CMD1/YBR109C Literature Guide Help

Other names published for CMD1: CaM, YBR109C

CMD1 - Protein Sequence Features (22)

ReferenceOther Genes Addressed
Lu KY, et al.  (2012) Profiling lipid-protein interactions using nonquenched fluorescent liposomal nanovesicles and proteome microarrays. Mol Cell Proteomics 11(11):1177-90
Nakashima K, et al.  (2012) Specific conformation and Ca(2+)-binding mode of yeast calmodulin: insight into evolutionary development. J Biochem 152(1):27-35
Ogura K, et al.  (2012) Solution structures of yeast Saccharomyces cerevisiae calmodulin in calcium- and target peptide-bound states reveal similarities and differences to vertebrate calmodulin. Genes Cells 17(3):159-72
Yokouchi T, et al.  (2003) Solution X-ray scattering data show structural differences among chimeras of yeast and chicken calmodulin: implications for structure and function. Biochemistry 42(7):2195-201
Ishida H, et al.  (2002) The solution structure of apocalmodulin from Saccharomyces cerevisiae implies a mechanism for its unique Ca2+ binding property. Biochemistry 41(52):15536-42
Ishida H, et al.  (2000) Solution structures of the N-terminal domain of yeast calmodulin: Ca2+-dependent conformational change and its functional implication. Biochemistry 39(45):13660-8
Lee SY and Klevit RE  (2000) The whole is not the simple sum of its parts in calmodulin from S. cerevisiae. Biochemistry 39(15):4225-30
Yazawa M, et al.  (1999) A strange calmodulin of yeast. Mol Cell Biochem 190(1-2):47-54
Rayner TF and Stark MJ  (1998) Identification and characterization of the KlCMD1 gene encoding Kluyveromyces lactis calmodulin. Yeast 14(9):869-75
Nakashima K, et al.  (1996) Chimeras of yeast and chicken calmodulin demonstrate differences in activation mechanisms of target enzymes. Biochemistry 35(17):5602-10
Harris E, et al.  (1995) Gain-of-function mutations in a human calmodulin-like protein identify residues critical for calmodulin action in yeast. Mol Gen Genet 247(2):137-47
Brockerhoff SE, et al.  (1994) The unconventional myosin, Myo2p, is a calmodulin target at sites of cell growth in Saccharomyces cerevisiae. J Cell Biol 124(3):315-23
Harris E, et al.  (1994) Functional consequences in yeast of single-residue alterations in a consensus calmodulin. J Cell Sci 107 ( Pt 11):3235-49
Ohya Y and Botstein D  (1994) Diverse essential functions revealed by complementing yeast calmodulin mutants. Science 263(5149):963-6
Matsuura I, et al.  (1993) Mutagenesis of the fourth calcium-binding domain of yeast calmodulin. J Biol Chem 268(18):13267-73
Sun GH, et al.  (1992) Mutations in yeast calmodulin cause defects in spindle pole body functions and nuclear integrity. J Cell Biol 119(6):1625-39
Matsuura I, et al.  (1991) A site-directed mutagenesis study of yeast calmodulin. J Biochem 109(1):190-7
Persechini A, et al.  (1991) Calmodulins with deletions in the central helix functionally replace the native protein in yeast cells. Proc Natl Acad Sci U S A 88(2):449-52
Sun GH, et al.  (1991) Half-calmodulin is sufficient for cell proliferation. Expressions of N- and C-terminal halves of calmodulin in the yeast Saccharomyces cerevisiae. J Biol Chem 266(11):7008-15
Luan Y, et al.  (1987) Yeast calmodulin: structural and functional differences compared with vertebrate calmodulin. J Biochem 102(6):1531-7
Ohya Y, et al.  (1987) Purification and biochemical properties of calmodulin from Saccharomyces cerevisiae. Eur J Biochem 168(1):13-9
Davis TN, et al.  (1986) Isolation of the yeast calmodulin gene: calmodulin is an essential protein. Cell 47(3):423-31