PDI family protein ERp29 recognizes P-domain of molecular chaperone calnexin.

No abstract is available for this paper.

• Publication year

  2017

• Venue

  Biochemical and Biophysical Research Communications - BBRC

• Publication date

  2017-06-03

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/j.bbrc.2017.04.139PMID 28456374
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• Misfolded Proteins

  2019cited by this paper
• HaloTag Technology: A Versatile Platform for Biomedical Applications

  2015cited by this paper
• Glycan specificity of a testis-specific lectin chaperone calmegin and effects of hydrophobic interactions.

  2014cited by this paper
• PDI family protein ERp29 forms 1:1 complex with lectin chaperone calreticulin.

  2014influential reference
• The human protein disulfide isomerase gene family

  2012cited by this paper
• Binding Properties and Stability of the Ras-Association Domain of Rap1-GTP Interacting Adapter Molecule (RIAM)

  2012cited by this paper
• Structural Basis of Cyclophilin B Binding by the Calnexin/Calreticulin P-domain*♦

  2010cited by this paper
• A structural overview of the PDI family of proteins

  2010cited by this paper
• Physical and functional interaction of transmembrane thioredoxin-related protein with major histocompatibility complex class I heavy chain: redox-based protein quality control and its potential relevance to immune responses.

  2009cited by this paper
• Substrate Specificity of the Oxidoreductase ERp57 Is Determined Primarily by Its Interaction with Calnexin and Calreticulin

  2009cited by this paper
• Structural Basis of the Migfilin-Filamin Interaction and Competition with Integrin β Tails*

  2008cited by this paper
• Crystal structure of the bb' domains of the protein disulfide isomerase ERp57.

  2006influential reference
• Overexpression of ERp29 in the thyrocytes of FRTL-5 cells

  2005cited by this paper
• The human protein disulphide isomerase family: substrate interactions and functional properties

  2005cited by this paper
• Specific interaction of ERp57 and calnexin determined by NMR spectroscopy and an ER two‐hybrid system

  2004influential reference
• Misfolded proteins, endoplasmic reticulum stress and neurodegeneration.

  2004cited by this paper
• Lectin control of protein folding and sorting in the secretory pathway.

  2003cited by this paper
• Quality control in the endoplasmic reticulum protein factory

  2003cited by this paper
• TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain

  2002cited by this paper
• Localization of the Lectin, ERp57 Binding, and Polypeptide Binding Sites of Calnexin and Calreticulin*

  2002cited by this paper
• Identification of ERp29, an Endoplasmic Reticulum Lumenal Protein, as a New Member of the Thyroglobulin Folding Complex*

  2002cited by this paper
• NMR structures of 36 and 73-residue fragments of the calreticulin P-domain.

  2002cited by this paper
• ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin.

  1999cited by this paper
• ERp28, a human endoplasmic-reticulum-lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box motif.

  1998cited by this paper
• The Molecular Chaperone Calnexin Binds Glc1Man9GlcNAc2 Oligosaccharide as an Initial Step in Recognizing Unfolded Glycoproteins (*)

  1995cited by this paper

• Expression, purification, and enzymatic characterization of human UDP-glucose:glycoprotein glucosyltransferase-Selenoprotein F complex from Sf9 insect cells.

  2025cites this paper
• N-glycan-dependent protein maturation and quality control in the ER

  2025cites this paper
• Thioredoxin Domain Containing 5 (TXNDC5): Friend or Foe?

  2024cites this paper
• Label-Free Quantitative Proteomics Analysis of Producer and Non-producer Chinese Hamsters Ovary (CHO) Cells under ER Stress Conditions

  2023cites this paper
• Analysis of Selenoprotein F Binding to UDP‐Glucose:Glycoprotein Glucosyltransferase (UGGT) by a Photoreactive Crosslinker

  2022cites this paper
• Oligomannose-Type Glycan Processing in the Endoplasmic Reticulum and Its Importance in Misfolding Diseases

  2022cites this paper
• ER whorls triggered by GhCNX6 were discovered involved in drought stress on cotton

  2022cites this paper
• Functional structure analysis and genome-wide identification of CNX gene family in cotton

  2022cites this paper
• Arabidopsis PDI11 interacts with lectin molecular chaperons calreticulin 1 and 2 through its D domain.

  2021cites this paper
• Two protein disulfide isomerase subgroups work synergistically in catalyzing oxidative protein folding.

  2021cites this paper
• Glycan structure-based perspectives on the entry and release of glycoproteins in the calnexin/calreticulin cycle.

  2021cites this paper
• Folding and Quality Control of Glycoproteins

  2021cites this paper
• Dimerization of ER-resident molecular chaperones mediated by ERp29.

  2020cites this paper
• Calnexin cycle – structural features of the ER chaperone system

  2020cites this paper
• Calnexin/Calreticulin and Assays Related to N-Glycoprotein Folding In Vitro.

  2020cites this paper
• [The potential role of calnexin in the activation of cardiac fibroblasts].

  2020cites this paper
• Glycan dependent refolding activity of ER glucosyltransferase (UGGT).

  2020cites this paper
• The Probable, Possible, and Novel Functions of ERp29

  2020cites this paper
• Chemical Synthesis Based Approach to Glycoprotein Functions in the Endoplasmic Reticulum.

  2020cites this paper
• Structural insights into N-linked glycan-mediated protein folding from chemical and biological perspectives.

  2020cites this paper
• Structural Aspects of ER Glycoprotein Quality-Control System Mediated by Glucose Tagging.

  2018cites this paper
• Characterization of the oxidative protein folding activity of a unique plant oxidoreductase, Arabidopsis protein disulfide isomerase-11.

  2018cites this paper
• Mapping the ER Interactome: The P Domains of Calnexin and Calreticulin as Plurivalent Adapters for Foldases and Chaperones.

  2017cites this paper
• Functional characterisation of the Endoplasmic Reticulum protein (ERp27)

  2017cites this paper