Výsledky vyhledávání

Sulfide sensitivity in fishes of the Indian River lagoon, Florida

Autor: L E, Greene, E, Van Handel

Publikováno v: Journal of the American Mosquito Control Association. 8(1)

Lagoon fishes, in netted holding cages, were placed in an impounded salt marsh and submitted to a gradient of sulfide-rich artesian well water. Near the well head, all specimens of 13 species died within 5-45 min, while all individuals of 5 species s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::3419b166c2957b7817f3aa0dcb37d3d8
https://pubmed.ncbi.nlm.nih.gov/1583499

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Uncoating of coated vesicles by yeast hsp70 proteins

Autor: B C, Gao, J, Biosca, E A, Craig, L E, Greene, E, Eisenberg

Publikováno v: The Journal of biological chemistry. 266(29)

The ability of hsp70 isoenzymes from wild-type and mutant yeast strains to uncoat bovine brain coated vesicles was analyzed and compared with that of the brain uncoating ATPase. Results show that, among the four major cytoplasmic isoenzymes produced

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6b6e21008dacef1427cdef73078d2ea7
https://pubmed.ncbi.nlm.nih.gov/1833403

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Dissociation of clathrin from coated vesicles by the uncoating ATPase

Autor: L E, Greene, E, Eisenberg

Publikováno v: The Journal of biological chemistry. 265(12)

The uncoating ATPase has been shown to dissociate clathrin from both clathrin-coated vesicles and synthetic clathrin baskets (Rothman, J. E., and Schmid, S. L. (1986) Cell 46, 5-9). In the present study, we investigated the mechanism of action of the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c9eb268729aa29300e9a22e68b8b3f8e
https://pubmed.ncbi.nlm.nih.gov/1969864

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Dissociation of the actin.subfragment 1 complex by adenyl-5'-yl imidodiphosphate, ADP, and PPi

Autor: E Eisenberg, L E Greene

Publikováno v: Journal of Biological Chemistry. 255:543-548

The ability of adenyl-5'-yl imidodiphosphate (AMP-PNP), ADP, and PPi to dissociate the actin.myosin subfragment 1 (S-1) complex was studied using an analytical ultracentrifuge with UV optics, which enabled the direct determination of the dissociated

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::525a65cf109cbecddca7d0357203b38c
https://doi.org/10.1016/s0021-9258(19)86209-9

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Reaction of cardiac myosin with a purine disulfide analog of adenosine triphosphate. II. Stoichiometry and subunit location of labeling

Autor: R G Yount, L E Greene

Publikováno v: Journal of Biological Chemistry. 252:1681-1688

The reaction of bovine cardiac myosin with the site-specific purine disulfide analog of ATP, 6,6'-dithiobis (inosinyl imidodiphosphate), was studied to determine the stoichiometry of labeling and subunit location of the reactive cysteines. The analog

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::4e6ea3624a973b17d6702ca71b99ad89
https://doi.org/10.1016/s0021-9258(17)40602-8

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Cooperative binding of myosin subfragment one to regulated actin as measured by fluorescence changes of troponin I modified with different fluorophores

Autor: L E Greene

Publikováno v: Journal of Biological Chemistry. 261:1279-1285

Binding studies of myosin subfragment one (S-1) to regulated actin in the presence and absence of Ca2+ indicate that, as S-1 binds to regulated actin, tropomyosin-actin units undergo a cooperative transition from a weak to a strong S-1-binding form.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0864e41cfefef5b85923a174602ccfc9
https://doi.org/10.1016/s0021-9258(17)36087-8

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Stoichiometry of actin X S-1 cross-linked complex

Autor: L E Greene

Publikováno v: Journal of Biological Chemistry. 259:7363-7366

Mornet et al. ( Mornet , D., Bertrand , R., Pantel , P., Audemard , E., Kassab , R. (1981) Nature (Lond.) 292, 301-306) have shown that myosin subfragment 1 (S-1) can be covalently linked to F-actin by the zero-length cross-linker 1-ethyl-3-[3-(dimet

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::7e280c00a09e59d6f659e73488308f7f
https://doi.org/10.1016/s0021-9258(17)42795-5

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Effect of phosphorylation on the binding of smooth muscle heavy meromyosin X ADP to actin

Autor: L E Greene, J R Sellers

Publikováno v: Journal of Biological Chemistry. 262:4177-4181

Relaxation of both smooth and skeletal muscles appears to be caused primarily by inhibition of the step associated with Pi release in the actomyosin ATPase cycle, rather than by a block in the binding of the myosin X ATP and myosin X ADP X Pi complex

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::660260953e5cd287df093369150563a2
https://doi.org/10.1016/s0021-9258(18)61329-8

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Reaction of cardiac myosin with a purine disulfide analog of adenosine triphosphate. I. Kinetics of inactivation and binding of adenylyl imidodiphosphate

Autor: R G Yount, L E Greene

Publikováno v: Journal of Biological Chemistry. 252:1673-1680

Bovine cardiac myosin ATPase activity was rapidly inactivated by the purine disulfide analog of ATP,6,6'-dithiobis(inosinyl imidodiphosphate). Kinetic investigations showed that this analog acted as a site-specific reagent at 0 degrees with a Ki of 1

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::1b45631403971b512704f4c790af03ed
https://doi.org/10.1016/s0021-9258(17)40601-6

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