about
Identification and analysis of the acetylated status of poplar proteins reveals analogous N-terminal protein processing mechanisms with other eukaryotesA supramodular FHA/BRCT-repeat architecture mediates Nbs1 adaptor function in response to DNA damageN-terminal modifications of cellular proteins: The enzymes involved, their substrate specificities and biological effectsThe physiology of protein S-acylationThe Not4 RING E3 Ligase: A Relevant Player in Cotranslational Quality ControlCatalysis and Inhibition of Mycobacterium tuberculosis Methionine AminopeptidaseStructural Analysis of Bengamide Derivatives as Inhibitors of Methionine AminopeptidasesStructure and function of a cyanophage-encoded peptide deformylaseHydroxamic acids as potent inhibitors of Fe(II) and Mn(II) E. coli methionine aminopeptidase: biological activities and X-ray structures of oxazole hydroxamate-EcMetAP-Mn complexesCryo-EM structures of Arx1 and maturation factors Rei1 and Jjj1 bound to the 60S ribosomal subunitUnderstanding the highly efficient catalysis of prokaryotic peptide deformylases by shedding light on the determinants specifying the low activity of the human counterpartN-terminal acetylome analysis reveals the specificity of Naa50 (Nat5) and suggests a kinetic competition between N-terminal acetyltransferases and methionine aminopeptidases.Co-translational capturing of nascent ribosomal proteins by their dedicated chaperonesTop Down Proteomics Reveals Mature Proteoforms Expressed in Subcellular Fractions of the Echinococcus granulosus Preadult StageIdentification, purification and characterization of laterosporulin, a novel bacteriocin produced by Brevibacillus sp. strain GI-9Expression and characterization of Mycobacterium tuberculosis methionine aminopeptidase type 1aThe intrinsically disordered N-terminal domain of thymidylate synthase targets the enzyme to the ubiquitin-independent proteasomal degradation pathwayPlant cysteine oxidases are dioxygenases that directly enable arginyl transferase-catalysed arginylation of N-end rule targets.An improved workflow for quantitative N-terminal charge-based fractional diagonal chromatography (ChaFRADIC) to study proteolytic events in Arabidopsis thaliana.Rotational restriction of nascent peptides as an essential element of co-translational protein folding: possible molecular players and structural consequences.Growth inhibition of Escherichia coli and methicillin-resistant Staphylococcus aureus by targeting cellular methionine aminopeptidase.Methylation of aquaporins in plant plasma membrane.System for expression of microsporidian methionine amino peptidase type 2 (MetAP2) in the yeast Saccharomyces cerevisiaeN-terminal proteomics and ribosome profiling provide a comprehensive view of the alternative translation initiation landscape in mice and menProtein N-terminal processing: substrate specificity of Escherichia coli and human methionine aminopeptidases.Protein myristoylation in health and disease.Redox regulation of methionine aminopeptidase 2 activitySolvent-assisted slow conversion of a dithiazole derivative produces a competitive inhibitor of peptide deformylase.N-terminal acetylation inhibits protein targeting to the endoplasmic reticulumAmino-terminal extension present in the methionine aminopeptidase type 1c of Mycobacterium tuberculosis is indispensible for its activity.Experimental annotation of post-translational features and translated coding regions in the pathogen Salmonella TyphimuriumMbtH-like proteins as integral components of bacterial nonribosomal peptide synthetases.Comparative metagenomics of microbial traits within oceanic viral communitiesIdentification of protein stability determinants in chloroplastsRNF2 is the target for phosphorylation by the p38 MAPK and ERK signaling pathways.Nuclear factor-κB-inducing kinase (NIK) contains an amino-terminal inhibitor of apoptosis (IAP)-binding motif (IBM) that potentiates NIK degradation by cellular IAP1 (c-IAP1).Impact of the N-terminal amino acid on targeted protein degradation.Multiple classes of immune-related proteases associated with the cell death response in pepper plantsComprehensive quantitative analysis of ovarian and breast cancer tumor peptidomes.Identification and quantification of DNA repair protein apurinic/apyrimidinic endonuclease 1 (APE1) in human cells by liquid chromatography/isotope-dilution tandem mass spectrometry.
P2860
Q21090782-AAAD2DDE-D169-421D-A9A5-8791BD1C34F9Q24321669-D5BED684-8176-4518-B2BE-4107960FDABCQ27011436-6A1A60CC-0B24-4D83-8812-228F4FB1A333Q27014134-C503DEA2-E654-413C-A82A-B53063E3D706Q27027216-6C53E908-563A-4DD2-8FD7-179D22A9DC53Q27658805-1E4E0D1C-C775-4738-8BF1-CE26FBB9258AQ27671657-CF5B9BC7-E531-4B19-8414-5B5FF95838F0Q27676358-E64CB1BF-B63B-40DC-A93D-58569CF32318Q27678407-0BCB6BF4-44A7-446D-8FA5-867166290582Q27683374-37B349A3-1142-4D66-B51A-9F41097DD2F4Q27689078-A0498D95-63A6-48A9-990C-C755CCF20EFFQ27933661-9E3A3F71-0678-4162-B710-047C0038F11FQ27937424-F136743D-90A8-408D-A30B-818FF0CBC17EQ28268566-B37A2DD3-0233-49CD-BB58-6BCBAAF8BB9EQ28481396-F618AA58-3CF2-403E-B6E0-B3A299653D7BQ28487518-7A35C5A3-1902-435D-8195-C1C20204B5D8Q28749496-16255CDE-AB1C-47A7-927E-5ED150A0FBFAQ30313311-E5630C49-0871-439F-8155-4035F50D6778Q30316527-AF55057A-D1FC-42FC-AC13-928C0D9EED84Q30854248-973550BD-03C1-4AA2-803F-4114175D9FF7Q31010109-2383655B-6428-45AF-A6CD-4DF29A5EA0B0Q33250092-E44469E0-7766-48A7-87D4-46BA3BBFBEF7Q33372298-818F2BD9-31E9-4058-9C89-40A6ED436A63Q33583158-9CF96E6A-3758-45EB-A02D-87FD52328657Q33593465-9CCA3337-CF44-4DBE-8D78-E6A6EEEDBF9AQ33631172-0219C361-F366-42A8-80F4-57A8463F4F60Q33652216-EEF4D257-68CB-479C-94FF-9E324D478146Q33792568-4A96AEEA-6B10-46B0-8760-9A7113831163Q33927332-F35BB39C-F9EA-4F27-A945-4169AA723001Q33950959-F871F216-A532-47F2-A6EB-81617D42192BQ34002927-A309322B-FF8F-46E0-A0B2-1B2D2FDF7E50Q34138341-83B803E6-66B3-46B6-AC69-37878D1D5D69Q34163669-690C9840-0DA9-460E-A4B7-AFBC3C96E334Q34333927-1009EAF3-DC78-4FA5-B5DA-6BFB60229BD1Q34356314-05749C50-1A3C-437C-A827-0C458B98765DQ34431075-6CEDB9EF-D9DC-42DD-B9C9-57AD4D9DDF71Q34557941-C31CC2B5-672B-4BEF-A2F5-7C9C1123D5C0Q34733882-F7DE8FD4-4780-4316-9BE9-0E764DF76CBDQ34855337-802AD9E5-7B75-4074-A6A9-171F1C8AF196Q34904605-F7BF3CED-4964-4CCF-8A26-4B1D70ADEDC4
P2860
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Protein N-terminal methionine excision.
@ast
Protein N-terminal methionine excision.
@en
type
label
Protein N-terminal methionine excision.
@ast
Protein N-terminal methionine excision.
@en
prefLabel
Protein N-terminal methionine excision.
@ast
Protein N-terminal methionine excision.
@en
P1476
Protein N-terminal methionine excision
@en
P2093
Boularot A
Giglione C
P2888
P304
P356
10.1007/S00018-004-3466-8
P577
2004-06-01T00:00:00Z