Fridman R; Fuerst TR; Bird RE; Hoyhtya M; Oelkuct M; Kraus S; Komarek D; Liotta LA; Berman ML; Stetler-Stevenson WG
J Biol Chem; 1992 Aug; 267(22):15398-405. PubMed ID: 1322396
[TBL] [Abstract][Full Text] [Related]
7. The complex between a tissue inhibitor of metalloproteinases (TIMP-2) and 72-kDa progelatinase is a metalloproteinase inhibitor.
Kolkenbrock H; Orgel D; Hecker-Kia A; Noack W; Ulbrich N
Eur J Biochem; 1991 Jun; 198(3):775-81. PubMed ID: 1646720
[TBL] [Abstract][Full Text] [Related]
8. Cellular activation of the 72 kDa type IV procollagenase/TIMP-2 complex.
Brown PD; Kleiner DE; Unsworth EJ; Stetler-Stevenson WG
Kidney Int; 1993 Jan; 43(1):163-70. PubMed ID: 8433556
[TBL] [Abstract][Full Text] [Related]
9. TIMP-2: identification and characterization of a new member of the metalloproteinase inhibitor family.
Stetler-Stevenson WG; Krutzsch HC; Liotta LA
Matrix Suppl; 1992; 1():299-306. PubMed ID: 1480041
[TBL] [Abstract][Full Text] [Related]
10. Secreted inhibitors of metalloproteinases (IMPs) that are distinct from TIMP.
Banda MJ; Howard EW; Herron GS; Apodaca G
Matrix Suppl; 1992; 1():294-8. PubMed ID: 1480040
[TBL] [Abstract][Full Text] [Related]
11. Tumor cell invasion inhibited by TIMP-2.
Albini A; Melchiori A; Santi L; Liotta LA; Brown PD; Stetler-Stevenson WG
J Natl Cancer Inst; 1991 Jun; 83(11):775-9. PubMed ID: 1645772
[TBL] [Abstract][Full Text] [Related]
12. Human 92- and 72-kilodalton type IV collagenases are elastases.
Senior RM; Griffin GL; Fliszar CJ; Shapiro SD; Goldberg GI; Welgus HG
J Biol Chem; 1991 Apr; 266(12):7870-5. PubMed ID: 1850424
[TBL] [Abstract][Full Text] [Related]
13. The enzymatic evaluation of procollagenase and collagenase inhibitors in crude biological media.
Lefebvre V; Vaes G
Biochim Biophys Acta; 1989 Sep; 992(3):355-61. PubMed ID: 2550082
[TBL] [Abstract][Full Text] [Related]
14. The purification of tissue inhibitor of metalloproteinases-2 from its 72 kDa progelatinase complex. Demonstration of the biochemical similarities of tissue inhibitor of metalloproteinases-2 and tissue inhibitor of metalloproteinases-1.
Ward RV; Hembry RM; Reynolds JJ; Murphy G
Biochem J; 1991 Aug; 278 ( Pt 1)(Pt 1):179-87. PubMed ID: 1909113
[TBL] [Abstract][Full Text] [Related]
15. Preparation of active recombinant TIMP-1 from Escherichia coli inclusion bodies and complex formation with the recombinant catalytic domain of PMNL-collagenase.
Kleine T; Bartsch S; Bläser J; Schnierer S; Triebel S; Valentin M; Gote T; Tschesche H
Biochemistry; 1993 Dec; 32(51):14125-31. PubMed ID: 8260495
[TBL] [Abstract][Full Text] [Related]
16. Purification and characterization of a two-chain form of tissue inhibitor of metalloproteinases (TIMP) type 2 and a low molecular weight TIMP-like protein.
Miyazaki K; Funahashi K; Numata Y; Koshikawa N; Akaogi K; Kikkawa Y; Yasumitsu H; Umeda M
J Biol Chem; 1993 Jul; 268(19):14387-93. PubMed ID: 8314798
[TBL] [Abstract][Full Text] [Related]
17. Mosaic structure of the secreted ECM metalloproteases and interaction of the type IV collagenases with inhibitors.
Goldberg GI; Collier IE; Eisen AZ; Grant GA; Marmer BL; Wilhelm SM
Matrix Suppl; 1992; 1():25-30. PubMed ID: 1336109
[TBL] [Abstract][Full Text] [Related]
18. Immunoassays for the detection of human collagenase, stromelysin, tissue inhibitor of metalloproteinases (TIMP) and enzyme-inhibitor complexes.
Cooksley S; Hipkiss JB; Tickle SP; Holmes-Ievers E; Docherty AJ; Murphy G; Lawson AD
Matrix; 1990 Oct; 10(5):285-91. PubMed ID: 1964712
[TBL] [Abstract][Full Text] [Related]
19. Identification of a new metalloproteinase inhibitor that forms tight-binding complexes with collagenase.
Cawston TE; Curry VA; Clark IM; Hazleman BL
Biochem J; 1990 Jul; 269(1):183-7. PubMed ID: 2165393
[TBL] [Abstract][Full Text] [Related]
20. Low molecular weight, sequence based, collagenase inhibitors selectively block the interaction between collagenase and TIMP (tissue inhibitor of metalloproteinases).
Lelièvre Y; Bouboutou R; Boiziau J; Faucher D; Achard D; Cartwright T
Matrix; 1990 Oct; 10(5):292-9. PubMed ID: 1964713
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]