Literature DB >> 9138283

Relating matrix metalloproteinase structure to function: why the "hemopexin" domain?

G Murphy1, V Knäuper.   

Abstract

Matrix metalloproteinases are thought to be key players in the remodelling activity of cells associated with both physiological and pathological processes. They share a relatively conserved structure with a number of identifiable modules linked to their specific functions. The structure of the individual domains of a number of matrix metalloproteinases have now been elucidated. Here we review these data in the light of complementary studies on the behaviour of these enzymes in biological systems. In particular we focus on the C-terminal hemopexin-like domain which has intriguingly specific roles in individual matrix metalloproteinases.

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Year:  1997        PMID: 9138283     DOI: 10.1016/s0945-053x(97)90025-1

Source DB:  PubMed          Journal:  Matrix Biol        ISSN: 0945-053X            Impact factor:   11.583


  45 in total

Review 1.  A case of tumor betrayal: biphasic effects of TIMP-1 on Burkitt's lymphoma.

Authors:  L Yan; M A Moses
Journal:  Am J Pathol       Date:  2001-04       Impact factor: 4.307

Review 2.  Matrix metalloproteinase biology applied to vitreoretinal disorders.

Authors:  C S Sethi; T A Bailey; P J Luthert; N H Chong
Journal:  Br J Ophthalmol       Date:  2000-06       Impact factor: 4.638

3.  Substrate recognition by gelatinase A: the C-terminal domain facilitates surface diffusion.

Authors:  I E Collier; S Saffarian; B L Marmer; E L Elson; G Goldberg
Journal:  Biophys J       Date:  2001-10       Impact factor: 4.033

Review 4.  Clinical implications of matrix metalloproteinases.

Authors:  Malay Mandal; Amritlal Mandal; Sudip Das; Tapati Chakraborti; Chakraborti Sajal
Journal:  Mol Cell Biochem       Date:  2003-10       Impact factor: 3.396

Review 5.  Structural basis of matrix metalloproteinases and tissue inhibitors of metalloproteinases.

Authors:  Klaus Maskos; Wolfram Bode
Journal:  Mol Biotechnol       Date:  2003-11       Impact factor: 2.695

6.  Matrix metalloproteinase 9 gene polymorphisms are associated with a multiple family history of gastric cancer.

Authors:  Rieko Okada; Mariko Naito; Yuta Hattori; Toshio Seiki; Kenji Wakai; Hinako Nanri; Miki Watanabe; Sadao Suzuki; Tara Sefanya Kairupan; Naoyuki Takashima; Haruo Mikami; Keizo Ohnaka; Yoshiyuki Watanabe; Sakurako Katsuura-Kamano; Michiaki Kubo; Nobuyuki Hamajima; Hideo Tanaka
Journal:  Gastric Cancer       Date:  2016-04-06       Impact factor: 7.370

7.  Interaction of lubricin with type II collagen surfaces: adsorption, friction, and normal forces.

Authors:  Debby P Chang; Farshid Guilak; Gregory D Jay; Stefan Zauscher
Journal:  J Biomech       Date:  2013-12-11       Impact factor: 2.712

8.  Inhibition of matrix metalloproteinases suppresses the migration of skeletal muscle cells.

Authors:  Takanori Nishimura; Kazuki Nakamura; Yasuhiro Kishioka; Yuko Kato-Mori; Jun-ichi Wakamatsu; Akihito Hattori
Journal:  J Muscle Res Cell Motil       Date:  2008-06-19       Impact factor: 2.698

9.  Course of matrix metalloproteinase-9 isoforms after the administration of uric acid in patients with acute stroke: a proof-of-concept study.

Authors:  Sergio Amaro; Víctor Obach; Alvaro Cervera; Xabier Urra; Manuel Gómez-Choco; Anna M Planas; Angel Chamorro
Journal:  J Neurol       Date:  2009-04-27       Impact factor: 4.849

10.  Bone sialoprotein does not interact with pro-gelatinase A (MMP-2) or mediate MMP-2 activation.

Authors:  Queena Hwang; Sela Cheifetz; Christopher M Overall; Christopher A McCulloch; Jaro Sodek
Journal:  BMC Cancer       Date:  2009-04-22       Impact factor: 4.430

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