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注意:仅列出部分参考文献,下载原文获取全部文献信息。Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum
Marek Michalak et al.
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Calreticulin-dependent recycling in the early secretory pathway mediates optimal peptide loading of MHC class I molecules
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Assembly and intracellular trafficking of HLA-B*3501 and HLA-B*3503
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JOURNAL OF BIOLOGICAL CHEMISTRY (2009)
ERp57 Does Not Require Interactions with Calnexin and Calreticulin to Promote Assembly of Class I Histocompatibility Molecules, and It Enhances Peptide Loading Independently of Its Redox Activity
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被撤回的出版物: Lectin-deficient calreticulin retains full functionality as a chaperone for class I histocompatibility molecules (Retracted article. See vol. 27, pg. 2517, 2016)
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MOLECULAR BIOLOGY OF THE CELL (2008)
The redox activity of ERp57 is not essential for its functions in MHC class I peptide loading
David R. Peaper et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2008)
MHC class I assembly: out and about
Malini Raghavan et al.
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Selective loading of high-affinity peptides onto major histocompatibility complex class I molecules by the tapasin-ERp57 heterodimer
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Identifying protein construct variants with increased crystallization propensity -: A case study
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Identification by mutational analysis of amino acid residues essential in the chaperone function of calreticulin
V Martin et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2006)
Impaired assembly of the major histocompatibility complex class I peptide-loading complex in mice deficient in the oxidoreductase ERp57
N Garbi et al.
NATURE IMMUNOLOGY (2006)
Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex
DR Peaper et al.
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Delineation of the lectin site of the molecular chaperone calreticulin
SP Thomson et al.
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Molecular basis of listeriolysin O pH dependence
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Identification and characterization of structural domains of human ERp57 -: Association with calreticulin requires several domains
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Mutational analysis provides molecular insight into the carbohydrate-binding region of calreticulin: Pivotal roles of tyrosine-109 and aspartate-135 in carbohydrate recognition
M Kapoor et al.
BIOCHEMISTRY (2004)
A polypeptide binding conformation of calreticulin is induced by heat shock, calcium depletion, or by deletion of the C-terminal acidic region
SM Rizvi et al.
MOLECULAR CELL (2004)
Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery
MC Lo et al.
ANALYTICAL BIOCHEMISTRY (2004)
Major histocompatibility complex class I molecules expressed with monoglucosylated N-linked glycans bind calreticulin independently of their assembly status
PA Wearsch et al.
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Site-directed, Ligase-Independent Mutagenesis (SLIM): a single-tube methodology approaching 100% efficiency in 4 h
J Chiu et al.
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Dimerization and oligomerization of the chaperone calreticulin
CS Jorgensen et al.
EUROPEAN JOURNAL OF BIOCHEMISTRY (2003)
A major role for tapasin as a stabilizer of the TAP peptide transporter and consequences for MHC class I expression
N Garbi et al.
EUROPEAN JOURNAL OF IMMUNOLOGY (2003)
A new vector for high-throughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site
L Stols et al.
PROTEIN EXPRESSION AND PURIFICATION (2002)
TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain
EM Frickel et al.
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Assembly and antigen-presenting function of MHC class I molecules in cells lacking the ER chaperone calreticulin
B Gao et al.
IMMUNITY (2002)
The metal ion binding properties of calreticulin modulate its conformational flexibility and thermal stability
ZJ Li et al.
BIOCHEMISTRY (2001)
The structure of calnexin, an ER chaperone involved in quality control of protein folding
JD Schrag et al.
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Impaired assembly yet normal trafficking of MHC class I molecules in tapasin mutant mice
AG Grandea et al.
IMMUNITY (2000)