Structural and Functional Analysis of the Pro-Domain of Human Cathelicidin, LL-37 - Wikidata - awgldk - TriplyDB

Structural and Functional Analysis of the Pro-Domain of Human Cathelicidin, LL-37

Structural and Functional Analysis of the Pro-Domain of Human Cathelicidin, LL-37

http://www.wikidata.org/entity/Q27676356

about

Antiviral potential of cathelicidins Safety, efficacy and utility of methods of transferring adhesive and cohesive Escherichia coli cells to microplates to avoid aerosols Effect of recombinant prophenin 2 on the integrity and viability of Trichomonas vaginalis Human Cathelicidin Compensates for the Role of Apolipoproteins in Hepatitis C Virus Infectious Particle Formation Antiviral drug discovery: broad-spectrum drugs from nature.Unique features of human cathelicidin LL-37.Structure-Dependent Immune Modulatory Activity of Protegrin-1 Analogs.High-Throughput Quantification of Bacterial-Cell Interactions Using Virtual Colony Counts.

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P2860

Structural and Functional Analysis of the Pro-Domain of Human Cathelicidin, LL-37

http://www.wikidata.org/entity/Q27676356

description

2013 nî lūn-bûn

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2013 թուականի Մարտին հրատարակուած գիտական յօդուած

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2013 թվականի մարտին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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name

Structural and Functional Analysis of the Pro-Domain of Human Cathelicidin, LL-37

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Structural and Functional Analysis of the Pro-Domain of Human Cathelicidin, LL-37

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Structural and Functional Analysis of the Pro-Domain of Human Cathelicidin, LL-37

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type

label

Structural and Functional Analysis of the Pro-Domain of Human Cathelicidin, LL-37

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Structural and Functional Analysis of the Pro-Domain of Human Cathelicidin, LL-37

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Structural and Functional Analysis of the Pro-Domain of Human Cathelicidin, LL-37

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prefLabel

Structural and Functional Analysis of the Pro-Domain of Human Cathelicidin, LL-37

@ast

Structural and Functional Analysis of the Pro-Domain of Human Cathelicidin, LL-37

@en

Structural and Functional Analysis of the Pro-Domain of Human Cathelicidin, LL-37

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Structural and Functional Analysis of the Pro-Domain of Human Cathelicidin, LL-37

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Amy Galliher-Beckley

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Bryan Ericksen

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Changyou Zhan

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Eric Toth

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Guozhang Zou

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Jishu Shi

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Liqiong Lan

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Marzena Pazgier

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Minhua Ling

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

Weirong Yuan

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P2860

Processing of seminal plasma hCAP-18 to ALL-38 by gastricsin: a novel mechanism of generating antimicrobial peptides in vagina

FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis

Antibacterial activity and specificity of the six human {alpha}-defensins

Human alpha-defensins neutralize anthrax lethal toxin and protect against its fatal consequences

The refined 2.4 A X-ray crystal structure of recombinant human stefin B in complex with the cysteine proteinase papain: a novel type of proteinase inhibitor interaction

Sometimes it takes two to tango: contributions of dimerization to functions of human α-defensin HNP1 peptide

MolProbity: all-atom structure validation for macromolecular crystallography

Through the looking glass, mechanistic insights from enantiomeric human defensins

LL-37, the neutrophil granule- and epithelial cell-derived cathelicidin, utilizes formyl peptide receptor-like 1 (FPRL1) as a receptor to chemoattract human peripheral blood neutrophils, monocytes, and T cells

Human CAP18: a novel antimicrobial lipopolysaccharide-binding protein

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10.1021/BI301008R

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9

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52

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Edwin Pozharski

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2013-03-05T00:00:00Z

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235619545

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23406372

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3634326

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