Non-proteolytic, receptor/ligand interactions associate cellular membrane type-1 matrix metalloproteinase with the complement component C1q. (Q46617653)

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scientific article published on 16 September 2004

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English	Non-proteolytic, receptor/ligand interactions associate cellular membrane type-1 matrix metalloproteinase with the complement component C1q.	scientific article published on 16 September 2004

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/15375167

Non-proteolytic, receptor/ligand interactions associate cellular membrane type-1 matrix metalloproteinase with the complement component C1q. (English)

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/15375167

1 reference

based on heuristic

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3

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/15375167

8

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Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/15375167

author name string

Dmitri V Rozanov

1

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Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/15375167

Sergey Sikora

2

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/15375167

Tatiana I Postnova

4

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/15375167

Vladislav Golubkov

5

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/15375167

Alexei Savinov

6

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/15375167

Stephen Tomlinson

7

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Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/15375167

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publication date

16 September 2004

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Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/15375167

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/15375167

279

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Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/15375167

48

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Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/15375167

50321-50328

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/15375167

New functions for the matrix metalloproteinases in cancer progression

1 reference

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Membrane type-matrix metalloproteinases (MT-MMP)

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Control of the complement system.

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C1q: structure, function, and receptors

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Structural biology of the C1 complex of complement unveils the mechanisms of its activation and proteolytic activity

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Recent progress in the understanding of the structure-function relationships of the globular head regions of C1q.

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X-ray structure of the Ca2+-binding interaction domain of C1s. Insights into the assembly of the C1 complex of complement

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21 January 2018

The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties

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21 January 2018

Role of the C5b-9 complement complex in cell cycle and apoptosis

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cC1q-R (calreticulin) and gC1q-R/p33: ubiquitously expressed multi-ligand binding cellular proteins involved in inflammation and infection

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Determination of matrix metalloproteinase activity using biotinylated gelatin.

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21 January 2018

The cytoplasmic tail peptide sequence of membrane type-1 matrix metalloproteinase (MT1-MMP) directly binds to gC1qR, a compartment-specific chaperone-like regulatory protein

1 reference

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21 January 2018

Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease

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21 January 2018

An alternative processing of integrin alpha(v) subunit in tumor cells by membrane type-1 matrix metalloproteinase

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21 January 2018

The low density lipoprotein receptor-related protein LRP is regulated by membrane type-1 matrix metalloproteinase (MT1-MMP) proteolysis in malignant cells

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21 January 2018

The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor

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21 January 2018

Combination of multiple alignment analysis and surface mapping paves a way for a detailed pathway reconstruction--the case of VHL (von Hippel-Lindau) protein and angiogenesis regulatory pathway

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Molecular surface recognition: determination of geometric fit between proteins and their ligands by correlation techniques

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Aberrant, persistent inclusion into lipid rafts limits the tumorigenic function of membrane type-1 matrix metalloproteinase in malignant cells

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21 January 2018

Membrane type-1 matrix metalloproteinase functions as a proprotein self-convertase. Expression of the latent zymogen in Pichia pastoris, autolytic activation, and the peptide sequence of the cleavage forms

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21 January 2018

The hemopexin-like C-terminal domain of membrane type 1 matrix metalloproteinase regulates proteolysis of a multifunctional protein, gC1qR

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21 January 2018

Regulation of membrane type-matrix metalloproteinases

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21 January 2018

The serpin alpha1-proteinase inhibitor is a critical substrate for gelatinase B/MMP-9 in vivo.

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21 January 2018

Prinomastat, a hydroxamate inhibitor of matrix metalloproteinases, has a complex effect on migration of breast carcinoma cells

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Prointegrin maturation follows rapid trafficking and processing of MT1-MMP in Furin-Negative Colon Carcinoma LoVo Cells

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Complex pattern of membrane type 1 matrix metalloproteinase shedding. Regulation by autocatalytic cells surface inactivation of active enzyme

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Binding of active (57 kDa) membrane type 1-matrix metalloproteinase (MT1-MMP) to tissue inhibitor of metalloproteinase (TIMP)-2 regulates MT1-MMP processing and pro-MMP-2 activation.

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Membrane-type 1 matrix metalloproteinase: a key enzyme for tumor invasion

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Matrix-dependent proteolysis of surface transglutaminase by membrane-type metalloproteinase regulates cancer cell adhesion and locomotion.

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Constitutive and induced CD44 shedding by ADAM-like proteases and membrane-type 1 matrix metalloproteinase.

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Crystal structure of the complex formed by the membrane type 1-matrix metalloproteinase with the tissue inhibitor of metalloproteinases-2, the soluble progelatinase A receptor

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Clusterin, an abundant serum factor, is a possible negative regulator of MT6-MMP/MMP-25 produced by neutrophils.

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Identifiers

10.1074/JBC.M409174200

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/15375167

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

23 December 2017

http://europepmc.org/abstract/MED/15375167

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