Structural Basis of Carbohydrate Recognition by Calreticulin
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Human CLEC18 Gene Cluster Contains C-type Lectins with Differential Glycan-binding SpecificityN-linked sugar-regulated protein folding and quality control in the ERStructural 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 MechanismGentamicin Binds to the Megalin Receptor as a Competitive Inhibitor Using the Common Ligand Binding Motif of Complement Type Repeats: INSIGHT FROM THE NMR STRUCTURE OF THE 10TH COMPLEMENT TYPE REPEAT DOMAIN ALONE AND IN COMPLEX WITH GENTAMICINPlasticity of the β-Trefoil Protein Fold in the Recognition and Control of Invertebrate Predators and Parasites by a Fungal Defence SystemStructures of parasite calreticulins provide insights into their flexibility and dual carbohydrate/peptide-binding properties.Toward atomic force microscopy and mass spectrometry to visualize and identify lipid rafts in plasmodesmataThe polypeptide binding conformation of calreticulin facilitates its cell-surface expression under conditions of endoplasmic reticulum stress.The intrinsic and extrinsic effects of N-linked glycans on glycoproteostasis.Structural insight into substrate recognition by the endoplasmic reticulum folding-sensor enzyme: crystal structure of third thioredoxin-like domain of UDP-glucose:glycoprotein glucosyltransferaseCalreticulin is a thermostable protein with distinct structural responses to different divalent cation environments.Self-oligomerization is essential for enhanced immunological activities of soluble recombinant calreticulin.Protein folding and quality control in the endoplasmic reticulum: Recent lessons from yeast and mammalian cell systems.Convergent synthesis of homogeneous Glc1Man9GlcNAc2-protein and derivatives as ligands of molecular chaperones in protein quality control.Regulation of calreticulin-major histocompatibility complex (MHC) class I interactions by ATP.Structural basis for two-step glucose trimming by glucosidase II involved in ER glycoprotein quality controlGlycan-dependent and -independent interactions contribute to cellular substrate recruitment by calreticulin.The C-Terminal Acidic Region of Calreticulin Mediates Phosphatidylserine Binding and Apoptotic Cell Phagocytosis.Glycoprotein folding and quality-control mechanisms in protein-folding diseasesA conserved basic residue cluster is essential for the protein quality control function of the Arabidopsis calreticulin 3.Protein secretion and the endoplasmic reticulum.Calreticulin in the immune system: ins and outsThe many functions of the endoplasmic reticulum chaperones and folding enzymes.Convergent and divergent mechanisms of sugar recognition across kingdoms.Calreticulin: roles in cell-surface protein expression.Conformational Analysis of a High-Mannose-Type Oligosaccharide Displaying Glucosyl Determinant Recognised by Molecular Chaperones Using NMR-Validated Molecular Dynamics Simulation.Contributions of the Lectin and Polypeptide Binding Sites of Calreticulin to Its Chaperone Functions in Vitro and in Cells.Emerging structural insights into glycoprotein quality control coupled with N-glycan processing in the endoplasmic reticulum.Oncogenic Drivers in Myeloproliferative Neoplasms: From JAK2 to Calreticulin Mutations.Quality control of glycoprotein folding and ERAD: the role of N-glycan handling, EDEM1 and OS-9.Novel molecular mechanism of cellular transformation by a mutant molecular chaperone in myeloproliferative neoplasms.Cooperative role of calnexin and TigA in Aspergillus oryzae glycoprotein folding.An in vivo investigation of amino acid residues critical for the lectin function of Arabidopsis calreticulin 3.Synthesis of Glc1Man9-Glycoprotein Probes by a Misfolding/Enzymatic Glucosylation/Misfolding Sequence.Calreticulin: Challenges Posed by the Intrinsically Disordered Nature of Calreticulin to the Study of Its Function.Structure of the human MHC-I peptide-loading complex.Single-particle electron microscopy structure of UDP-glucose:glycoprotein glucosyltransferase suggests a selectivity mechanism for misfolded proteins.Molecular and Biochemical Characterization of Opisthorchis viverrini Calreticulin.Whole genome duplications have provided teleosts with many roads to peptide loaded MHC class I molecules.
P2860
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P2860
Structural Basis of Carbohydrate Recognition by Calreticulin
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2010 nî lūn-bûn
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2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
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2010 թվականի դեկտեմբերին հրատարակված գիտական հոդված
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2010年の論文
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年学术文章
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Structural Basis of Carbohydrate Recognition by Calreticulin
@ast
Structural Basis of Carbohydrate Recognition by Calreticulin
@en
Structural Basis of Carbohydrate Recognition by Calreticulin
@nl
type
label
Structural Basis of Carbohydrate Recognition by Calreticulin
@ast
Structural Basis of Carbohydrate Recognition by Calreticulin
@en
Structural Basis of Carbohydrate Recognition by Calreticulin
@nl
prefLabel
Structural Basis of Carbohydrate Recognition by Calreticulin
@ast
Structural Basis of Carbohydrate Recognition by Calreticulin
@en
Structural Basis of Carbohydrate Recognition by Calreticulin
@nl
P2093
P2860
P50
P3181
P356
P1476
Structural Basis of Carbohydrate Recognition by Calreticulin
@en
P2093
Angelika Rosenauer
Cosmin L Pocanschi
David B Williams
Sara Bastos-Aristizabal
P2860
P304
P3181
P356
10.1074/JBC.M110.168294
P407
P577
2010-12-03T00:00:00Z