نتایج جستجو برای: myosin light chain kinase

تعداد نتایج: 898607  

Journal: :The Journal of Cell Biology 1994
B D Ostrow P Chen R L Chisholm

In a number of systems phosphorylation of the regulatory light chain (RMLC) of myosin regulates the activity of myosin. In smooth muscle and vertebrate nonmuscle systems RMLC phosphorylation is required for contractile activity. In Dictyostelium discoideum phosphorylation of the RMLC regulates both ATPase activity and motor function. We have determined the site of phosphorylation on the Dictyos...

Journal: :Current Biology 2008
Nelson R. Alexander Kevin M. Branch Aron Parekh Emily S. Clark Izuchukwu C. Iwueke Scott A. Guelcher Alissa M. Weaver

Invadopodia are actin-rich subcellular protrusions with associated proteases used by cancer cells to degrade extracellular matrix (ECM) [1]. Molecular components of invadopodia include branched actin-assembly proteins, membrane trafficking proteins, signaling proteins, and transmembrane proteinases [1]. Similar structures exist in nontransformed cells, such as osteoclasts and dendritic cells, b...

پایان نامه :وزارت علوم، تحقیقات و فناوری - دانشگاه شیراز - دانشکده کشاورزی 1392

هدف از این پژوهش بررسی میزان متیلاسیون شماری از ژنهای مهم مرغ بود. بدین منظور 32 ژن از genbank انتخاب شد. پروموتورهای این ژنها با نرم افزار promoter prediction پیدا شدند. جزایر احتمالی موجود در هر توالی با نرم افزار cpg island searcher مشخص شدند. احتمال متیله شدن هر رشته dna یک ژن، با نرم افزار methylator و آنالیز متیلاسیون با نرم افزار epigraph انجام شد. در نهایت با استفاده از مدل مارکف پنهان،...

Journal: :The Biochemical journal 2002
Mitsuo Mita Hayato Yanagihara Shigeru Hishinuma Masaki Saito Michael P Walsh

Depolarization of the sarcolemma of smooth muscle cells activates voltage-gated Ca2+ channels, influx of Ca2+ and activation of cross-bridge cycling by phosphorylation of myosin catalysed by Ca2+/calmodulin-dependent myosin light-chain kinase (MLCK). Agonist stimulation of smooth muscle contraction often involves other kinases in addition to MLCK. In the present study, we address the hypothesis...

Journal: :The Biochemical journal 1999
E Leclerc C Corti H Schmid S Vetter P James E Carafoli

The interaction of serine/threonine-phosphorylated calmodulin with synthetic peptides corresponding to the calmodulin-binding domains of six enzymes has been studied by fluorescence spectroscopy. For five peptides, the dissociation constant of the calmodulin-peptide complex (K(d)) increased when calmodulin was phosphorylated. An increase of more than one order of magnitude was observed with pep...

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