Vertebrate and yeast calmodulin, despite significant sequence divergence, are functionally interchangeable.
about
Identification of a new mammalian centrin gene, more closely related to Saccharomyces cerevisiae CDC31 geneInteraction with calmodulin is required for the function of Spc110p, an essential component of the yeast spindle pole body.Mutations in yeast calmodulin cause defects in spindle pole body functions and nuclear integrity.Direct interaction between yeast spindle pole body components: Kar1p is required for Cdc31p localization to the spindle pole bodyHsl7 localizes to a septin ring and serves as an adapter in a regulatory pathway that relieves tyrosine phosphorylation of Cdc28 protein kinase in Saccharomyces cerevisiae.Regulatory subunit (CNB1 gene product) of yeast Ca2+/calmodulin-dependent phosphoprotein phosphatases is required for adaptation to pheromone.Mlc1p is a light chain for the unconventional myosin Myo2p in Saccharomyces cerevisiae.Calmodulin concentrates at regions of cell growth in Saccharomyces cerevisiae.Role of calmodulin and Spc110p interaction in the proper assembly of spindle pole body compenents.Presynaptic Calmodulin targets: lessons from structural proteomics.Calmodulins with deletions in the central helix functionally replace the native protein in yeast cellsProtein A-calmodulin fusions: a novel approach for investigating calmodulin function in yeast.Study of calcium signaling in non-excitable cells.Calcium binding is required for calmodulin function in Aspergillus nidulansCharacterization of green alga, yeast, and human centrins. Specific subdomain features determine functional diversity.Identification of functional connections between calmodulin and the yeast actin cytoskeleton.Multiple Ca2+/calmodulin-dependent protein kinase genes in a unicellular eukaryote.Lessons in Protein Design from Combined Evolution and Conformational Dynamics.Structural analysis of wild-type and mutant yeast calmodulins by limited proteolysis and electrospray ionization mass spectrometry.A temperature-sensitive calmodulin mutant loses viability during mitosis.Conserved properties of individual Ca2+-binding sites in calmodulinDownward causation by information control in micro-organisms.The transient receptor potential, TRP4, cation channel is a novel member of the family of calmodulin binding proteins.Sequential assignment of 1H, 15N, 13C resonances and secondary structure of human calmodulin-like protein determined by NMR spectroscopy.Structure-based systematic isolation of conditional-lethal mutations in the single yeast calmodulin gene.Calcium triggers reversal of calmodulin on nested anti-parallel sites in the IQ motif of the neuronal voltage-dependent sodium channel NaV1.2.From common signalling components to cell specific responses: insights from the cereal aleurone.Ca2+Binding to Calmodulin and Its Role inSchizosaccharomyces pombeas Revealed by Mutagenesis and NMR Spectroscopy
P2860
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P2860
Vertebrate and yeast calmodulin, despite significant sequence divergence, are functionally interchangeable.
description
1989 nî lūn-bûn
@nan
1989 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Vertebrate and yeast calmoduli ...... functionally interchangeable.
@ast
Vertebrate and yeast calmoduli ...... functionally interchangeable.
@en
Vertebrate and yeast calmoduli ...... functionally interchangeable.
@nl
type
label
Vertebrate and yeast calmoduli ...... functionally interchangeable.
@ast
Vertebrate and yeast calmoduli ...... functionally interchangeable.
@en
Vertebrate and yeast calmoduli ...... functionally interchangeable.
@nl
prefLabel
Vertebrate and yeast calmoduli ...... functionally interchangeable.
@ast
Vertebrate and yeast calmoduli ...... functionally interchangeable.
@en
Vertebrate and yeast calmoduli ...... functionally interchangeable.
@nl
P2860
P356
P1476
Vertebrate and yeast calmoduli ...... functionally interchangeable.
@en
P2093
P2860
P304
P356
10.1073/PNAS.86.20.7909
P407
P577
1989-10-01T00:00:00Z