Linkage of bacterial protein synthesis and presentation of MHC class I-restricted Listeria monocytogenes-derived antigenic peptides (Q28731374)

1

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Simone Schenk

2

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Andreas Bubert

3

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Gernot Geginat

Creative Commons Attribution 4.0 International

4

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language of work or name

English

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publication date

2012

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published in

PLOS One

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volume

7

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issue

3

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page(s)

e33335

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copyright license

start time

12 March 2012

1 reference

April 2022 Public Data File from Crossref

copyright status

copyrighted

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cites work

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Tight linkage between translation and MHC class I peptide ligand generation implies specialized antigen processing for defective ribosomal products

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Protein synthesis upon acute nutrient restriction relies on proteasome function

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Enhanced intracellular dissociation of major histocompatibility complex class I-associated peptides: a mechanism for optimizing the spectrum of cell surface-presented cytotoxic T lymphocyte epitopes.

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Role of tripeptidyl peptidase II in the processing of Listeria monocytogenes-derived MHC class I-presented antigenic peptides

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Recognition of bacteria in the cytosol of Mammalian cells by the ubiquitin system

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The major substrates for TAP in vivo are derived from newly synthesized proteins

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Degradation of newly synthesized collagen

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12 December 2020

Two Listeria monocytogenes CTL epitopes are processed from the same antigen with different efficiencies

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12 December 2020

CTL epitope generation is tightly linked to cellular proteolysis of a Listeria monocytogenes antigen

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12 December 2020

Intracellular rate-limiting steps in MHC class I antigen processing

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12 December 2020