(Q33292279)

English

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

scientific article published in September 2002

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scholarly article

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Europe PubMed Central

PubMed publication ID

25 July 2017

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

1 reference

Europe PubMed Central

PubMed publication ID

25 July 2017

molecular chaperones

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object named as

Alex Y Strongin

6

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author name string

Dmitry V Rozanov

1

1 reference

Europe PubMed Central

PubMed publication ID

25 July 2017

Berhane Ghebrehiwet

2

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Europe PubMed Central

PubMed publication ID

25 July 2017

BorisI Ratnikov

3

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Europe PubMed Central

PubMed publication ID

25 July 2017

Edward Z Monosov

4

1 reference

Europe PubMed Central

PubMed publication ID

25 July 2017

Elena I Deryugina

5

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Europe PubMed Central

PubMed publication ID

25 July 2017

language of work or name

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publication date

1 September 2002

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Europe PubMed Central

PubMed publication ID

25 July 2017

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Europe PubMed Central

PubMed publication ID

25 July 2017

527

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Europe PubMed Central

PubMed publication ID

25 July 2017

1-3

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Europe PubMed Central

PubMed publication ID

25 July 2017

51-57

1 reference

Europe PubMed Central

PubMed publication ID

25 July 2017

Matrix metalloproteinases

1 reference

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Specialized surface protrusions of invasive cells, invadopodia and lamellipodia, have differential MT1-MMP, MMP-2, and TIMP-2 localization

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

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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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Proteolysis and cell migration: creating a path?

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Transmembrane/cytoplasmic domain-mediated membrane type 1-matrix metalloprotease docking to invadopodia is required for cell invasion

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Regulation of membrane-type-1 matrix metalloproteinase activity by its cytoplasmic domain

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Mutation analysis of membrane type-1 matrix metalloproteinase (MT1-MMP). The role of the cytoplasmic tail Cys(574), the active site Glu(240), and furin cleavage motifs in oligomerization, processing, and self-proteolysis of MT1-MMP expressed in brea

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Structure and function of gC1q-R: a multiligand binding cellular protein

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

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Identification of functional domains on gC1Q-R, a cell surface protein that binds to the globular "heads" of C1Q, using monoclonal antibodies and synthetic peptides.

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Determination of matrix metalloproteinase activity using biotinylated gelatin.

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Functional activation of integrin alpha V beta 3 in tumor cells expressing membrane-type 1 matrix metalloproteinase

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MT1-MMP initiates activation of pro-MMP-2 and integrin alphavbeta3 promotes maturation of MMP-2 in breast carcinoma cells

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Site-specific mutagenesis of the human fibroblast interferon gene

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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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Regulation of membrane-type matrix metalloproteinase 1 activity by dynamin-mediated endocytosis

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Oligomerization through hemopexin and cytoplasmic domains regulates the activity and turnover of membrane-type 1 matrix metalloproteinase

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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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Cytoplasmic tail-dependent internalization of membrane-type 1 matrix metalloproteinase is important for its invasion-promoting activity.

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The propeptide domain of membrane type 1-matrix metalloproteinase acts as an intramolecular chaperone when expressed in trans with the mature sequence in COS-1 cells

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Regulation of membrane-type matrix metalloproteinase-1 expression by growth factors and phorbol 12-myristate 13-acetate.

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Crystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix protein

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Protein kinase C [micro] is regulated by the multifunctional chaperon protein p32

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p32 (gC1qBP) is a general protein kinase C (PKC)-binding protein; interaction and cellular localization of P32-PKC complexes in ray hepatocytes

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Interaction of the alpha(1B)-adrenergic receptor with gC1q-R, a multifunctional protein

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Interaction between GABA(A) receptor beta subunits and the multifunctional protein gC1q-R

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Interaction between complement receptor gC1qR and hepatitis C virus core protein inhibits T-lymphocyte proliferation

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P32/TAP, a cellular protein that interacts with EBNA-1 of Epstein-Barr virus.

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10.1016/S0014-5793(02)03153-8

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Europe PubMed Central

PubMed publication ID

25 July 2017

release_6qgy3mfi7re6fhlxbgyhlqkxhm

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https://api.fatcat.wiki/v0/release/6qgy3mfi7re6fhlxbgyhlqkxhm

24 November 2022

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PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

25 July 2017

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