Zobrazeno 1 - 10
of 235
pro vyhledávání: '"Y, Benyamin"'
Publikováno v:
Journal of Muscle Research and Cell Motility. 16:543-552
We have purified dystrophin from Torpedo marmorata electric tissue by means of alkaline extraction in conjunction with an affinity chromatography column using anti-peptide antibodies. Using solution (cosedimentation) and solid phase experiments (sedi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c8b617f56b26ca58457c75e26b19cbf
https://doi.org/10.1007/bf00126438
https://doi.org/10.1007/bf00126438
Publikováno v:
Biochemical and Biophysical Research Communications. 209:426-432
Whereas the interaction of the N-terminal domain of gelsolin with monomeric actin is well known, the location of domains 2-3 interacting with the actin filament during the severing process remains uncertain. In this study we define an interface that
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03c967f485bb3119095b3db92508830e
https://doi.org/10.1006/bbrc.1995.1520
https://doi.org/10.1006/bbrc.1995.1520
Autor:
Etienne Audemard, C. Roustan, Marie-Christine Lebart, C. Méjean, Y. Benyamin, Jean Derancourt, D Casanova
Publikováno v:
Journal of Biological Chemistry. 269:4279-4284
We have isolated an NH2-terminal fragment of filamin (M(r) = 70,000) after digestion with Staphylococus aureus V8 protease. This fragment was shown to interact with filamentous actin in cosedimentation assays. Using cross-reactive anti-peptides antib
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0acff79265753278848c9186037c64f3
https://doi.org/10.1016/s0021-9258(17)41775-3
https://doi.org/10.1016/s0021-9258(17)41775-3
Publikováno v:
Journal of Biological Chemistry. 268:5642-5648
The interaction between alpha-actinin and actin was further characterized using natural and synthetic peptides of actin together with anti-actin antibodies of known specificity. We demonstrated that two alpha-actinin binding sequences on actin are lo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::14a9a65ee2f5f60f607805be571caf0f
https://doi.org/10.1016/s0021-9258(18)53368-8
https://doi.org/10.1016/s0021-9258(18)53368-8
Publikováno v:
European Journal of Biochemistry. 209:555-562
The interface between gizzard filamin and skeletal muscle actin was located on the actin monomer. Conserved sequences 105-120 and 360-372, in the actin subdomain 1 near the myosin binding sites, were involved in this interaction. The corresponding pe
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53bb12c78d6bd230755a2eaac133e33d
https://doi.org/10.1111/j.1432-1033.1992.tb17320.x
https://doi.org/10.1111/j.1432-1033.1992.tb17320.x
Publikováno v:
European Journal of Biochemistry. 206:251-257
Scallop muscle arginine kinase binds to F-actin from mollusc and rabbit muscle in vitro. One site of interaction appears to be located in residues 305-325 of a C-terminal fragment (residues 285-375) of actin. The binding is hindered in the presence o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::378c3fb49428b7ec1164fa560869d9b7
https://doi.org/10.1111/j.1432-1033.1992.tb16923.x
https://doi.org/10.1111/j.1432-1033.1992.tb16923.x
Publikováno v:
Biological Journal of the Linnean Society. 41:163-169
An immunological test that can be made on living animals is developed to identify M. m. musculus mice from the two other short-tailed mice (M. spicilegus and M. spretoides) occurring in Eastern Europe. This test uses fractionated albumin antiserum as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f01bbe531dc38e5ef98a9ce25edd0d36
https://doi.org/10.1111/j.1095-8312.1990.tb00827.x
https://doi.org/10.1111/j.1095-8312.1990.tb00827.x
Publikováno v:
Experientia. 46:303-307
Three closely related species of short-tailed mice (Mus musculus musculus, M. spretoides and M. spicilegus) were tentatively discriminated using immunological techniques based on albumin cross-reactivity. Different fractionations of crude albumin ant
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6ffae38195af3758ebf931cac8908ecd
https://doi.org/10.1007/bf01951773
https://doi.org/10.1007/bf01951773
Publikováno v:
Acta physiologica Scandinavica. 185(1)
Aim: The ubiquitin-proteasome system is known to be involved in many situations leading to skeletal muscle atrophy. However, the cellular mechanisms triggering the atrophic process initiation are still poorly understood. For short periods of rat hind
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90bcb2806682be46c07944c80b6c76fe
https://pubmed.ncbi.nlm.nih.gov/16128695
https://pubmed.ncbi.nlm.nih.gov/16128695
Publikováno v:
European journal of biochemistry. 268(24)
ADF/cofilins are actin binding proteins that bind actin close to both the N- and C-termini (site 1), and we have found a second cofilin binding site (site 2) centered around helix 112-125 [Renoult, C., Ternent, D., Maciver, S.K., Fattoum, A., Astier,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::aedd2900d2b53bba5d3f5274c5aca97f
https://pubmed.ncbi.nlm.nih.gov/11737197
https://pubmed.ncbi.nlm.nih.gov/11737197