A Common Single Nucleotide Polymorphism in Endoplasmic Reticulum Aminopeptidase 2 Induces a Specificity Switch That Leads to Altered Antigen Processing (Q27670921)

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Language	Label	Description	Also known as
English	A Common Single Nucleotide Polymorphism in Endoplasmic Reticulum Aminopeptidase 2 Induces a Specificity Switch That Leads to Altered Antigen Processing	scientific article

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scholarly article

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A Common Single Nucleotide Polymorphism in Endoplasmic Reticulum Aminopeptidase 2 Induces a Specificity Switch That Leads to Altered Antigen Processing (English)

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endoplasmic reticulum

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single-nucleotide polymorphism

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based on heuristic

inferred from title

author name string

Irini Evnouchidou

1

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James Birtley

2

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Sergey Seregin

3

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Athanasios Papakyriakou

4

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Efthalia Zervoudi

5

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Martina Samiotaki

6

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George Panayotou

7

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Petros Giastas

8

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Olivia Petrakis

9

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Dimitris Georgiadis

10

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Andrea Amalfitano

11

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Emmanuel Saridakis

12

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Irene M Mavridis

13

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Efstratios Stratikos

14

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language of work or name

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publication date

1 September 2012

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Journal of Immunology

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189

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5

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2383-92

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The crystal structure of human endoplasmic reticulum aminopeptidase 2 reveals the atomic basis for distinct roles in antigen processing

1 reference

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Fetal ERAP2 variation is associated with preeclampsia in African Americans in a case-control study

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Structural basis for antigenic peptide precursor processing by the endoplasmic reticulum aminopeptidase ERAP1

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20 March 2017

PHENIX: a comprehensive Python-based system for macromolecular structure solution

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20 March 2017

Structure of aminopeptidase N from Escherichia coli complexed with the transition-state analogue aminophosphinic inhibitor PL250

1 reference

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1 reference

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Interaction between ERAP1 and HLA-B27 in ankylosing spondylitis implicates peptide handling in the mechanism for HLA-B27 in disease susceptibility

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Probing the S1 specificity pocket of the aminopeptidases that generate antigenic peptides.

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29 September 2017

Cutting Edge: Coding single nucleotide polymorphisms of endoplasmic reticulum aminopeptidase 1 can affect antigenic peptide generation in vitro by influencing basic enzymatic properties of the enzyme

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Somatic mutations at EZH2 Y641 act dominantly through a mechanism of selectively altered PRC2 catalytic activity, to increase H3K27 trimethylation

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Placental leucine aminopeptidase efficiently generates mature antigenic peptides in vitro but in patterns distinct from endoplasmic reticulum aminopeptidase 1

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Endoplasmic reticulum aminopeptidases: Biology and pathogenic potential

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1 reference

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1 reference

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The specificity of trimming of MHC class I-presented peptides in the endoplasmic reticulum.

1 reference

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1 reference

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The internal sequence of the peptide-substrate determines its N-terminus trimming by ERAP1.

1 reference

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Endoplasmic reticulum aminopeptidase 1 (ERAP1) trims MHC class I-presented peptides in vivo and plays an important role in immunodominance.

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1 reference

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The ER aminopeptidase, ERAP1, trims precursors to lengths of MHC class I peptides by a "molecular ruler" mechanism.

1 reference

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Cross-presentation: underlying mechanisms and role in immune surveillance

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Phosphinic peptides as zinc metalloproteinase inhibitors

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Protein degradation and the generation of MHC class I-presented peptides.

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Identifiers

10.4049/JIMMUNOL.1200918

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release_sbxcxqkbsfatfhcbm2eii37pbq

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