Zobrazeno 1 - 10
of 52
pro vyhledávání: '"T D, Pollard"'
Publikováno v:
Annual Review of Physiology. 53:653-682
Autor:
T D, Pollard
Publikováno v:
Nature reviews. Molecular cell biology. 2(12)
Many biologists are active in politics in the United States. Their efforts combined with those of other advocates, such as patient groups and members of Congress, have made funding of biomedical research a priority for both of the main political part
Publikováno v:
Journal of molecular biology. 312(4)
We investigated the effect of actin filament length and capping protein on the rate of end-to-end annealing of actin filaments. Long filaments were fragmented by shearing and allowed to recover. Stabilizing filaments with phalloidin in most experimen
Publikováno v:
Journal of molecular biology. 295(3)
Two factors have limited studies of the properties of nucleotide-free actin (NFA). First, actin lacking bound nucleotide denatures rapidly without stabilizing agents such as sucrose; and second, without denaturants such as urea, it is difficult to re
Publikováno v:
The Journal of biological chemistry. 274(49)
The Acanthamoeba myosin-IA heavy chain gene encodes a 134-kDa protein with a catalytic domain, three potential light chain binding sites, and a tail with separately folded tail homology (TH) -1, -2, and -3 domains. TH-1 is highly resistant to trypsin
Publikováno v:
Biochemistry. 38(46)
The 70 C-terminal amino acids of Wiskott-Aldrich syndrome protein (WASp WA) activate the actin nucleation activity of the Arp2/3 complex. WASp WA binds both the Arp2/3 complex and actin monomers, but the mechanism by which it activates the Arp2/3 com
Publikováno v:
Methods in enzymology. 298
Autor:
D A, Kaiser, T D, Pollard
Publikováno v:
Journal of molecular biology. 256(1)
We characterized several deletion and substitution mutations of Acanthamoeba profilin and nine monoclonal antibodies to Acanthamoeba profilin. The results provide two independent lines of evidence about the binding sites for actin and poly-L-proline
Publikováno v:
Cancer research. 54(14)
The adenomatous polyposis coli protein (APC) is mutated in familial adenomatous polyposis patients as well as in sporadic colorectal tumors. In an attempt to further understand the function of APC, the subcellular localization of APC was examined. Wi
Autor:
T D, Pollard, S, Quirk
Publikováno v:
Society of General Physiologists series. 49