Identification of an N-domain histidine essential for chaperone function in calreticulin.

doi:10.1074/jbc.M309497200

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Topics Community

Back to search

Article

Identification of an N-domain histidine essential for chaperone function in calreticulin.

The Journal of biological chemistry - 12 Dec 2003

Guo Lei, Groenendyk Jody, Papp Sylvia, Dabrowska Monika, Knoblach Barbara, Kay Cyril, Parker J M Robert, Opas Michal, Michalak Marek

Abstract excerpt

Calreticulin is an endoplasmic reticulum (ER) luminal Ca(2+)-binding chaperone involved in folding of newly synthesized glycoproteins via the "calreticulin-calnexin cycle." We reconstituted ER of calreticulin-deficient cells with N-terminal histidine (His25, His82, His128, and His153) calreticulin mutants and carried out a functional analysis. In crt(-/-) cells bradykinin-dependent Ca2+ release is altered, and...

Topics

Animals
Blotting, Western
Bradykinin
Calcium
Calreticulin
Circular Dichroism
Cytoplasm
Electrophoresis, Polyacrylamide Gel
Endoplasmic Reticulum
Histidine
Immunoglobulins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Magnetic Resonance Spectroscopy

Malate Dehydrogenase

Mice

Microscopy, Fluorescence

Models, Molecular

Molecular Chaperones

Mutagenesis, Site-Directed

Source

Open in PubMed

Identifiers

PMID: 14522955
DOI: 10.1074/jbc.M309497200

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Identification of an N-domain histidine essential for chaperone function in calreticulin.PMID 14522955Read ↗

Identification by mutational analysis of amino acid residues essential in the chaperone function of calreticulin.Semantic proximity Read ↗

Compromised calnexin function in calreticulin-deficient cells.Semantic proximity Read ↗

Impact of Calreticulin and Its Mutants on Endoplasmic Reticulum Function in Health and Disease.Semantic proximity Read ↗

Calreticulin is essential for cardiac development.Semantic proximity Read ↗

Calnexin, calreticulin, and Bip/Kar2p in protein folding.Semantic proximity Read ↗

Contrasting Functions of Calreticulin and Calnexin in Glycoprotein Folding and ER Quality ControlSemantic proximity Read ↗

Lectin-deficient calreticulin retains full functionality as a chaperone for class I histocompatibility molecules.Semantic proximity Read ↗

Pharmacologic rescue of conformationally-defective proteins: implications for the treatment of human disease.Semantic proximity Read ↗

Prolonged association of temperature-sensitive mutants of human P-glycoprotein with calnexin during biogenesis.Semantic proximity Read ↗

Identification and characterization of calreticulin as a novel plasminogen receptor.Semantic proximity Read ↗

Co-chaperone FKBP38 promotes HERG trafficking.Semantic proximity Read ↗

The polypeptide binding conformation of calreticulin facilitates its cell-surface expression under conditions of endoplasmic reticulum stress.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.