Characterization of Tetrahymena histone H2B variants and posttranslational populations by electron capture dissociation (ECD) Fourier transform ion cyclotron mass spectrometry (FT-ICR MS).
about
Characterization of histone H2A and H2B variants and their post-translational modifications by mass spectrometryIdentification of protein N-terminal methyltransferases in yeast and humansNepsilon-formylation of lysine is a widespread post-translational modification of nuclear proteins occurring at residues involved in regulation of chromatin functionMass spectrometry-based detection and assignment of protein posttranslational modificationsA Hybrid Mechanism for the Synechocystis Arsenate Reductase Revealed by Structural Snapshots during Arsenate ReductionIdentification of histone H3 lysine 36 acetylation as a highly conserved histone modification.Analysis of histones in Xenopus laevis. II. mass spectrometry reveals an index of cell type-specific modifications on H3 and H4.Comprehensive phosphoprotein analysis of linker histone H1 from Tetrahymena thermophila.Organismal differences in post-translational modifications in histones H3 and H4.Long-distance combinatorial linkage between methylation and acetylation on histone H3 N termini.Peptide mass mapping of acetylated isoforms of histone H4 from mouse lymphosarcoma cells treated with histone deacetylase (HDACs) inhibitors.Utility of mass spectrometry for proteome analysis: part I. Conceptual and experimental approaches.Microarray analyses of gene expression during the Tetrahymena thermophila life cycleData processing algorithms for analysis of high resolution MSMS spectra of peptides with complex patterns of posttranslational modificationsα-N-methylation of damaged DNA-binding protein 2 (DDB2) and its function in nucleotide excision repair.High resolution electron transfer dissociation studies of unfractionated intact histones from murine embryonic stem cells using on-line capillary LC separation: determination of abundant histone isoforms and post-translational modificationsLysine propionylation and butyrylation are novel post-translational modifications in histonesChemical and biochemical approaches in the study of histone methylation and demethylationUnbiased proteomic screen for binding proteins to modified lysines on histone H3.Extensive and varied modifications in histone H2B of wild-type and histone deacetylase 1 mutant Neurospora crassaAnalysis of intact protein isoforms by mass spectrometry.Quantitative mass spectrometry reveals the epigenome as a target of arsenic.The Tetrahymena thermophila phagosome proteome.Breaking the histone code with quantitative mass spectrometry.Decoding protein modifications using top-down mass spectrometryMass spectrometry identifies and quantifies 74 unique histone H4 isoforms in differentiating human embryonic stem cellsMass spectrometry-based strategies for characterization of histones and their post-translational modifications.Histone proteomics and the epigenetic regulation of nucleosome mobility.Functional proteomics in histone research and epigenetics.Fourier transform ion cyclotron resonance: state of the art.Tissue-specific expression and post-translational modification of histone H3 variants.Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.Global histone profiling by LC-FTMS after inhibition and knockdown of deacetylases in human cellsUnambiguous determination of isobaric histone modifications by reversed-phase retention time and high-mass accuracy.Quantitative proteomics reveals histone modifications in crosstalk with H3 lysine 27 methylation.Systems-wide proteomic characterization of combinatorial post-translational modification patterns.Defining pluripotent stem cells through quantitative proteomic analysis.SILAC-based proteomic analysis to dissect the "histone modification signature" of human breast cancer cells.Analysis of arginine and lysine methylation utilizing peptide separations at neutral pH and electron transfer dissociation mass spectrometry.Mass spectrometry-based proteomics for the analysis of chromatin structure and dynamics.
P2860
Q24297556-1DD56991-45E2-4B60-8C72-691688615F93Q24313543-BCE14185-2F13-46C8-831A-28949FDFA695Q24648389-351A5E99-05B8-452A-BBA4-912E58FA778BQ27001576-EB2CC033-0307-49BC-B905-C5F089ADF261Q28607586-C9D84F3C-8341-497E-8FAC-5AEAB8BCAE9CQ30437262-8D4E563D-DEF2-4259-B95A-3E7E855A77ECQ30437404-ED7A5BCB-04B2-41D0-B3AD-E7C6551C2EB6Q30440955-859FFF3D-AD37-4146-929A-440EDC107CEDQ30442461-33B4D6C2-38A4-4557-BD0E-2F3D480B33B9Q30444527-247093A7-5401-4A4F-888B-BC26B065883FQ30795759-FFA675E5-F3A7-40D0-8CB6-09315A12B344Q33393366-34552352-C86B-46CF-ABB1-4A1799652842Q33407199-ED78692C-47C6-484E-956F-899F3F07DB26Q33517067-E95D93A9-0A1E-4779-94B1-7A85A4780AE9Q33718452-4730A68E-3573-4007-8035-E30124148A49Q33854961-DFA84A44-8A04-48F6-BF39-128BE390502BQ34027794-73AA9A4A-6684-4207-ABFA-CA6602EB9C78Q34030702-72A86210-7771-4255-B027-5A774FE10CB5Q34038791-6131910F-AF34-46AA-BCA8-841033011BC2Q35031576-AD7D5411-AA43-4885-9DDC-E2F15EAF8BF9Q35111010-1BED0179-AE74-4EDC-A926-CE190651A96BQ35180456-61AD439B-7F99-4025-B07A-18E0CB00423CQ35216748-DA169C83-7E33-4678-A6C2-AE1D3B949678Q35645008-9BB57490-868C-40E9-ACEF-BAB7109B5595Q36628274-B5756318-A427-4967-A35D-68CA538E7B32Q36670103-DD7D1A3D-114F-4C5E-AE2D-7B416BA0D920Q36787236-02D6F4A2-8EFA-445C-B415-8F3ABC4F2B8FQ36913037-AB496546-0EAF-4F03-8DA1-2A14FBBB12D3Q36913044-A6F3BEEF-FB7E-4CF0-8110-7006CF4DBE45Q36945438-E96B389C-248D-498C-A4BE-D52A74881785Q37041986-B58D73C8-7127-414C-9E59-CCADB99DE982Q37080670-57AC687A-08F5-4035-87BF-5226E697E666Q37438475-AC970B9D-D05E-42EA-8221-527DED7ADAB7Q37456238-A0247A82-6902-472A-91A3-617E6B19A5E5Q37623626-B6409223-37F0-427A-9D5D-3A7D16FF7E47Q37685118-175CF9F7-F1B3-41AB-9530-FAB5338A754FQ37844151-55EB8286-6DA4-426B-93B5-A2282AB62C6AQ39682430-9DA91FF1-C8D0-4D59-99E3-F82F448A488AQ39784445-BC679F85-6DD2-49AD-B0F3-B3242F912D02Q40042389-28B036DC-47A4-46D0-AD55-2D7EDDB36838
P2860
Characterization of Tetrahymena histone H2B variants and posttranslational populations by electron capture dissociation (ECD) Fourier transform ion cyclotron mass spectrometry (FT-ICR MS).
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh
2004年學術文章
@zh-hant
name
Characterization of Tetrahymen ...... mass spectrometry (FT-ICR MS).
@en
Characterization of Tetrahymen ...... electron capture dissociation
@nl
type
label
Characterization of Tetrahymen ...... mass spectrometry (FT-ICR MS).
@en
Characterization of Tetrahymen ...... electron capture dissociation
@nl
prefLabel
Characterization of Tetrahymen ...... mass spectrometry (FT-ICR MS).
@en
Characterization of Tetrahymen ...... electron capture dissociation
@nl
P2093
P2860
P1476
Characterization of Tetrahymen ...... mass spectrometry (FT-ICR MS).
@en
P2093
Burlingame AL
Chalkley RJ
Chalmers MJ
Marshall AG
McFarland MA
Medzihradszky KF
P2860
P304
P356
10.1074/MCP.M400041-MCP200
P577
2004-06-15T00:00:00Z