Three-dimensional structure topology of the calreticulin P-domain based on NMR assignment (Q31864661)

4 July 2017

Three-dimensional structure topology of the calreticulin P-domain based on NMR assignment (English)

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4 July 2017

1

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Wüthrich K

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4 July 2017

Riek R

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Braun D

series ordinal

3

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4 July 2017

Helenius A

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5

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4 July 2017

language of work or name

English

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publication date

1 January 2001

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4 July 2017

5

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inferred from page(s)

published in

FEBS Letters

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4 July 2017

488

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1-2

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4 July 2017

69-73

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Protein folding in the cell

4 July 2017

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Setting the standards: quality control in the secretory pathway

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Association of folding intermediates of glycoproteins with calnexin during protein maturation

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Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins

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

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Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi

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

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ERp57 functions as a subunit of specific complexes formed with the ER lectins calreticulin and calnexin

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Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin

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Identification and crystallization of a protease-resistant core of calnexin that retains biological activity.

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Chaperone activity and structure of monomeric polypeptide binding domains of GroEL

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Three-dimensional (1)H-TOCSY-relayed ct-[(13)C, (1)H]-HMQC for aromatic spin system identification in uniformly (13)C-labeled proteins.

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Time-saving methods for heteronuclear multidimensional NMR of ((13)C, (15)N) doubly labeled proteins.

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The program XEASY for computer-supported NMR spectral analysis of biological macromolecules

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Torsion angle dynamics for NMR structure calculation with the new program DYANA

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Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Computation of sterically allowed proton-proton distances and statistical analysis of proton-proton distances in single crystal protein conformations.

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

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1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects

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Processing of multi-dimensional NMR data with the new software PROSA

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Calnexin, calreticulin and the folding of glycoproteins

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The role of the lectin calnexin in conformation independent binding to N-linked glycoproteins and quality control.

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Calreticulin: one protein, one gene, many functions.

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Methodological advances in protein NMR

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Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances

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Empirical correlation between protein backbone conformation and C.alpha. and C.beta. 13C nuclear magnetic resonance chemical shifts

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1 reference

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Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Basic pancreatic trypsin inhibitor

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7 January 2021

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Statistical Basis for the Use of 13Calpha Chemical Shifts in Protein Structure Determination

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7 January 2021

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Identifiers

DOI

10.1016/S0014-5793(00)02382-6

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4 July 2017

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