A chemoenzymatic approach toward the rapid and sensitive detection of O-GlcNAc posttranslational modifications. - Wikidata - awgldk - TriplyDB

A chemoenzymatic approach toward the rapid and sensitive detection of O-GlcNAc posttranslational modifications.

A chemoenzymatic approach toward the rapid and sensitive detection of O-GlcNAc posttranslational modifications.

http://www.wikidata.org/entity/Q44704206

about

Exploring the O-GlcNAc proteome: direct identification of O-GlcNAc-modified proteins from the brain Glycan Engineering for Cell and Developmental Biology Site-Specifically Labeled Immunoconjugates for Molecular Imaging--Part 1: Cysteine Residues and Glycans The hexosamine signaling pathway: deciphering the "O-GlcNAc code"Enzymatic labeling of proteins: techniques and approaches Regulation of calcium/calmodulin-dependent kinase IV by O-GlcNAc modification.Direct identification of nonreducing GlcNAc residues on N-glycans of glycoproteins using a novel chemoenzymatic method Fold-recognition and comparative modeling of human alpha2,3-sialyltransferases reveal their sequence and structural similarities to CstII from Campylobacter jejuni.Site specific conjugation of fluoroprobes to the remodeled Fc N-glycans of monoclonal antibodies using mutant glycosyltransferases: application for cell surface antigen detection O-GlcNAc protein modification in plants: Evolution and function.The role of O-GlcNAc signaling in the pathogenesis of diabetic retinopathy.Detection of 5-hydroxymethylcytosine in DNA by transferring a keto-glucose by using T4 phage β-glucosyltransferase Tools for Studying Glycans: Recent Advances in Chemoenzymatic Glycan Labeling Enrichment of O-GlcNAc modified proteins by the periodate oxidation-hydrazide resin capture approach Chemoenzymatic synthesis of uridine 5'-diphospho-2-acetonyl-2-deoxy-alpha-D-glucose as C(2)-carbon isostere of UDP-GlcNAc Quantification of O-glycosylation stoichiometry and dynamics using resolvable mass tags.Mapping of O-GlcNAc sites of 20 S proteasome subunits and Hsp90 by a novel biotin-cystamine tag.Beta-N-acetylglucosamine (O-GlcNAc) is part of the histone code Assignment of protein function in the postgenomic era.O-GlcNAcylation: a novel post-translational mechanism to alter vascular cellular signaling in health and disease: focus on hypertension.Z-band alternatively spliced PDZ motif protein (ZASP) is the major O-linked β-N-acetylglucosamine-substituted protein in human heart myofibrils The E2F-1 associated retinoblastoma-susceptibility gene product is modified by O-GlcNAc.Boronic acid-functionalized detonation nanodiamond for specific enrichment of glycopeptides in glycoproteome analysis.Improved synthesis of UDP-2-(2-ketopropyl)galactose and a first synthesis of UDP-2-(2-ketopropyl)glucose for the site-specific linking of biomolecules via modified glycan residues using glycosyltransferases Proteomic approaches for site-specific O-GlcNAcylation analysis.Chemical reporters for fluorescent detection and identification of O-GlcNAc-modified proteins reveal glycosylation of the ubiquitin ligase NEDD4-1 Reversible hydrazide chemistry-based enrichment for O-GlcNAc-modified peptides and glycopeptides having non-reducing GlcNAc residues.Site-specific antibody-drug conjugates: the nexus of bioorthogonal chemistry, protein engineering, and drug development Site-specific antibody-drug conjugation through an engineered glycotransferase and a chemically reactive sugar Chemical approaches to understanding O-GlcNAc glycosylation in the brain.The N-acetyl-binding pocket of N-acetylglucosaminyltransferases also accommodates a sugar analog with a chemical handle at C2.Role of a single amino acid in the evolution of glycans of invertebrates and vertebrates Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease.The roles of O-linked β-N-acetylglucosamine in cardiovascular physiology and disease.Exploring kinase cosubstrate promiscuity: monitoring kinase activity through dansylation.Bioconjugation and detection of lactosamine moiety using alpha1,3-galactosyltransferase mutants that transfer C2-modified galactose with a chemical handle.Mutant glycosyltransferases assist in the development of a targeted drug delivery system and contrast agents for MRI Glycoproteomics enabled by tagging sialic acid- or galactose-terminated glycans Applications of glycosyltransferases in the site-specific conjugation of biomolecules and the development of a targeted drug delivery system and contrast agents for MRI.Use of novel mutant galactosyltransferase for the bioconjugation of terminal N-acetylglucosamine (GlcNAc) residues on live cell surface

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A chemoenzymatic approach toward the rapid and sensitive detection of O-GlcNAc posttranslational modifications.

http://www.wikidata.org/entity/Q44704206

description

2003 nî lūn-bûn

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2003年の論文

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年學術文章

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2003年學術文章

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name

A chemoenzymatic approach towa ...... sttranslational modifications.

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A chemoenzymatic approach towa ...... sttranslational modifications.

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type

label

A chemoenzymatic approach towa ...... sttranslational modifications.

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A chemoenzymatic approach towa ...... sttranslational modifications.

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prefLabel

A chemoenzymatic approach towa ...... sttranslational modifications.

@en

A chemoenzymatic approach towa ...... sttranslational modifications.

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A chemoenzymatic approach towa ...... sttranslational modifications.

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Alexander Lippert

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Boopathy Ramakrishnan

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Katherine G Poulin-Kerstien

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Linda C Hsieh-Wilson

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Nathan Lamarre-Vincent

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Nelly Khidekel

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Pradman K Qasba

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Sabine Arndt

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52

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14692737

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