Distinct contributions of the lectin and arm domains of calnexin to its molecular chaperone function (Q38358222)

2 September 2017

Distinct contributions of the lectin and arm domains of calnexin to its molecular chaperone function (English)

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2 September 2017

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Achim Brockmeier

1

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2 September 2017

Ulf Brockmeier

series ordinal

2

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2 September 2017

David B Williams

series ordinal

3

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2 September 2017

language of work or name

English

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publication date

12 December 2008

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Journal of Biological Chemistry

2 September 2017

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2 September 2017

284

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2 September 2017

6

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2 September 2017

3433-3444

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Protein targeting to and translocation across the membrane of the endoplasmic reticulum

2 September 2017

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

The translocon: a dynamic gateway at the ER membrane

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Protein targeting and translocation at the endoplasmic reticulum membrane--through the eye of a needle?

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Quality control in the endoplasmic reticulum

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Endoplasmic reticulum-associated degradation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Quality Control and Protein Folding in the Secretory Pathway

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Specific interaction of ERp57 and calnexin determined by NMR spectroscopy and an ER two-hybrid system

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Human, mouse, and rat calnexin cDNA cloning: identification of potential calcium binding motifs and gene localization to human chromosome 5

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

NMR structure of the calreticulin P-domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Potent lectin-independent chaperone function of calnexin under conditions prevalent within the lumen of the endoplasmic reticulum

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Minor folding defects trigger local modification of glycoproteins by the ER folding sensor GT

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

The ER protein folding sensor UDP-glucose glycoprotein-glucosyltransferase modifies substrates distant to local changes in glycoprotein conformation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Roles of N-linked glycans in the endoplasmic reticulum

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Calreticulin promotes folding of functional human leukocyte antigen class I molecules in vitro

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

A polypeptide binding conformation of calreticulin is induced by heat shock, calcium depletion, or by deletion of the C-terminal acidic region.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Polypeptide substrate recognition by calnexin requires specific conformations of the calnexin protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Lectin-deficient calnexin is capable of binding class I histocompatibility molecules in vivo and preventing their degradation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Relationship between calnexin and BiP in suppressing aggregation and promoting refolding of protein and glycoprotein substrates

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Glycoprotein folding in the endoplasmic reticulum: a tale of three chaperones?

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Delineation of the lectin site of the molecular chaperone calreticulin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

P-domain and lectin site are involved in the chaperone function of Saccharomyces cerevisiae calnexin homologue

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Site-directed mutagenesis by overlap extension using the polymerase chain reaction

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Substrate binding to the molecular chaperone Hsp104 and its regulation by nucleotides

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Assignment of the contribution of the tryptophan residues to the circular dichroism spectrum of human carbonic anhydrase II.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Specificity of DnaK-peptide binding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Peptide substrate identification for yeast Hsp40 Ydj1 by screening the phage display library

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Structure-based mutagenesis studies of the peptide substrate binding fragment of type I heat-shock protein 40

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Contributions of tryptophan side chains to the far-ultraviolet circular dichroism of proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Interactions of substrate with calreticulin, an endoplasmic reticulum chaperone

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Kinetics and the mechanism of interaction of the endoplasmic reticulum chaperone, calreticulin, with monoglucosylated (Glc1Man9GlcNAc2) substrate

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Fluorescent iminodiacetamide derivatives as potential ionophores for optical zinc ion-selective sensors

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

The chaperonin GroEL does not recognize apo-alpha-lactalbumin in the molten globule state.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Detection of oligomerisation and substrate recognition sites of small heat shock proteins by peptide arrays.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Structural analysis of substrate binding by the molecular chaperone DnaK

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

The Hsp70 and Hsp60 chaperone machines

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Mutational analysis provides molecular insight into the carbohydrate-binding region of calreticulin: pivotal roles of tyrosine-109 and aspartate-135 in carbohydrate recognition.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

Peptide-binding specificity of the molecular chaperone BiP

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M804866200

21 January 2018

Identifiers

DOI

10.1074/JBC.M804866200

1 reference

2 September 2017

1 reference