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Calmodulin and Its Binding Proteins in Parkinson’s Disease
Parkinson’s disease (PD) is a neurodegenerative disorder that manifests with rest tremor, muscle rigidity and movement disturbances. At the microscopic level it is characterized by formation of specific intraneuronal inclusions, called Lewy bodies (LBs),
Serge Weis +2 more
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PLANT-SPECIFIC CALMODULIN-BINDING PROTEINS
Annual Review of Plant Biology, 2005Calmodulin CaM is a ubiquitous Ca2+sensor protein (16 to 18 kD) with no catalytic activity that can, upon binding Ca2+, activate target proteins involved in various cellular processes. The CaM prototype is comprised of two globular domains connected with a long flexible helix. Each globular domain contains a pair of intimately linked EF hands.
Bouche, Nicolas +3 more
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Calmodulin-binding proteins of Saccharomycescerevisiae
Biochemical and Biophysical Research Communications, 1990The subcellular distribution of calmodulin-binding proteins in the soluble, plasma membrane, and nuclear fractions of Saccharomyces cerevisiae was analyzed with a gel binding assay using 125I-labeled calmodulin. Over 20 binding proteins were detected. The calmodulin-binding protein profiles were markedly different among the fractions.
Y S, Liu +3 more
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Planta, 1996
A 21-kDa calmodulin (CaM)-binding protein and a 19-kDa calmodulin-binding protein were detected in 0.1 M CaCl2 extracts of Angelica dahurica L. suspension-cultured cells and carrot (Daucus carota L.) suspension-cultured cells, respectively, using a biotinylated cauliflower CaM gel-overlay technique in the presence of 1 mM Ca2+.
Tang, Jun +3 more
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A 21-kDa calmodulin (CaM)-binding protein and a 19-kDa calmodulin-binding protein were detected in 0.1 M CaCl2 extracts of Angelica dahurica L. suspension-cultured cells and carrot (Daucus carota L.) suspension-cultured cells, respectively, using a biotinylated cauliflower CaM gel-overlay technique in the presence of 1 mM Ca2+.
Tang, Jun +3 more
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Calmodulin-binding protein kinases in plants
Trends in Plant Science, 2003Many calmodulin-binding protein kinases have been isolated from plants. Plant calmodulin-binding protein kinases are novel protein kinases that differ from calcium-dependent protein kinases in many important respects. Calmodulin-binding protein kinases are likely to be crucial mediators of responses to diverse endogenous and environmental cues in ...
Lei, Zhang, Ying-Tang, Lu
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Calmodulin-binding protein of erythrocyte cytoskeleton
Biochemical and Biophysical Research Communications, 1981Abstract Previously we have shown that purified spectrin binds calmodulin in the presence of Ca2+ with a Kd value of 3 μM (Sobue, K. et al. (1980) Biochemistry International 1, 561–566). We now provide evidence that the calmodulin-binding activity found in the human erythrocyte cytoskeleton is indeed due to spectrin and no other binding proteins are ...
K, Sobue +3 more
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CALMODULIN-BINDING PROTEINS IN BRAIN
Neurochemistry International, 1983It is now widely accepted that actions of intracellular Ca(2+) are mediated by a four-domain Ca(2+)-binding protein, calmodulin. Brain is especially rich in calmodulin, containing about 400 mg (24 ?mol) of EGTA-extractable calmodulin per kg of brain. However, only a fraction of the above amount is required for the calmodulin-activated enzymes and most ...
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CALMODULIN AND CALMODULIN-BINDING PROTEINS IN PLANTS
Annual Review of Plant Physiology and Plant Molecular Biology, 1998▪ Abstract Calmodulin is a small Ca2+-binding protein that acts to transduce second messenger signals into a wide array of cellular responses. Plant calmodulins share many structural and functional features with their homologs from animals and yeast, but the expression of multiple protein isoforms appears to be a distinctive feature of higher plants ...
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Calmodulin-binding proteins of Tetrahymena microsomal membranes
Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1985Tetrahymena calmodulin radioiodinated with a lactoperoxidase method retained full ability to activate Tetrahymena guanylate cyclase. Binding of [125I]calmodulin to Tetrahymena microsomal membranes was Ca2+-dependent and inhibited by excess unlabeled calmodulin or trifluoperazine.
S, Nagao, Y, Nozawa
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Ca2+/calmodulin-binding proteins in Dictyostelium discoideum
Research in Microbiology, 1991We have initiated a systematic study of Ca2+/calmodulin-regulated enzymes in the cellular slime mold Dictyostelium discoideum. Using 125I-labelled D. discoideum calmodulin (CaM) as a functional probe, several Ca2+/CaM-binding proteins were detected in crude cell lysates.
T, Winckler, H, Dammann, R, Mutzel
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