نتایج جستجو برای: reactive tropomyosin

تعداد نتایج: 160509  

Journal: :The Journal of Cell Biology 1976
E Lazarides

During the spreading of a population of rat embryo cells, approximately 40% of the cells develop a strikingly regular network which precedes the formation of the straight actin filament bundles seen in the fully spread out cells. Immunofluorescence studies with antibodies specific for the skeletal muscle structural proteins actin, alpha-actinin, and tropomyosin indicate that this network is com...

Journal: :American journal of physiology. Gastrointestinal and liver physiology 2006
Sita Somara Khalil N Bitar

Thin-filament regulation of smooth muscle contraction involves phosphorylation, association, and dissociation of contractile proteins in response to agonist stimulation. Phosphorylation of caldesmon weakens its association with actin leading to actomyosin interaction and contraction. Present data from colonic smooth muscle cells indicate that acetylcholine induced a significant association of c...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1995
M Gimona A Watakabe D M Helfman

Tropomyosins consist of nearly 100% alpha-helix and assemble into parallel and in-register coiled-coil dimers. In vitro it has been established that nonmuscle as well as native muscle tropomyosins can form homodimers. However, a mixture of muscle alpha and beta tropomyosin subunits results in the formation of the thermodynamically more stable alpha/beta heterodimer. Although the assembly prefer...

Journal: :The Biochemical journal 1973
B Bullard R Dabrowska L Winkelman

1. Myosin, actin and the regulatory proteins were prepared from insect flight muscle. 2. The light subunit composition of the myosin differed from that of vertebrate muscle myosin. The ionic strength and pH dependence of the myosin adenosine triphosphatase (ATPase) were measured. 3. Actin was associated with a protein of subunit molecular weight 55000 and was purified by gel filtration. Impure ...

Journal: :Human molecular genetics 2012
Julien Ochala David S Gokhin Isabelle Pénisson-Besnier Susana Quijano-Roy Nicole Monnier Joël Lunardi Norma B Romero Velia M Fowler

In humans, congenital myopathy-linked tropomyosin mutations lead to skeletal muscle dysfunction, but the cellular and molecular mechanisms underlying such dysfunction remain obscure. Recent studies have suggested a unifying mechanism by which tropomyosin mutations partially inhibit thin filament activation and prevent proper formation and cycling of myosin cross-bridges, inducing force deficits...

Journal: :The Journal of Experimental Medicine 1980
B N Manjula V A Fischetti

Partial sequences of three immunologically distinct group A streptococcal M proteins (M5, M6, and M24) revealed significant homology with each other, certain amino acid residues being conserved within the three molecules. In addition, a common feature of the sequenced regions of these M proteins was their high alpha-helical potential and the presence of a repeating seven residue periodicity tha...

Journal: :Circulation research 2014
Meera Cozhimuttam Viswanathan Gaurav Kaushik Adam J Engler William Lehman Anthony Cammarato

RATIONALE Regulation of striated muscle contraction is achieved by Ca2+ -dependent steric modulation of myosin cross-bridge cycling on actin by the thin filament troponin-tropomyosin complex. Alterations in the complex can induce contractile dysregulation and disease. For example, mutations between or near residues 112 to 136 of cardiac troponin-T, the crucial TnT1 (N-terminal domain of troponi...

Journal: :The Journal of biological chemistry 1992
L A Sung V M Fowler K Lambert M A Sussman D Karr S Chien

Human erythrocyte tropomodulin is a novel tropomyosin regulatory protein that binds to the end of erythrocyte tropomyosin and blocks heat-to-tail association of tropomyosin along actin filaments. It has been proposed to play a role in modulating the association of tropomyosin with the spectrin-actin complex in the erythrocyte membrane skeleton. Immunoscreening of a human fetal liver cDNA expres...

Journal: :The Biochemical journal 1998
M El-Mezgueldi O Copeland I D Fraser S B Marston P A Huber

Recent analysis has shown the presence of three sequences in the C-terminal 170 amino acids of human caldesmon (domain 4) which are involved in actin binding and tropomyosin-dependent inhibition of actomyosin ATPase. Two are in domain 4b (amino acids 715-793) and one is in domain 4a (amino acids 636-714). In the present work we have compared recombinant peptides containing either domain 4a or d...

Journal: :The Journal of pharmacology and experimental therapeutics 1999
K Matsunaga K Nakatani M Murakami K Yamaguchi Y Ohizumi

Goniodomin A has been shown to cause the conformational change of actin to modify actomyosin ATPase activity. Goniodomin A induced a potent stimulation of the actomyosin ATPase activities of the actin-myosin reconstituted system and natural actomyosin in the range of 10(-8) to 10(-7) M. When the concentration was increased above 10(-7) M, actomyosin ATPase activity was decreased. Interestingly,...

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