Kinase peptide specificity: improved determination and relevance to protein phosphorylation
about
LOK is a major ERM kinase in resting lymphocytes and regulates cytoskeletal rearrangement through ERM phosphorylationPin1 prolyl isomerase regulates endothelial nitric oxide synthaseSubstrate discrimination among mitogen-activated protein kinases through distinct docking sequence motifsIdentification of Thr29 as a critical phosphorylation site that activates the human proton channel Hvcn1 in leukocytesProtein kinases associated with the yeast phosphoproteome.Structure of the Toxoplasma gondii ROP18 Kinase Domain Reveals a Second Ligand Binding Pocket Required for Acute VirulenceDissecting phosphorylation networks: lessons learned from yeastIdentification and characterization of a leucine-rich repeat kinase 2 (LRRK2) consensus phosphorylation motifDeciphering the Arginine-binding preferences at the substrate-binding groove of Ser/Thr kinases by computational surface mappingMouse class III myosins: kinase activity and phosphorylation sitesExtensive phosphorylation of Smoothened in Hedgehog pathway activationSpatial exclusivity combined with positive and negative selection of phosphorylation motifs is the basis for context-dependent mitotic signaling.Development of an intracellularly acting inhibitory peptide selective for PKN.A single pair of acidic residues in the kinase major groove mediates strong substrate preference for P-2 or P-5 arginine in the AGC, CAMK, and STE kinase families.Rational Redesign of a Functional Protein Kinase-Substrate Interaction.Human-specific evolution and adaptation led to major qualitative differences in the variable receptors of human and chimpanzee natural killer cellsPhosphorylation of paxillin at threonine 538 by PKCdelta regulates LFA1-mediated adhesion of lymphoid cells.Expanding the repertoire of an ERK2 recruitment site: cysteine footprinting identifies the D-recruitment site as a mediator of Ets-1 binding.Current technologies to identify protein kinase substrates in high throughputCritical role of novel Thr-219 autophosphorylation for the cellular function of PKCtheta in T lymphocytes.The tumour suppressor RASSF1A is a novel substrate of PKC.Profiling the substrate specificity of protein kinases by on-bead screening of peptide librariesProtein kinase CbetaII-mediated phosphorylation of endothelial nitric oxide synthase threonine 495 mediates the endothelial dysfunction induced by FK506 (tacrolimus).Disrupting the CH1 domain structure in the acetyltransferases CBP and p300 results in lean mice with increased metabolic controlProfileGrids: a sequence alignment visualization paradigm that avoids the limitations of Sequence LogosRapid Identification of Protein Kinase Phosphorylation Site Motifs Using Combinatorial Peptide LibrariescJun N-terminal kinase (JNK) phosphorylation of serine 36 is critical for p66Shc activationSeq2Logo: a method for construction and visualization of amino acid binding motifs and sequence profiles including sequence weighting, pseudo counts and two-sided representation of amino acid enrichment and depletionNovel Insights into the PKCβ-dependent Regulation of the Oxidoreductase p66Shc.Rapid T cell receptor-mediated SHP-1 S591 phosphorylation regulates SHP-1 cellular localization and phosphatase activityTransphosphorylation of E. coli Proteins during Production of Recombinant Protein Kinases Provides a Robust System to Characterize Kinase Specificity.Understanding and exploiting substrate recognition by protein kinases.The nuclear orphan receptor NR2F6 suppresses lymphocyte activation and T helper 17-dependent autoimmunityZIPping to pain relief: the role (or not) of PKMζ in chronic pain.Targeted activation of conventional and novel protein kinases C through differential translocation patternsNovel phosphorylation site markers of protein kinase C delta activation.Exceptional disfavor for proline at the P + 1 position among AGC and CAMK kinases establishes reciprocal specificity between them and the proline-directed kinases.Protein kinase C-dependent phosphorylation of transient receptor potential canonical 6 (TRPC6) on serine 448 causes channel inhibition.Graphlet kernels for prediction of functional residues in protein structures.Two Sample Logo: a graphical representation of the differences between two sets of sequence alignments.
P2860
Q24316935-B1D4A028-02CC-45A7-950E-4EFAD3F88620Q24617827-58BA0D22-23EB-45B2-9800-8078BF956D21Q24647635-A0E8C657-995F-4E0F-9C04-A604E567F7A4Q24648598-1E0F876B-5F3D-4D5F-A639-BD648516F8D6Q25256184-3334DBE9-7698-4806-BF76-85FE4460E9AAQ27680375-DC076162-F3C9-4B23-AF6C-558DE4719711Q27686946-1EB439CD-B8DC-4BDF-BB5C-ED568D7659AFQ28475942-CAC9FB6D-A506-4762-BC10-AF216DA6D269Q28478059-1299CAF2-AC32-466B-BFD8-A74C329FA275Q28512769-A5318B48-C42B-4C19-B534-961469EE2952Q28770067-0CFBDDD6-3212-4E38-9021-ECE7585376ECQ30414432-39E18C78-2370-4DA6-BCFC-9C30FF100F2FQ30450204-CC506C42-467A-4D7D-8735-EAB29CC8082EQ33222589-398F6ADA-5FDE-45C5-ABA9-ECE1FD3CFCD5Q33721699-AEFA3530-1867-4776-BC9B-D239CCC91096Q33747569-7858B4B1-2936-4B2C-B73E-F018FAFFC7B6Q33803975-F2FD0118-266B-476A-A3A1-738CAC3A9FEAQ33964467-CCD52B05-D743-4C6D-A829-292E427F67A0Q34019229-63D0C031-BEE7-423C-9D4F-FFC236B3FE99Q34133617-AE7A4EF1-271D-428A-98B6-2966F06E2E98Q34783040-71E8B961-4FB1-43CD-A69D-D7D8833B337CQ34814639-1984621A-9D19-42D2-94BB-F58CDF8EB9F2Q35003081-2A7E6C12-9E5A-4B55-BA99-338905D21819Q35185366-E508B7FD-7F9B-4AB6-97B4-D880633C3CC9Q35263913-1C9DB466-8D82-44C9-96AB-6E788B010CC5Q35821378-1880C357-708C-4AEA-934B-0B74927B4356Q35921419-657085B1-06D3-4407-A937-9727D954254AQ36088409-BE2CFBB6-7071-4D21-A5BE-215A08D32097Q36131918-55A27B1B-2573-41E5-AA4B-49E64A27029AQ36157339-D572B059-93A5-4ED4-B2D1-3B36BE07D59FQ36434730-5208526E-C4AA-4D09-836C-CFC5AC9682C2Q36631005-C1D5E277-4000-4F0B-83CD-1464ABE37845Q37087730-2B38847B-AA9B-494C-B66E-877335CA5A6CQ38083881-B6911B1F-17B0-4170-90A1-0318BC0A5E6CQ39004144-961CD17B-DB00-42E8-9499-9F9BB724A843Q40113218-A95F0EF3-CB73-4B89-9448-31A34EAF318BQ40472370-A1F4E42D-A875-414E-A0E1-574415B9BB65Q41197267-223EE1DC-B73C-4FFC-AB71-F1905577B781Q42272603-5B1E8F12-5EF7-43BF-BB52-4D1CC3E31D72Q42683783-3383B982-1E5C-4A75-A322-79251FF17039
P2860
Kinase peptide specificity: improved determination and relevance to protein phosphorylation
description
2004 nî lūn-bûn
@nan
2004 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
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
name
Kinase peptide specificity: im ...... nce to protein phosphorylation
@ast
Kinase peptide specificity: im ...... nce to protein phosphorylation
@en
type
label
Kinase peptide specificity: im ...... nce to protein phosphorylation
@ast
Kinase peptide specificity: im ...... nce to protein phosphorylation
@en
prefLabel
Kinase peptide specificity: im ...... nce to protein phosphorylation
@ast
Kinase peptide specificity: im ...... nce to protein phosphorylation
@en
P2093
P2860
P356
P1476
Kinase peptide specificity: im ...... nce to protein phosphorylation
@en
P2093
Guozhi Zhu
John Hallam
Juan Herrero
Koichi Fujii
Stephen Shaw
P2860
P304
13744-13749
P356
10.1073/PNAS.0401881101
P407
P577
2004-09-08T00:00:00Z