The perforin pore facilitates the delivery of cationic cargos. - Test2 - elhamkhani - TriplyDB

The perforin pore facilitates the delivery of cationic cargos.

The perforin pore facilitates the delivery of cationic cargos.

http://www.wikidata.org/entity/Q37691703

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Human antimicrobial peptides and proteins Perforin competent CD8 T cells are sufficient to cause immune-mediated blood-brain barrier disruption.Analysis of Perforin Assembly by Quartz Crystal Microbalance Reveals a Role for Cholesterol and Calcium-independent Membrane Binding.Granzyme K-deficient mice show no evidence of impaired antiviral immunity.The mystery behind membrane insertion: a review of the complement membrane attack complex Finding a Balance between Protection and Pathology: The Dual Role of Perforin in Human Disease.Transduction Methods for Cytosolic Delivery of Proteins and Bioconjugates into Living Cells.The Membrane Attack Complex/Perforin Superfamily.Perforin Promotes Amyloid Beta Internalisation in Neurons.

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P2860

The perforin pore facilitates the delivery of cationic cargos.

http://www.wikidata.org/entity/Q37691703

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

@tr

scientific article published on 20 February 2014

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

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vědecký článek

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name

The perforin pore facilitates the delivery of cationic cargos.

@en

The perforin pore facilitates the delivery of cationic cargos.

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type

label

The perforin pore facilitates the delivery of cationic cargos.

@en

The perforin pore facilitates the delivery of cationic cargos.

@nl

prefLabel

The perforin pore facilitates the delivery of cationic cargos.

@en

The perforin pore facilitates the delivery of cationic cargos.

@nl

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JBC.M113.544890

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Journal of Biological Chemistry

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The perforin pore facilitates the delivery of cationic cargos.

@en

P2093

Antony Y Matthews

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Michelle A Dunstone

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

Stephanie C Kondos

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P2860

Human perforin employs different avenues to damage membranes

NMR characterization of the interaction between the C-terminal domain of interferon-gamma and heparin-derived oligosaccharides

Perforin pores in the endosomal membrane trigger the release of endocytosed granzyme B into the cytosol of target cells.

Cytotoxic T lymphocyte granules are secretory lysosomes, containing both perforin and granzymes

The major human and mouse granzymes are structurally and functionally divergent

Ratcheting up protein translocation with anthrax toxin

Crystal structure of the caspase activator human granzyme B, a proteinase highly specific for an Asp-P1 residue

The three-dimensional structure of human granzyme B compared to caspase-3, key mediators of cell death with cleavage specificity for aspartic acid in P1

Granulysin crystal structure and a structure-derived lytic mechanism

The structural basis for membrane binding and pore formation by lymphocyte perforin

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9172-9181

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scholarly article

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10.1074/JBC.M113.544890

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13

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289

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James C. Whisstock

Joseph A Trapani

Michael E D'Angelo

Sarah E Stewart

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2014-02-20T00:00:00Z

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24558045

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3979413

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