Zobrazeno 1 - 10
of 30
pro vyhledávání: '"Myosin tail"'
Autor:
Bosch, Jürgen, Turley, Stewart, Daly, Thomas M., Bogh, Stephen M., Villasmil, Michelle L., Roach, Claudia, Zhou, Na, Morrisey, Joanne M., Vaidya, Akhil B., Bergman, Lawrence W., Hol, Wim G. J.
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 2006 Mar . 103(13), 4852-4857.
Externí odkaz:
https://www.jstor.org/stable/30048710
Autor:
Ashley L. Arthur, Fernanda Pires Borrega, Carlos Kikuti, Livia D. Songster, Anne Houdusse, Akash Bhattacharya, Margaret A. Titus, Helena Sirkia
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2019, 116 (44), pp.22196-22204. ⟨10.1073/pnas.1901527116⟩
Proceedings of the National Academy of Sciences of the United States of America, National Academy of Sciences, 2019, 116 (44), pp.22196-22204. ⟨10.1073/pnas.1901527116⟩
Filopodia are actin-filled protrusions employed by cells to interact with their environment. Filopodia formation in Amoebozoa and Metazoa requires the phylogenetically diverse MyTH4-FERM (MF) myosins DdMyo7 and Myo10, respectively. While Myo10 is kno
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d4cc047891834252c270832ea60db1d
https://hal.archives-ouvertes.fr/hal-02349330
https://hal.archives-ouvertes.fr/hal-02349330
Autor:
Saswata S. Sarkar, Arjun S. Adhikari, James A. Spudich, Kathleen M. Ruppel, Margaret S. Sunitha, Darshan V. Trivedi, Shirley Sutton, Suman Nag
A working model for β-cardiac myosin in the sequestered state and binding assays reveal interactions between the myosin head and tail that are disrupted by mutations associated with hypertrophic cardiomyopathy. Hypertrophic cardiomyopathy (HCM) is p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2d3edf3242c7b9995cad154215671263
https://europepmc.org/articles/PMC5737966/
https://europepmc.org/articles/PMC5737966/
Autor:
Moisés Wasserman, Isabel C Castellanos, Paula C. Hernández, Liliana Morales, Jacqueline Chaparro-Olaya
Publikováno v:
Repositorio U. El Bosque
Universidad El Bosque
instacron:Universidad El Bosque
Universidad El Bosque
instacron:Universidad El Bosque
The mobility and invasion strategy of Plasmodium falciparum is governed by a protein complex known as the glideosome, which contains an actin-myosin motor. It has been shown that myosin A of the parasite (PfMyoA) is the myosin of the glideosome, and
Publikováno v:
Journal of Aquatic Food Product Technology. 24:698-711
Biochemical and rheological properties of surimi were examined based on: (a) salting time (from 18 to 3 min) while maintaining 21 min for total chopping time; and (b) total chopping time (from 6 to 21 min) while salting during the final 3 min. Extend
Publikováno v:
Fisheries Science. 71:662-671
The effect of salt concentration on the thermal denaturation profile of myosin in walleye pollack and carp myofibrils was compared by studying the subfragment-1 (S-1) and rod denaturation rates upon heating. Species-specific denaturation mode observe
Autor:
Ludmila Skubiszak, Leszek Kowalczyk
Publikováno v:
Acta Biochimica Polonica. 49:829-840
Computer modelling related to the real dimensions of both the whole filament and the myosin molecule subfragments has revealed two alternative modes for myosin molecule packing which lead to the head disposition similar to that observed by EM on the
Autor:
Peter Simpson, Anthony A. Holder, Stephen R. Martin, Judith L. Green, Ronald I. Howson, Jemima C. Thomas, Edward W. Tate, D.K. Moss, Ernesto Cota
Publikováno v:
Molecular bioSystems. 6(3)
The myosin tail domain interacting protein-myosin A (MTIP-MyoA) protein complex is an essential element of the motor driving invasion of red blood cells by the Plasmodium species that cause malaria. Here we report the key determinants of binding at t
Autor:
Gerald Offer
Publikováno v:
Journal of Molecular Biology. 216:213-218
Sharp bends have previously been observed in the tail of the skeletal myosin molecule at well-defined positions 44, 75 and 135 nm from the head-tail junction, and in vertebrate smooth myosin at two positions about 45 and 96 nm from this junction. The
Publikováno v:
Journal of molecular biology. 377(2)
Numerous types of biological motion are driven by myosin thick filaments. Although the exact structure of the filament backbone is not known, it has long been hypothesized that periodically arranged charged regions along the myosin tail are the main