Zobrazeno 1 - 10
of 27
pro vyhledávání: '"S. Victor Perry"'
Autor:
S. Victor Perry, Clare E. Gallon, Abdellatif Fattoum, Barry A. Levine, Matthew A. Hodgkin, Valerie B. Patchell
Publikováno v:
European Journal of Biochemistry. 269:5088-5100
Peptides corresponding to the N-terminus of skeletal myosin light chain 1 (rsMLC1 1–37) and the short loop of human cardiac β-myosin (hcM398–414) have been shown to interact with skeletal F-actin by NMR and fluorescence measurements. Skeletal tr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::727479e5ee0800baf860972e42364d60
https://doi.org/10.1046/j.1432-1033.2002.03227.x
https://doi.org/10.1046/j.1432-1033.2002.03227.x
Autor:
Barry A. Levine, James S. Evans, S. Victor Perry, Valerie B. Patchell, Yuan Gao, Clare E. Gallon
Publikováno v:
The Journal of biological chemistry. 280(15)
The N terminus of skeletal myosin light chain 1 and the cardiomyopathy loop of human cardiac myosin have been shown previously to bind to actin in the presence and absence of tropomyosin (Patchell, V. B., Gallon, C. E., Hodgkin, M. A., Fattoum, A., P
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d4334ebc569ae2b9d0ebb3bcd3552623
https://pubmed.ncbi.nlm.nih.gov/15695827
https://pubmed.ncbi.nlm.nih.gov/15695827
Autor:
Valerie B, Patchell, Clare E, Gallon, Matthew A, Hodgkin, Abdellatif, Fattoum, S Victor, Perry, Barry A, Levine
Publikováno v:
European journal of biochemistry. 269(20)
Peptides corresponding to the N-terminus of skeletal myosin light chain 1 (rsMLC1 1-37) and the short loop of human cardiac beta-myosin (hcM398-414) have been shown to interact with skeletal F-actin by NMR and fluorescence measurements. Skeletal trop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8391eb71f3b84c73c7d7700f6aa52219
https://pubmed.ncbi.nlm.nih.gov/12383268
https://pubmed.ncbi.nlm.nih.gov/12383268
Autor:
Arthur J. G. Moir, Etienne Audemard, S. Victor Perry, Dominique Mornet, Valerie B. Patchell, Barry A. Levine
Publikováno v:
European journal of biochemistry. 193(3)
The interaction between actin and caldesmon that is associated with the inhibition of actomyosin ATPase activity in smooth muscle has been studied using 1H-NMR spectroscopy. Binding studies using the intact molecules were complemented by the use of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cbe5d928c6e6b69ccdb1c88ced7a1ef5
https://pubmed.ncbi.nlm.nih.gov/2147415
https://pubmed.ncbi.nlm.nih.gov/2147415
Autor:
S. Victor Perry
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1000:159-178
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d8d5d3b646531486afb85bc88ac4a09b
https://doi.org/10.1016/s0006-3002(89)80015-0
https://doi.org/10.1016/s0006-3002(89)80015-0
Autor:
Roger J.A. Grand, S. Victor Perry
Publikováno v:
FEBS Letters. 92:137-142
Recent studies have shown that a troponin C-like protein is present in vertebrate smooth muscle [l-5] . This protein can form Ca”-dependent complexes with troponin I from fast skeletal muscle in a similar manner to those obtained with skeletal musc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ea5bc48654559d8abba2acd26c5d7f0c
https://doi.org/10.1016/0014-5793(78)80739-x
https://doi.org/10.1016/0014-5793(78)80739-x
Publikováno v:
Experimental Cell Research. 122:339-350
1. 1. Immunochemical studies have shown that the major forms of troponin T present in fast skeletal, slow skeletal and cardiac muscles are different proteins. 2. 2. Similar studies indicate that the major form of troponin C present in fast skeletal m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8f15fda3e7faccf7e3ae6d10b0512b12
https://doi.org/10.1016/0014-4827(79)90310-0
https://doi.org/10.1016/0014-4827(79)90310-0
Autor:
S. Victor Perry, Gurtej K. Dhoot
Publikováno v:
Experimental Cell Research. 127:75-87
1. 1. Using the immunoperoxidase staining technique with monospecific antibodies to the polymorphic forms of the components of the troponin complex, two types of cells could be distinguished in rat leg muscles at 18 days' gestation. 2. 2. One kind of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e837517d975e5c34f60b890ad2ba100e
https://doi.org/10.1016/0014-4827(80)90416-4
https://doi.org/10.1016/0014-4827(80)90416-4
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 997:135-143
Regions of rabbit and bovine cardiac troponin T that are involved in binding tropomyosin, troponin C and troponin I have been identified. Two sites of contact for tropomyosin have been located, situated between residues 92–178 and 180–284 of trop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::84f83d573597862d85e2b4d2252ad3ae
https://doi.org/10.1016/0167-4838(89)90145-3
https://doi.org/10.1016/0167-4838(89)90145-3
Publikováno v:
Experimental Cell Research. 117:357-370
1. 1. Antibodies raised against troponin I isolated from human cardiac and rabbit fast and slow skeletal muscles have been shown to be specific for the polymorphic forms of troponin I against which they were raised, i.e. they are tissue specific. 2.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d8b105c9430a7a4bfb4bc5503b19289a
https://doi.org/10.1016/0014-4827(78)90149-0
https://doi.org/10.1016/0014-4827(78)90149-0