Zobrazeno 1 - 10
of 36
pro vyhledávání: '"Lewis C. Gershman"'
Publikováno v:
Biochemistry. 41:6734-6743
We have quantitated the in vitro interactions of profilin and the profilin-actin complex (PA) with the actin filament barbed end using profilin and nonmuscle beta,gamma-actin prepared from bovine spleen. Actin filament barbed end elongation was initi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fc1d544b1ee360e7fe522b2130a4b0e1
https://doi.org/10.1021/bi016083t
https://doi.org/10.1021/bi016083t
Publikováno v:
Biochemistry. 39:13176-13188
The interaction of profilin and non-muscle beta,gamma-actin prepared from bovine spleen has been investigated under physiologic ionic conditions. Profilin binding to actin decreases the affinity of actin for MgADP and MgATP by about 65- and 13-fold,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e99a0731cc48a6607cad2ad532bb45c3
https://doi.org/10.1021/bi001520+
https://doi.org/10.1021/bi001520+
Publikováno v:
Biochemistry. 39:64-74
A covalently linked actin dimer is identified in solutions of actin prepared from an acetone powder from skeletal muscle. This actin dimer acts as an actin nucleating factor (ANF), decreasing the half-time for spontaneous actin polymerization. ANF re
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9e0b1000aefb47f94c06e195ad3479d6
https://doi.org/10.1021/bi9914964
https://doi.org/10.1021/bi9914964
Autor:
Lynn A. Selden, Bryan Lincoln, Henry J. Kinosian, Lewis C. Gershman, Jay Newman, James E. Estes, Hurwitz C
Publikováno v:
Biophysical Journal. 75(6):3092-3100
Gelsolin is a Ca2+-regulated actin-binding protein that can sever, cap, and nucleate growth from the pointed ends of actin filaments. In this study we have measured the binding of the amino-terminal half of gelsolin, G1–3, to pyrene-labeled F-actin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5305de1622d92146ea88a454dcea9de3
Autor:
Henry J. Kinosian, Jay Newman, Lewis C. Gershman, Lynn A. Selden, James E. Estes, Bryan Lincoln
Publikováno v:
Biophysical Journal. 75:3101-3109
Regulation of the F-actin severing activity of gelsolin by Ca2+ has been investigated under physiologic ionic conditions. Tryptophan fluorescence intensity measurements indicate that gelsolin contains at least two Ca2+ binding sites with affinities o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::de3b825d117fc7efe4942711b66cade5
https://doi.org/10.1016/s0006-3495(98)77751-3
https://doi.org/10.1016/s0006-3495(98)77751-3
Publikováno v:
Journal of Biological Chemistry. 268:8683-8691
We have reinvestigated nucleotide binding to actin in order to resolve conflicts regarding the mechanism of nucleotide dissociation and exchange. We present evidence that supports a mechanism for nucleotide binding to actin in which the tightly bound
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6f19adc9ecd3834dd539b9b2d3872cc2
https://doi.org/10.1016/s0021-9258(18)52929-x
https://doi.org/10.1016/s0021-9258(18)52929-x
Publikováno v:
Journal of Muscle Research and Cell Motility. 13:272-284
Actin is known to undergo reversible monomer-polymer transitions that coincide with various cell activities such as cell shape changes, locomotion, endocytosis and exocytosis. This dynamic state of actin filament self-assembly and disassembly is thou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c824be425d3f4ec84b7e32e0ffa50b1
https://doi.org/10.1007/bf01766455
https://doi.org/10.1007/bf01766455
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1077:151-158
Previous work by this laboratory has shown that the tightly bound divalent cation of actin affects the enthalpy of the polymerization reaction for ATP-actin (Selden et al. (1986) J. Muscle Res. Cell Motil. 7, 215-224). In the present study, we have m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ec742da8d6d6e050b3fc3963bc71998
https://doi.org/10.1016/0167-4838(91)90052-2
https://doi.org/10.1016/0167-4838(91)90052-2
Publikováno v:
Journal of Biological Chemistry. 266:76-82
Each actin molecule has one high affinity site which binds a divalent cation. It has been proposed that an isomerization of the actin molecule is involved in divalent cation exchange at this site ("isomerization model," Frieden, C. (1982) J. Biol. Ch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5154fe3dfad69d64dcbaf9ba5c822c19
https://doi.org/10.1016/s0021-9258(18)52404-2
https://doi.org/10.1016/s0021-9258(18)52404-2
Publikováno v:
Biochemistry. 43(20)
Using vertebrate cytoplasmic actin consisting of a mixture of beta and gamma isoforms, we previously characterized profilin and nucleotide binding to monomeric actin (Kinosian, H. J., et al. (2000) Biochemistry 39, 13176-13188) and F-actin barbed end
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f203607107a24389d7cfa27682d7c5f5
https://pubmed.ncbi.nlm.nih.gov/15147209
https://pubmed.ncbi.nlm.nih.gov/15147209