Strong cation exchange-based fractionation of Lys-N-generated peptides facilitates the targeted analysis of post-translational modifications.
about
Identification and analysis of the acetylated status of poplar proteins reveals analogous N-terminal protein processing mechanisms with other eukaryotesPeptide orientation affects selectivity in ion-exchange chromatographyA review of COFRADIC techniques targeting protein N-terminal acetylation.Straightforward and de novo peptide sequencing by MALDI-MS/MS using a Lys-N metalloendopeptidase.Perturbation of the yeast N-acetyltransferase NatB induces elevation of protein phosphorylation levelsAnnotation of the zebrafish genome through an integrated transcriptomic and proteomic analysis.Protein analysis by shotgun/bottom-up proteomicsThe generating function of CID, ETD, and CID/ETD pairs of tandem mass spectra: applications to database searchImplementing visible 473 nm photodissociation in a Q-Exactive mass spectrometer: towards specific detection of cysteine-containing peptides.Enhancing the identification of phosphopeptides from putative basophilic kinase substrates using Ti (IV) based IMAC enrichmentIn-depth quantitative cardiac proteomics combining electron transfer dissociation and the metalloendopeptidase Lys-N with the SILAC mouseDatabase independent proteomics analysis of the ostrich and human proteome.Advanced proteomic liquid chromatography.Increasing phosphoproteomic coverage through sequential digestion by complementary proteases.Campylobacter proteomics: guidelines, challenges and future perspectives.Development of multidimensional liquid chromatography and application in proteomic analysis.Protein and peptide fractionation, enrichment and depletion: tools for the complex proteome.Natural substrates of plant proteases: how can protease degradomics extend our knowledge?Strong cation exchange chromatography in analysis of posttranslational modifications: innovations and perspectives.Quantitative mass spectrometry in proteomics: critical review update from 2007 to the present.Towards single-cell LC-MS phosphoproteomics.Identifying novel targets of oncogenic EGF receptor signaling in lung cancer through global phosphoproteomics.Profiling of N-acetylated protein termini provides in-depth insights into the N-terminal nature of the proteomeUnblocking the sink: improved CID-based analysis of phosphorylated peptides by enzymatic removal of the basic C-terminal residue.Comparative assessment of site assignments in CID and electron transfer dissociation spectra of phosphopeptides discloses limited relocation of phosphate groups.LysargiNase mirrors trypsin for protein C-terminal and methylation-site identification.Comparison of retention behavior of oligolysine and oligoarginine in ion-pairing chromatography using heptafluorobutyric acid.High Sensitivity Quantitative Proteomics Using Automated Multidimensional Nano-flow Chromatography and Accumulated Ion Monitoring on Quadrupole-Orbitrap-Linear Ion Trap Mass Spectrometer.Why phosphoproteomics is still a challenge
P2860
Q21090782-9279854C-7D7C-40C5-A718-367407360776Q24634607-CCF27C31-994B-42A7-9D98-DBBF5FC3FE16Q30872116-4F1E1E31-528D-4B9D-9E5A-976317143226Q33388167-EE836CC1-CF8B-4746-ACAF-C8D3DF1F39E4Q33761749-06378FA3-39A3-4EF6-9E07-ACAC46D84C9AQ34468432-DCB5B59D-A294-4C27-BE5C-3F80C69E30BCQ34600986-7AFB853A-0A9A-4A09-8F34-48F50CC586C0Q35006588-2E5112C0-AEC4-4112-95E3-8F9D91D5E334Q35241962-BB1AC560-CB5E-4C19-9B09-46CA1A524627Q35497380-1AE2BBE3-8F57-4FB8-B361-026BFDBF3C03Q35497768-F4EC9B8A-DF48-4C41-94D8-AFEE91139D58Q35673775-AC90603C-2BAA-4438-960E-087A7A172913Q36295883-00C87955-6A2E-4FAD-A44E-99FFD5CD3A7EQ36668577-F2EF18CC-5AF5-4685-81D7-B0BEBA997BB0Q37390668-5670E3F1-D07C-4338-99FD-54DB824045FFQ37802868-20D6C67D-FC37-45DC-B237-0F819B9D24D9Q37829409-80D9C1B9-1D2D-41B2-8CBB-1CBFBB3ABF04Q37946960-8610D20E-4217-44B6-8F77-169CE7E8719FQ37969061-11048EA4-0DAF-42E7-8EB8-22992DCD7911Q38024637-BC9939B7-7701-4138-851D-543C1255E090Q38234569-9F2D4E9A-C48F-41B8-BE81-9FA6A2A50394Q38420747-1F5AA149-0256-40F3-9D6B-A8286D2F138DQ39754008-8D4D86E9-F45D-4911-BE9D-EDC93F9E2120Q41886466-663CA2F8-B686-438B-89FF-B87E761840B3Q42106276-45AB6FDA-B016-4398-B0C5-DAF429310437Q43023362-62A87615-3320-446B-9A65-273528E9B71DQ44659394-CDFA4EDF-1549-4042-AD5D-51E3E4682299Q47933556-F93F7DD4-349B-4018-B01E-FB0C9FFB64BCQ57842145-BD91340C-AC8B-4ED1-AD70-1DD1A4BFD66E
P2860
Strong cation exchange-based fractionation of Lys-N-generated peptides facilitates the targeted analysis of post-translational modifications.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Strong cation exchange-based f ...... t-translational modifications.
@en
Strong cation exchange-based f ...... t-translational modifications.
@nl
type
label
Strong cation exchange-based f ...... t-translational modifications.
@en
Strong cation exchange-based f ...... t-translational modifications.
@nl
prefLabel
Strong cation exchange-based f ...... t-translational modifications.
@en
Strong cation exchange-based f ...... t-translational modifications.
@nl
P2093
P2860
P1476
Strong cation exchange-based f ...... t-translational modifications.
@en
P2093
A F Maarten Altelaar
Albert J R Heck
Andreas O Helbig
Nadia Taouatas
P2860
P304
P356
10.1074/MCP.M800285-MCP200
P577
2008-09-29T00:00:00Z