Calreticulin, a Ca2 -binding chaperone of the endoplasmic reticulum (Q24306716)

Europe PubMed Central

title

Calreticulin, a Ca2 -binding chaperone of the endoplasmic reticulum (English)

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main subject

endoplasmic reticulum

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molecular chaperones

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Calreticulin

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sequestering of calcium ion

GOA release 2020-03-11

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International Journal of Biochemistry & Cell Biology

GOA release 2020-03-11

author name string

Pascal Gelebart

series ordinal

1

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Michal Opas

series ordinal

2

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Marek Michalak

series ordinal

3

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language of work or name

English

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publication date

February 2005

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published in

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volume

37

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issue

2

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page(s)

260-6

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cites work

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NMR structures of 36 and 73-residue fragments of the calreticulin P-domain

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Ca2 signaling and calcium binding chaperones of the endoplasmic reticulum

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Identification of a novel calreticulin isoform (Crt2) in human and mouse

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Necrotic cell death in C. elegans requires the function of calreticulin and regulators of Ca(2 ) release from the endoplasmic reticulum

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Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin

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The Structure of calnexin, an ER chaperone involved in quality control of protein folding

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Calreticulin differentially modulates calcium uptake and release in the endoplasmic reticulum and mitochondria.

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Cardiac-specific expression of calcineurin reverses embryonic lethality in calreticulin-deficient mouse

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Identification of an N-domain Histidine Essential for Chaperone Function in Calreticulin

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Calreticulin is essential for cardiac development

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Functional specialization of calreticulin domains

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Calreticulin, a calcium-binding molecular chaperone, is required for stress response and fertility in Caenorhabditis elegans

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Calreticulin and calnexin in the endoplasmic reticulum are important for phagocytosis

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The contribution of N-glycans and their processing in the endoplasmic reticulum to glycoprotein biosynthesis

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Identifiers

DOI

1 reference

Consolidated OpenCitations Corpus – April 2017

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Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

15474971

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Consolidated OpenCitations Corpus – April 2017