Activation and proteolytic activity of the Treponema pallidum metalloprotease, pallilysin. - Test2 - elhamkhani - TriplyDB

Activation and proteolytic activity of the Treponema pallidum metalloprotease, pallilysin.

Activation and proteolytic activity of the Treponema pallidum metalloprotease, pallilysin.

http://www.wikidata.org/entity/Q34387058

about

Current status of syphilis vaccine development: need, challenges, prospects Structural characterization of zinc-bound Zmp1, a zinc-dependent metalloprotease secreted by Clostridium difficile Identification of Tp0751 (Pallilysin) as a Treponema pallidum Vascular Adhesin by Heterologous Expression in the Lyme disease Spirochete.The Structure of Treponema pallidum Tp0751 (Pallilysin) Reveals a Non-canonical Lipocalin Fold That Mediates Adhesion to Extracellular Matrix Components and Interactions with Host Cells.Conservation of the Host-Interacting Proteins Tp0750 and Pallilysin among Treponemes and Restriction of Proteolytic Capacity to Treponema pallidum.Reduced Treponema pallidum-Specific Opsonic Antibody Activity in HIV-Infected Patients With Syphilis.Thrombin Cleavage of Plasmodium falciparum Erythrocyte Membrane Protein 1 Inhibits Cytoadherence.A defined syphilis vaccine candidate inhibits dissemination of Treponema pallidum subspecies pallidum.The multifunctional role of the pallilysin-associated Treponema pallidum protein, Tp0750, in promoting fibrinolysis and extracellular matrix component degradation Pathogenic Leptospira Secreted Proteases Target the Membrane Attack Complex: A Potential Role for Thermolysin in Complement Inhibition.Treponema pallidum, the syphilis spirochete: making a living as a stealth pathogen.Evaluation of two novel leptospiral proteins for their interaction with human host components.The Treponema pallidum Outer Membrane.Vaccine development for syphilis.IFNγ Enhances CD64-Potentiated Phagocytosis of Treponema pallidum Opsonized with Human Syphilitic Serum by Human Macrophages Leptospira interrogans Secreted Proteases Degrade Extracellular Matrix and Plasma Proteins From the Host.

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P2860

Activation and proteolytic activity of the Treponema pallidum metalloprotease, pallilysin.

http://www.wikidata.org/entity/Q34387058

description

2012 nî lūn-bûn

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2012 թուականի Յուլիսին հրատարակուած գիտական յօդուած

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2012年の論文

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2012年学术文章

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Activation and proteolytic act ...... m metalloprotease, pallilysin.

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Activation and proteolytic act ...... m metalloprotease, pallilysin.

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Activation and proteolytic act ...... m metalloprotease, pallilysin.

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Activation and proteolytic act ...... m metalloprotease, pallilysin.

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Activation and proteolytic act ...... m metalloprotease, pallilysin.

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Activation and proteolytic act ...... m metalloprotease, pallilysin.

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Activation and proteolytic act ...... m metalloprotease, pallilysin.

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JOURNAL.PPAT.1002822

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Activation and proteolytic act ...... m metalloprotease, pallilysin.

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Caroline E Cameron

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Julia Hassler

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Lisa Honeyman

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Rebecca Hof

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Simon Houston

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P2860

Complete Genome Sequence of Treponema pallidum, the Syphilis Spirochete

The Transition from Closed to Open Conformation of Treponema pallidum Outer Membrane-associated Lipoprotein TP0453 Involves Membrane Sensing and Integration by Two Amphipathic Helices

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'

Fibrinogen and fibrin

Protein identification and analysis tools in the ExPASy server

TP0326, a Treponema pallidum β-barrel assembly machinery A (BamA) orthologue and rare outer membrane protein

The omptin family of enterobacterial surface proteases/adhesins: from housekeeping in Escherichia coli to systemic spread of Yersinia pestis.

Proteus mirabilis ZapA metalloprotease degrades a broad spectrum of substrates, including antimicrobial peptides

Pathogen entrapment by transglutaminase--a conserved early innate immune mechanism.

Cellular architecture of Treponema pallidum: novel flagellum, periplasmic cone, and cell envelope as revealed by cryo electron tomography.

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10.1371/JOURNAL.PPAT.1002822

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