Inhibition of the tumor necrosis factor-alpha-converting enzyme by its pro domain. - Wikidata - wikimedia - TriplyDB

Inhibition of the tumor necrosis factor-alpha-converting enzyme by its pro domain.

Inhibition of the tumor necrosis factor-alpha-converting enzyme by its pro domain.

http://www.wikidata.org/entity/Q44853351

about

MMP13 mutation causes spondyloepimetaphyseal dysplasia, Missouri type (SEMD(MO)Processing of Snake Venom Metalloproteinases: Generation of Toxin Diversity and Enzyme Inactivation A Disintegrin and Metalloprotease (ADAM): Historical Overview of Their Functions The structure of the catalytic domain of Tannerella forsythia karilysin reveals it is a bacterial xenologue of animal matrix metalloproteinases A Disintegrin and Metalloprotease 17 in the Cardiovascular and Central Nervous Systems The transmembrane domain of TACE regulates protein ectodomain shedding A biosensor for the activity of the "sheddase" TACE (ADAM17) reveals novel and cell type-specific mechanisms of TACE activation Cross-domain inhibition of TACE ectodomain Ectodomain Shedding by ADAM17: Its Role in Neutrophil Recruitment and the Impairment of This Process during Sepsis ADAM-17: the enzyme that does it all.Alternative mRNA splicing generates two distinct ADAM12 prodomain variants.The ADAMs family of proteases: new biomarkers and therapeutic targets for cancer?ADAM9 inhibition increases membrane activity of ADAM10 and controls α-secretase processing of amyloid precursor protein Inhibitory role of TACE/ADAM17 cytotail in protein ectodomain shedding The Functional Maturation of A Disintegrin and Metalloproteinase (ADAM) 9, 10, and 17 Requires Processing at a Newly Identified Proprotein Convertase (PC) Cleavage Site.Regulated surface expression and shedding support a dual role for semaphorin 4D in platelet responses to vascular injury Fluorescent Analogue of Batimastat Enables Imaging of α-Secretase in Living Cells Molecular mechanisms of soluble cytokine receptor generation.Application of structural dynamic approaches provide novel insights into the enzymatic mechanism of the tumor necrosis factor-alpha-converting enzyme Regulation of mature ADAM17 by redox agents for L-selectin shedding Harnessing the natural inhibitory domain to control TNFα Converting Enzyme (TACE) activity in vivo.Tumor necrosis factor-alpha-converting enzyme activities and tumor-associated macrophages in breast cancer.Clinical implications of compounds designed to inhibit ECM-modifying metalloproteinases.Propeptides as modulators of functional activity of proteases.Reactive oxygen species and p38 mitogen-activated protein kinase mediate tumor necrosis factor α-converting enzyme (TACE/ADAM-17) activation in primary human monocytes.Fine Tuning Cell Migration by a Disintegrin and Metalloproteinases.Heparan sulfate regulates ADAM12 through a molecular switch mechanism.Regulation of ADAMTS9 secretion and enzymatic activity by its propeptide.Amino-terminal TACE prodomain attenuates TNFR2 cleavage independently of the cysteine switch.A novel mechanism of latency in matrix metalloproteinases.Chaperone-like properties of the prodomain of TNFalpha-converting enzyme (TACE) and the functional role of its cysteine switch.Recent Advances in ADAM17 Research: A Promising Target for Cancer and Inflammation.Fell-Muir Lecture: Metalloproteinases: from demolition squad to master regulators.Reactive site mutations in tissue inhibitor of metalloproteinase-3 disrupt inhibition of matrix metalloproteinases but not tumor necrosis factor-alpha-converting enzyme.Substitution of methionine 435 with leucine, isoleucine, and serine in tumor necrosis factor alpha converting enzyme inactivates ectodomain shedding activity.ADAM12 Is a Four-leafed Clover Specific inhibition of ADAM17/TACE promotes neurogenesis in the injured motor cortex

P2860

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P2860

Inhibition of the tumor necrosis factor-alpha-converting enzyme by its pro domain.

http://www.wikidata.org/entity/Q44853351

description

2004 nî lūn-bûn

@nan

2004年の論文

@ja

2004年学术文章

@wuu

2004年学术文章

@zh

2004年学术文章

@zh-cn

2004年学术文章

@zh-hans

2004年学术文章

@zh-my

2004年学术文章

@zh-sg

2004年學術文章

@yue

2004年學術文章

@zh-hant

name

Inhibition of the tumor necrosis factor-alpha-converting enzyme by its pro domain.

@en

Inhibition of the tumor necrosis factor-alpha-converting enzyme by its pro domain.

@nl

type

label

Inhibition of the tumor necrosis factor-alpha-converting enzyme by its pro domain.

@en

Inhibition of the tumor necrosis factor-alpha-converting enzyme by its pro domain.

@nl

prefLabel

Inhibition of the tumor necrosis factor-alpha-converting enzyme by its pro domain.

@en

Inhibition of the tumor necrosis factor-alpha-converting enzyme by its pro domain.

@nl

P1433

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P2860

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P698

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P356

P1433

Journal of Biological Chemistry

P1476

Inhibition of the tumor necrosis factor-alpha-converting enzyme by its pro domain.

@en

P2093

Ann B Miller

http://www.w3.org/2001/XMLSchema#string

Ariel Solomon

http://www.w3.org/2001/XMLSchema#string

Irit Sagi

http://www.w3.org/2001/XMLSchema#string

M Anthony Leesnitzer

http://www.w3.org/2001/XMLSchema#string

Marcos E Milla

http://www.w3.org/2001/XMLSchema#string

Patricia E Gonzales

http://www.w3.org/2001/XMLSchema#string

P2860

Metalloprotease-disintegrin MDC9: intracellular maturation and catalytic activity

Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha

Cloning and characterization of ADAM28: evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28

The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family

ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions

Crystal structure of the catalytic domain of human tumor necrosis factor-alpha-converting enzyme

Structure of human pro-matrix metalloproteinase-2: activation mechanism revealed

A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells

Catalytic activity of human ADAM33

The C-terminal domains of TACE weaken the inhibitory action of N-TIMP-3

P304

31638-31645

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P31

scholarly article

P356

10.1074/JBC.M401311200

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P407

P433

30

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P478

279

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P577

2004-04-20T00:00:00Z

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P698

15100227

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