Relating matrix metalloproteinase structure to function: why the "hemopexin" domain? (Q41460643)

1 October 2017

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title

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

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1 October 2017

Murphy G

1

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1 October 2017

Knäuper V

series ordinal

2

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1 October 2017

publication date

1 March 1997

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1 October 2017

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1 October 2017

volume

15

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1 October 2017

issue

8-9

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1 October 2017

page(s)

511-518

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Intermolecular autolytic cleavage can contribute to the activation of progelatinase A by cell membranes

1 October 2017

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Stromelysin-1: three-dimensional structure of the inhibited catalytic domain and of the C-truncated proenzyme

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The AP-1 site and MMP gene regulation: what is all the fuss about?

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A helping hand for collagenases: the haemopexin-like domain

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Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'

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7 January 2021

Cellular activation of the 72 kDa type IV procollagenase/TIMP-2 complex

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Fragments of human fibroblast collagenase. Purification and characterization

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7 January 2021

Human progelatinase A can be activated by autolysis at a rate that is concentration-dependent and enhanced by heparin bound to the C-terminal domain

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7 January 2021

The C-terminal (haemopexin-like) domain structure of human gelatinase A (MMP2): structural implications for its function

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The helping hand of collagenase-3 (MMP-13): 2.7 A crystal structure of its C-terminal haemopexin-like domain

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Fragmentation of human polymorphonuclear-leucocyte collagenase

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Cellular mechanisms for human procollagenase-3 (MMP-13) activation. Evidence that MT1-MMP (MMP-14) and gelatinase a (MMP-2) are able to generate active enzyme

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7 January 2021

The role of the C-terminal domain of human collagenase-3 (MMP-13) in the activation of procollagenase-3, substrate specificity, and tissue inhibitor of metalloproteinase interaction

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7 January 2021

Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed beta-propeller

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7 January 2021

Crystal structure of the haemopexin-like C-terminal domain of gelatinase A

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7 January 2021

Structure of the catalytic domain of fibroblast collagenase complexed with an inhibitor

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7 January 2021

30 Tissue inhibitors of matrix metalloendopeptidases

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7 January 2021

Different domain interactions are involved in the binding of tissue inhibitors of metalloproteinases to stromelysin-1 and gelatinase A

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7 January 2021

Membrane type 1 matrix metalloproteinase digests interstitial collagens and other extracellular matrix macromolecules

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7 January 2021

Furin-dependent intracellular activation of the human stromelysin-3 zymogen

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7 January 2021

Transmembrane-deletion mutants of the membrane-type matrix metalloproteinase-1 process progelatinase A and express intrinsic matrix-degrading activity

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7 January 2021

Complex roles of matrix metalloproteinases in tumor progression.

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7 January 2021

Evolutionary families of metallopeptidases

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7 January 2021

Structural implications for the role of the N terminus in the ‘superactivation’ of collagenases

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7 January 2021

Proteolytic processing mechanisms in the biosynthesis of neuroendocrine peptides: the subtilisin-like proprotein convertases.

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7 January 2021

Extracellular matrix binding properties of recombinant fibronectin type II-like modules of human 72-kDa gelatinase/type IV collagenase. High affinity binding to native type I collagen but not native type IV collagen

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7 January 2021

The metzincins — Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc‐peptidases

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7 January 2021

The mechanism of inhibition of collagenase by TIMP-1.

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7 January 2021

Cell surface-mediated activation of progelatinase A: demonstration of the involvement of the C-terminal domain of progelatinase A in cell surface binding and activation of progelatinase A by primary fibroblasts

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7 January 2021

The soluble catalytic domain of membrane type 1 matrix metalloproteinase cleaves the propeptide of progelatinase A and initiates autoproteolytic activation. Regulation by TIMP-2 and TIMP-3.

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7 January 2021

Structure-function relationships in the tissue inhibitors of metalloproteinases

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7 January 2021

The activity of the tissue inhibitors of metalloproteinases is regulated by C-terminal domain interactions: a kinetic analysis of the inhibition of gelatinase A.

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7 January 2021

10.1016/S0945-053X(97)90025-1

Identifiers

DOI

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1 October 2017

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