Shotgun identification of protein modifications from protein complexes and lens tissue - Test2 - elhamkhani - TriplyDB

Shotgun identification of protein modifications from protein complexes and lens tissue

Shotgun identification of protein modifications from protein complexes and lens tissue

http://www.wikidata.org/entity/Q24534333

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Immunoaffinity profiling of tyrosine phosphorylation in cancer cells Mass spectrometric analysis of the human 40S ribosomal subunit: native and HCV IRES-bound complexes FBH1 promotes DNA double-strand breakage and apoptosis in response to DNA replication stress Modifications of human betaA1/betaA3-crystallins include S-methylation, glutathiolation, and truncation Methylation and carbamylation of human gamma-crystallins The role of GRASP55 in Golgi fragmentation and entry of cells into mitosis Architecture of the budding yeast kinetochore reveals a conserved molecular core In silico proteome analysis to facilitate proteomics experiments using mass spectrometry Bacillus cereus Phosphopentomutase Is an Alkaline Phosphatase Family Member That Exhibits an Altered Entry Point into the Catalytic Cycle N-terminal domain of B-crystallin provides a conformational switch for multimerization and structural heterogeneity Cell cycle-dependent phosphorylation of the DNA polymerase epsilon subunit, Dpb2, by the Cdc28 cyclin-dependent protein kinase.Rtn1p is involved in structuring the cortical endoplasmic reticulum.The mitogen-activated protein kinase Slt2 regulates nuclear retention of non-heat shock mRNAs during heat shock-induced stress.The yeast lgl family member Sro7p is an effector of the secretory Rab GTPase Sec4p.Phosphorylation of the chromosomal passenger protein Bir1 is required for localization of Ndc10 to the spindle during anaphase and full spindle elongation.Mass spectrometry-based proteomics Nuclear LC3 Associates with Slowly Diffusing Complexes that Survey the Nucleolus Synaptojanin-1 plays a key role in astrogliogenesis: possible relevance for Down's syndrome Proteolipid protein is required for transport of sirtuin 2 into CNS myelin Elucidation of Zymomonas mobilis physiology and stress responses by quantitative proteomics and transcriptomics ISPTM: an iterative search algorithm for systematic identification of post-translational modifications from complex proteome mixtures Racemisation and human cataract. D-Ser, D-Asp/Asn and D-Thr are higher in the lifelong proteins of cataract lenses than in age-matched normal lenses Wnt proteins are lipid-modified and can act as stem cell growth factors Proteomic analysis of post-translational modifications Analysis of surface-exposed outer membrane proteins in Helicobacter pylori.Analyzing proteomes and protein function using graphical comparative analysis of tandem mass spectrometry results.Lens β-crystallins: the role of deamidation and related modifications in aging and cataract.Quantitative proteomic analysis of histone modifications Proteomic analysis of wild-type and mutant huntingtin-associated proteins in mouse brains identifies unique interactions and involvement in protein synthesis.Identification of novel chondroitin proteoglycans in Caenorhabditis elegans: embryonic cell division depends on CPG-1 and CPG-2 Cell-cycle regulation of formin-mediated actin cable assembly.Cortactin promotes exosome secretion by controlling branched actin dynamics Spindle-E cycling between nuage and cytoplasm is controlled by Qin and PIWI proteins The pseudokinase CaMKv is required for the activity-dependent maintenance of dendritic spines.Comprehensive analysis of proteins of pH fractionated samples using monolithic LC/MS/MS, intact MW measurement and MALDI-QIT-TOF MS Blind search for post-translational modifications and amino acid substitutions using peptide mass fingerprints from two proteases.Budding yeast centrosome duplication requires stabilization of Spc29 via Mps1-mediated phosphorylation Identification of 2D-gel proteins: a comparison of MALDI/TOF peptide mass mapping to mu LC-ESI tandem mass spectrometry.Advances in proteomics data analysis and display using an accurate mass and time tag approach.Proteomics in pathology research.

P2860

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P2860

Shotgun identification of protein modifications from protein complexes and lens tissue

http://www.wikidata.org/entity/Q24534333

description

2002 nî lūn-bûn

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2002 թուականի Յունիսին հրատարակուած գիտական յօդուած

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2002 թվականի հունիսին հրատարակված գիտական հոդված

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年论文

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name

Shotgun identification of protein modifications from protein complexes and lens tissue

@ast

Shotgun identification of protein modifications from protein complexes and lens tissue

@en

Shotgun identification of protein modifications from protein complexes and lens tissue

@nl

type

label

Shotgun identification of protein modifications from protein complexes and lens tissue

@ast

Shotgun identification of protein modifications from protein complexes and lens tissue

@en

Shotgun identification of protein modifications from protein complexes and lens tissue

@nl

prefLabel

Shotgun identification of protein modifications from protein complexes and lens tissue

@ast

Shotgun identification of protein modifications from protein complexes and lens tissue

@en

Shotgun identification of protein modifications from protein complexes and lens tissue

@nl

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Shotgun identification of protein modifications from protein complexes and lens tissue

@en

P2093

Avery Weiss

http://www.w3.org/2001/XMLSchema#string

Dirk Wolters

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John I Clark

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John R Yates

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Joseph J Tasto

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Judy M Clark

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Rovshan Sadygov

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W Hayes McDonald

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P2860

Acetylation of histones and transcription-related factors

Accurate quantitation of protein expression and site-specific phosphorylation

In vivo acetylation identified at lysine 70 of human lens alphaA-crystallin

A generic protein purification method for protein complex characterization and proteome exploration

An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database

Large-scale analysis of the yeast proteome by multidimensional protein identification technology

The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage

Quantitative analysis of complex protein mixtures using isotope-coded affinity tags

Identification by electrospray ionization mass spectrometry of the sites of tyrosine phosphorylation induced in activated Jurkat T cells on the protein tyrosine kinase ZAP-70

Post-translational modifications of water-soluble human lens crystallins from young adults

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7900-5

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scholarly article

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2744981

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10.1073/PNAS.122231399

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P407

P433

12

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99

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Michael P. Washburn

Kathleen L. Gould

Michael J MacCoss

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2002-06-11T00:00:00Z

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11313129

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12060738

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122992

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