In vivo chemical modification of proteins (post-translational modification).
about
Selenocysteine, pyrrolysine, and the unique energy metabolism of methanogenic archaeaWhat is the optimum size for the genetic alphabet?hSP, the domain-duplicated homolog of pS2 protein, is co-expressed with pS2 in stomach but not in breast carcinomaA mammalian protein kinase with potential for serine/threonine and tyrosine phosphorylation is related to cell cycle regulatorsIdentification of protein N-terminal methyltransferases in yeast and humansStructure of human hemopexin: O-glycosyl and N-glycosyl sites and unusual clustering of tryptophan residuesComparison of initiation of protein synthesis in procaryotes, eucaryotes, and organellesThe widespread role of non-enzymatic reactions in cellular metabolismPurification, characterization, and kinetic mechanism of S-adenosyl-L-methionine: vitexin 2"-O-rhamnoside 7-O-methyltransferase of Avena sativa LSignaling mediated by the cytosolic domain of peptidylglycine alpha-amidating monooxygenaseKCR1, a membrane protein that facilitates functional expression of non-inactivating K+ currents associates with rat EAG voltage-dependent K+ channelsIdentification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulumIndependent highly sensitive characterization of asparagine deamidation and aspartic acid isomerization by sheathless CZE-ESI-MS/MS.Structural analysis of a highly glycosylated and unliganded gp120-based antigen using mass spectrometry.Analysis of the Sendai virus M gene and protein.Post-translational modifications induce significant yet not extreme changes to protein structure.Involvement of superoxide dismutase in spore coat assembly in Bacillus subtilis.Involvement of the proteasome in various degradative processes in mammalian cells.In vivo sulfation of the contact site A glycoprotein of Dictyostelium discoideum.Role of the alpha-amino group of protein in ubiquitin-mediated protein breakdown.Measurement of nonsulfated cholecystokinins.Intramembrane translocation and posttranslational palmitoylation of the chloroplast 32-kDa herbicide-binding protein.Life is sweet! A novel role for N-glycans in Drosophila lifespan.Molecular mechanism for eliminylation, a newly discovered post-translational modificationPantothenate is required in Neurospora crassa for assembly of subunit peptides of cytochrome c oxidase and ATPase/ATP synthase.Signal processing by protein tyrosine phosphorylation in plants.Proteomics: current techniques and potential applications to lung disease.The major tyrosine-sulfated protein of the bovine anterior pituitary is a secretory protein present in gonadotrophs, thyrotrophs, mammotrophs, and corticotrophs.Glucocorticoid-regulated glycoprotein maturation in wild-type and mutant rat cell linesGlucocorticoid-regulated localization of cell surface glycoproteins in rat hepatoma cells is mediated within the Golgi complex.Subunit II of cytochrome c oxidase from Paracoccus denitrificans. DNA sequence, gene expression and the protein.Cloning and sequencing of cDNA encoding the complete mouse liver alcohol dehydrogenase.Nucleotide sequence of cDNA and predicted amino acid sequence of rat liver uricase.Cloning and sequencing of rat liver cDNAs encoding the regulatory protein of glucokinase.Glucocorticoid-regulated compartmentalization of cell surface-associated glycoproteins in rat hepatoma cells: evidence for an independent response that requires receptor function and de novo RNA synthesis.Imaging beyond the proteomeIdentification of a precursor in the biosynthesis of the p21 transforming protein of harvey murine sarcoma virus.Polypeptide structure and encoding location of the adenovirus serotype 2 late, nonstructural 33K protein.Identification of the initiation site of poliovirus polyprotein synthesis.Diphtheria toxin-resistant mutants of Saccharomyces cerevisiae.
P2860
Q21296868-9AB3FFED-0EE9-4154-BFDE-74F0EDA54ED1Q22066193-2376B3C6-0BE8-4281-AAA1-2AE61A7854F6Q24300126-B43AF44F-0BC7-41F1-9C0E-7C8538A4D3CBQ24310682-18DC4DCF-E1BA-4BD2-95CF-47403F2D72D5Q24313543-46C87B98-F8F3-479A-B087-3724A46C222EQ24594858-13E4A841-E37E-4F27-970A-F1CDED608527Q24654718-4C173B2C-7A25-4D9B-A154-ADB9AF45A61EQ26996495-810DA72F-7363-47E9-97A9-848B915B53CDQ28272366-940657CD-9E94-4468-913F-AC4425EE4D4AQ28565137-7E4251AD-95C0-42BA-8BDD-776FAD348844Q28580641-EEF27262-36E9-4AD5-9DA2-DCD8BB57DC82Q29620019-0E9D44C8-2A1A-4D87-9BC1-AC953D0894D1Q30384596-2B042C15-89C8-46E4-B6F8-30114E7A6FCCQ30393415-2D918056-5E3D-41DA-BC7D-364200287094Q30411854-9A4DC0BE-FDA1-4FE4-8100-7FEC1341049CQ30420946-F5CC6BE9-5722-4064-ABBE-37D7400EAA96Q33729583-E882BBF0-28A6-4853-880A-6C5B306B87B7Q33849783-04D9AD3E-6C14-4397-8E21-01DCD4C2BE1FQ33933683-AE46345F-59D7-4D09-B549-3416372E2144Q34245587-A983C775-37A2-490C-BB47-0CD6DDF85EDEQ34415302-D5E37943-3E77-4A9C-8541-7EF400449FCBQ34604200-E244FB16-3679-4105-9E5F-AA4574E6B4FAQ34643533-89AC47C9-EB4A-41DD-BDB2-19DE661CCEAAQ35119053-B7268110-DE2F-4336-9A3E-86B46A8E28DCQ35607366-EE86F2A4-319A-4160-96BA-35F4EC8B1026Q35671262-6A7C58B0-0843-43D6-B4B7-39F691F97607Q35798681-A4E4BF6C-6DEE-486F-9F9A-FAE5D122B0DCQ36211959-063DB090-199D-4EDE-950E-BA0053F0DE52Q36216590-DF0DB6FE-43C0-4EA5-A908-4A1E614FE0CDQ36218555-1D079B62-E268-414A-8F63-B2D4D9C9D4E4Q36282312-41882729-7F31-4727-B84B-0530189FDF00Q36435342-3757F02F-7AF0-416F-A270-8FC08F0D236EQ36444109-97049FA4-E785-4191-A980-0B15DF99E8DDQ36695722-35A456C3-CA2C-489A-A3DD-F8554D959BB1Q36838916-0186079E-4301-4C6F-B528-45182577396AQ36862717-281ED32F-71E9-43CC-8C19-D7416B280AC7Q36921386-3F1CD492-0F01-4EA3-95B4-2B088271ED01Q36929212-6BFDA971-FD7C-42DA-8854-31C7EE4E5EBAQ36941452-3BB06A30-A2F0-4FFD-B446-51333EC98B92Q36952490-12F64581-B077-414D-A053-FF0C82A5B523
P2860
In vivo chemical modification of proteins (post-translational modification).
description
1981 nî lūn-bûn
@nan
1981年の論文
@ja
1981年論文
@yue
1981年論文
@zh-hant
1981年論文
@zh-hk
1981年論文
@zh-mo
1981年論文
@zh-tw
1981年论文
@wuu
1981年论文
@zh
1981年论文
@zh-cn
name
In vivo chemical modification of proteins (post-translational modification).
@en
type
label
In vivo chemical modification of proteins (post-translational modification).
@en
prefLabel
In vivo chemical modification of proteins (post-translational modification).
@en
P1476
In vivo chemical modification of proteins (post-translational modification).
@en
P2093
P304
P356
10.1146/ANNUREV.BI.50.070181.004031
P577
1981-01-01T00:00:00Z