Výsledky vyhledávání - "A. Galińska-Rakoczy"

Mechanism of actin polymerization by myosin subfragment-1 probed by dynamic light scattering

Autor: Barbara Jachimska, H. Strzelecka-Gołaszewska, A. Galińska-Rakoczy

Publikováno v: Bioelectrochemistry. 70:53-57

Monomeric actin (G-actin) polymerizes spontaneously into helical filaments in the presence of inorganic salts. The slowest, rate-limiting step of the polymerization process is formation of actin trimers, the smallest oligomers that serve as nuclei fo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76bf02673e78ce4968f4c5b4d1f92368
https://doi.org/10.1016/j.bioelechem.2006.03.035

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Role of Actin DNase-I-Binding Loop in Myosin Subfragment 1-Induced Polymerization of G-actin: Implications for the Mechanism of Polymerization

Autor: Hanna Strzelecka-Gołaszewska, Agnieszka Galińska-Rakoczy, Barbara Wawro, Sofia Khaitlina

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

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New aspects of the spontaneous polymerization of actin in the presence of salts

Autor: Barbara Wawro, Hanna Strzelecka-Gołaszewska, Agnieszka Galińska-Rakoczy

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

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Conformational indeterminism in protein misfolding: chiral amplification on amyloidogenic pathway of insulin

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

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