Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Agnieszka Galińska-Rakoczy"'
Publikováno v:
Biophysical Journal. 88:2883-2896
Proteolytic cleavage of actin between Gly42 and Val43 within its DNase-I-binding loop (D-loop) abolishes the ability of Ca-G-actin to spontaneously polymerize in the presence of KCl. Here we show that such modified actin is assembled into filaments,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7af90d2eea2016378d860f1cb8d9778f
https://doi.org/10.1529/biophysj.104.049155
https://doi.org/10.1529/biophysj.104.049155
Publikováno v:
Journal of molecular biology. 387(4)
The mechanism of salt-induced actin polymerization involves the energetically unfavorable nucleation step, followed by filament elongation by the addition of monomers. The use of a bifunctional cross-linker, N,N'-(1,4-phenylene)dimaleimide, revealed
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9dd65184b3dd2664da1daa810117be94
https://pubmed.ncbi.nlm.nih.gov/19340945
https://pubmed.ncbi.nlm.nih.gov/19340945
Autor:
Leszek Rupnicki, Rumi Adachi, Agnieszka Galińska-Rakoczy, Yuji Goto, Anna Loksztejn, Wojciech Dzwolak
Publikováno v:
Journal of the American Chemical Society. 129(24)
Unlike folding, protein aggregation is a multipathway, kinetically controlled process yielding different conformations of fibrils. The dynamics and determinism/indeterminism boundaries of misfolded conformations remain obscure. Here we show that, upo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d94da1b75fce17b402fbce192160d68e
https://pubmed.ncbi.nlm.nih.gov/17518465
https://pubmed.ncbi.nlm.nih.gov/17518465