Crystal structure and mutational analysis of the Saccharomyces cerevisiae cell cycle regulatory protein Cks1: implications for domain swapping, anion binding and protein interactions
about
A negatively charged amino acid in Skp2 is required for Skp2-Cks1 interaction and ubiquitination of p27Kip1A duplicated motif controls assembly of zona pellucida domain proteinsCascades of multisite phosphorylation control Sic1 destruction at the onset of S phaseCks1 activates transcription by binding to the ubiquitylated proteasome.Three different binding sites of Cks1 are required for p27-ubiquitin ligationRole of conformational heterogeneity in domain swapping and adapter function of the Cks proteinsThe quaternary structure of the recombinant bovine odorant-binding protein is modulated by chemical denaturantsA Synthetic Dosage Lethal Genetic Interaction Between CKS1B and PLK1 Is Conserved in Yeast and Human Cancer Cells.The Prozone Effect Accounts for the Paradoxical Function of the Cdk-Binding Protein Suc1/CksCks1: Structure, Emerging Roles and Implications in Multiple CancersSolution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge region determining the affinity for a phosphorylated substrate.The enigma of the near-symmetry of proteins: Domain swapping.Multisite phosphorylation networks as signal processors for Cdk1.S-phase cyclin-dependent kinases promote sister chromatid cohesion in budding yeast.Morphogenesis signaling components influence cell cycle regulation by cyclin dependent kinase.Phosphorylation-dependent binding of cyclin B1 to a Cdc6-like domain of human separase.
P2860
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P2860
Crystal structure and mutational analysis of the Saccharomyces cerevisiae cell cycle regulatory protein Cks1: implications for domain swapping, anion binding and protein interactions
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2000 nî lūn-bûn
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2000 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
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2000 թվականի օգոստոսին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年論文
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2000年论文
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Crystal structure and mutation ...... nding and protein interactions
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Crystal structure and mutation ...... nding and protein interactions
@en
Crystal structure and mutation ...... nding and protein interactions
@nl
type
label
Crystal structure and mutation ...... nding and protein interactions
@ast
Crystal structure and mutation ...... nding and protein interactions
@en
Crystal structure and mutation ...... nding and protein interactions
@nl
prefLabel
Crystal structure and mutation ...... nding and protein interactions
@ast
Crystal structure and mutation ...... nding and protein interactions
@en
Crystal structure and mutation ...... nding and protein interactions
@nl
P2093
P921
P3181
P1433
P1476
Crystal structure and mutation ...... nding and protein interactions
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P2093
P304
P3181
P356
10.1016/S0969-2126(00)00175-1
P577
2000-08-01T00:00:00Z