Quantitative proteomics reveals regulation of dynamic components within TATA-binding protein (TBP) transcription complexes.
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Towards elucidating the stability, dynamics and architecture of the nucleosome remodeling and deacetylase complex by using quantitative interaction proteomicsComplementary quantitative proteomics reveals that transcription factor AP-4 mediates E-box-dependent complex formation for transcriptional repression of HDM2Quantitative affinity purification mass spectrometry: a versatile technology to study protein-protein interactionsAIRE-PHD fingers are structural hubs to maintain the integrity of chromatin-associated interactomeCooperative action of NC2 and Mot1p to regulate TATA-binding protein function across the genomeA combined approach of quantitative interaction proteomics and live-cell imaging reveals a regulatory role for endoplasmic reticulum (ER) reticulon homology proteins in peroxisome biogenesisEstablishment of a protein frequency library and its application in the reliable identification of specific protein interaction partners.A role for BAF57 in cell cycle-dependent transcriptional regulation by the SWI/SNF chromatin remodeling complex.A genetic engineering solution to the "arginine conversion problem" in stable isotope labeling by amino acids in cell culture (SILAC).Profiling of protein interaction networks of protein complexes using affinity purification and quantitative mass spectrometry.Beyond hairballs: The use of quantitative mass spectrometry data to understand protein-protein interactionsLinear motif-mediated interactions have contributed to the evolution of modularity in complex protein interaction networksChallenges and rewards of interaction proteomics.Comparison of strong cation exchange and SDS-PAGE fractionation for analysis of multiprotein complexesProteomics reveals a physical and functional link between hepatocyte nuclear factor 4alpha and transcription factor IID.New dimensions in the study of protein complexes using quantitative mass spectrometry.Proteogenomics and systems biology: quest for the ultimate missing parts.Linking the proteins--elucidation of proteome-scale networks using mass spectrometry.Unraveling the dynamics of protein interactions with quantitative mass spectrometry.Isolation and characterization of plant protein complexes by mass spectrometry.Transient protein-protein interactions.Two steps forward--one step back: advances in affinity purification mass spectrometry of macromolecular complexes.Resolving protein interactions and complexes by affinity purification followed by label-based quantitative mass spectrometry.Quantitative proteomics: A strategic ally to map protein interaction networks.Broader implications of SILAC-based proteomics for dissecting signaling dynamics in cancer.Studying macromolecular complex stoichiometries by peptide-based mass spectrometryQuantitative proteomics using SILAC: Principles, applications, and developments.Triple SILAC to determine stimulus specific interactions in the Wnt pathway.Dicer-dependent and -independent Argonaute2 protein interaction networks in mammalian cellsStoichiometry of chromatin-associated protein complexes revealed by label-free quantitative mass spectrometry-based proteomicsA Double-Barrel Liquid Chromatography-Tandem Mass Spectrometry (LC-MS/MS) System to Quantify 96 Interactomes per DayIdentifying specific protein interaction partners using quantitative mass spectrometry and bead proteomes.Tracking transcription factor complexes on DNA using total internal reflectance fluorescence protein binding microarrays.Quantitative mass spectrometry of TATA binding protein-containing complexes and subunit phosphorylations during the cell cycle.Interaction profiling of RNA-binding ubiquitin ligases reveals a link between posttranscriptional regulation and the ubiquitin system.Stable Isotope Labeling by Amino Acids in Cell Culture (SILAC) Technology in Fission Yeast.Protein complexes: the forest and the trees.Discrimination between stable and dynamic components of protein complexes by means of quantitative proteomics
P2860
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P2860
Quantitative proteomics reveals regulation of dynamic components within TATA-binding protein (TBP) transcription complexes.
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年学术文章
@wuu
2007年学术文章
@zh
2007年学术文章
@zh-cn
2007年学术文章
@zh-hans
2007年学术文章
@zh-my
2007年学术文章
@zh-sg
2007年學術文章
@yue
2007年學術文章
@zh-hant
name
Quantitative proteomics reveal ...... (TBP) transcription complexes.
@en
Quantitative proteomics reveal ...... ts within TATA-binding protein
@nl
type
label
Quantitative proteomics reveal ...... (TBP) transcription complexes.
@en
Quantitative proteomics reveal ...... ts within TATA-binding protein
@nl
prefLabel
Quantitative proteomics reveal ...... (TBP) transcription complexes.
@en
Quantitative proteomics reveal ...... ts within TATA-binding protein
@nl
P2093
P2860
P1476
Quantitative proteomics reveal ...... (TBP) transcription complexes.
@en
P2093
Annemieke Kolkman
Florence Mousson
H Th Marc Timmers
W W M Pim Pijnappel
P2860
P304
P356
10.1074/MCP.M700306-MCP200
P577
2007-12-17T00:00:00Z