Identification by Mutational Analysis of Amino Acid Residues Essential in the Chaperone Function of Calreticulin-Reference-Cited by-同舟云学术

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Identification by Mutational Analysis of Amino Acid Residues Essential in the Chaperone Function of Calreticulin

Published:2006-01 Issue:4 Volume:281 Page:2338-2346
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Martin Virginie,Groenendyk Jody,Steiner Simone S.,Guo Lei,Dabrowska Monika,Parker J.M. Robert,Müller-Esterl Werner,Opas Michal,Michalak Marek

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference32 articles.

1. Quality control in the endoplasmic reticulum

2. Lectin control of protein folding and sorting in the secretory pathway

3. Enhanced Catalysis of Ribonuclease B Folding by the Interaction of Calnexin or Calreticulin with ERp57

4. Association of folding intermediates of glycoproteins with calnexin during protein maturation

5. Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control.

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1. Calreticulin: Endoplasmic reticulum Ca²⁺ gatekeeper;Journal of Cellular and Molecular Medicine;2023-07-09

2. Antigen presentation in vertebrates: Structural and functional aspects;Developmental & Comparative Immunology;2023-07

3. Calreticulin Shortage Results in Disturbance of Calcium Storage, Mitochondrial Disease, and Kidney Injury;Cells;2022-04-13

4. Z-α ₁ -antitrypsin polymers impose molecular filtration in the endoplasmic reticulum after undergoing phase transition to a solid state;Science Advances;2022-04-08

5. Mapping human calreticulin regions important for structural stability;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2021-11

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