Identification by mutational analysis of amino acid residues essential in the chaperone function of calreticulin.
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Generation of amyloid-β is reduced by the interaction of calreticulin with amyloid precursor protein, presenilin and nicastrinStructural Basis of Carbohydrate Recognition by CalreticulinStructural and Functional Relationships between the Lectin and Arm Domains of CalreticulinX-Ray Structure of the Human Calreticulin Globular Domain Reveals a Peptide-Binding Area and Suggests a Multi-Molecular MechanismERp27, a new non-catalytic endoplasmic reticulum-located human protein disulfide isomerase family member, interacts with ERp57Structures of parasite calreticulins provide insights into their flexibility and dual carbohydrate/peptide-binding properties.Calnexin deficiency leads to dysmyelination.Higher plant calreticulins have acquired specialized functions in ArabidopsisIdentification of the rheumatoid arthritis shared epitope binding site on calreticulin.Modes of calreticulin recruitment to the major histocompatibility complex class I assembly pathwayCalsperin is a testis-specific chaperone required for sperm fertility.Endoplasmic reticulum calcium depletion impacts chaperone secretion, innate immunity, and phagocytic uptake of cellsGlycan-dependent and -independent interactions contribute to cellular substrate recruitment by calreticulin.Ca2+-signaling, alternative splicing and endoplasmic reticulum stress responses.Calreticulin: roles in cell-surface protein expression.Contributions of the Lectin and Polypeptide Binding Sites of Calreticulin to Its Chaperone Functions in Vitro and in Cells.Diverging functions among calreticulin isoforms in higher plants.Novel molecular mechanism of cellular transformation by a mutant molecular chaperone in myeloproliferative neoplasms.Functional roles of calreticulin in cancer biology.ERp57 modulates STAT3 signaling from the lumen of the endoplasmic reticulumDefining the requirements for the pathogenic interaction between mutant calreticulin and MPL in MPN.Role of cysteine amino acid residues in calnexin.
P2860
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P2860
Identification by mutational analysis of amino acid residues essential in the chaperone function of calreticulin.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
2005年论文
@zh
2005年论文
@zh-cn
name
Identification by mutational a ...... rone function of calreticulin.
@en
type
label
Identification by mutational a ...... rone function of calreticulin.
@en
prefLabel
Identification by mutational a ...... rone function of calreticulin.
@en
P2093
P2860
P356
P1476
Identification by mutational a ...... rone function of calreticulin.
@en
P2093
J M Robert Parker
Jody Groenendyk
Marek Michalak
Michal Opas
Monika Dabrowska
Simone S Steiner
Virginie Martin
P2860
P304
P356
10.1074/JBC.M508302200
P407
P577
2005-11-16T00:00:00Z