نتایج جستجو برای: tropomyosin

تعداد نتایج: 4091  

Journal: :The Journal of Cell Biology 1993
P Vibert R Craig W Lehman

Caldesmon is known to inhibit actomyosin ATPase and filament sliding in vitro, and may play a role in modulating smooth muscle contraction as well as in diverse cellular processes including cytokinesis and exocytosis. However, the structural basis of caldesmon action has not previously been apparent. We have recorded electron microscope images of negatively stained thin filaments containing cal...

2016
Lorenzo R. Sewanan Jeffrey R. Moore William Lehman Stuart G. Campbell

Point mutations to the human gene TPM1 have been implicated in the development of both hypertrophic and dilated cardiomyopathies. Such observations have led to studies investigating the link between single residue changes and the biophysical behavior of the tropomyosin molecule. However, the degree to which these molecular perturbations explain the performance of intact sarcomeres containing mu...

Journal: :Current Biology 2012
Alex R. Hodges Elena B. Krementsova Carol S. Bookwalter Patricia M. Fagnant Thomas E. Sladewski Kathleen M. Trybus

Myosin V is an actin-based motor protein involved in intracellular cargo transport [1]. Given this physiological role, it was widely assumed that all class V myosins are processive, able to take multiple steps along actin filaments without dissociating. This notion was challenged when several class V myosins were characterized as nonprocessive in vitro, including Myo2p, the essential class V my...

Journal: :The Journal of biological chemistry 1997
K Kashiwada W Nishida K Hayashi K Ozawa Y Yamanaka H Saga T Yamashita M Tohyama S Shimada K Sato K Sobue

Isoform diversity of tropomyosin is generated from the limited genes by a combination of differential transcription and alternative splicing. In the case of the alpha-tropomyosin (alpha-TM) gene, exon 2a rather than exon 2b is specifically spliced in alpha-TM-SM mRNA, which is one of the major tropomyosin isoforms in smooth muscle cells. Here we demonstrate that expressions of alpha-tropomyosin...

2017
Danielle M. Paul John M. Squire Edward P. Morris

The structures of muscle thin filaments reconstituted using skeletal actin and cardiac troponin and tropomyosin have been determined with and without bound Ca2+ using electron microscopy and reference-free single particle analysis. The resulting density maps have been fitted with atomic models of actin, tropomyosin and troponin showing that: (i) the polarity of the troponin complex is consisten...

2010
Renato E Rossi Giorgio Monasterolo Cristoforo Incorvaia Philippe Moingeon Franco Frati Giovanni Passalacqua Lucilla Rossi Giorgio W Canonica

BACKGROUND Some studies reported the possible induction of food allergy, caused by neo-sensitization to cross-reacting allergens, during immunotherapy with aeroallergens, while other studies ruled out such possibility. OBJECTIVES The aim of this study was to evaluate the development of neo-sensitization to Pen a 1 (tropomyosin) as well as the appearance of reactions after ingestion of foods c...

Journal: :The Journal of Cell Biology 2003
Ryan E. Mudry Cynthia N. Perry Meredith Richards Velia M. Fowler Carol C. Gregorio

Actin (thin) filament length regulation and stability are essential for striated muscle function. To determine the role of the actin filament pointed end capping protein, tropomodulin1 (Tmod1), with tropomyosin, we generated monoclonal antibodies (mAb17 and mAb8) against Tmod1 that specifically disrupted its interaction with tropomyosin in vitro. Microinjection of mAb17 or mAb8 into chick cardi...

2001
Mary D. Pato Lawrence B. Smillie

The interactions of a variety of large fragments of rabbit skeletal muscle a-tropomyosin, prepared as previously described, with troponin-T and a soluble tropomyosin-binding fragment of troponin-T (CB1) have been investigated by affinity chromatography and gel filtration. No specific interactions between NHz-terminal fragments encompassing residues 1-189 with troponin, troponin-T, or CB1 immobi...

Journal: :The Journal of Cell Biology 1993
V M Fowler M A Sussmann P G Miller B E Flucher M P Daniels

The length and spatial organization of thin filaments in skeletal muscle sarcomeres are precisely maintained and are essential for efficient muscle contraction. While the major structural components of skeletal muscle sarcomeres have been well characterized, the mechanisms that regulate thin filament length and spatial organization are not well understood. Tropomodulin is a new, 40.6-kD tropomy...

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