Heimdallarchaea encodes profilin with eukaryotic-like actin regulation and polyproline binding.

Autor: Survery S; Department of Molecular Bioscience, The Wenner-Gren Institute, Stockholm University, Stockholm, Sweden. sabeen.survery@su.se., Hurtig F; Department of Molecular Bioscience, The Wenner-Gren Institute, Stockholm University, Stockholm, Sweden., Haq SR; Department of Molecular Bioscience, The Wenner-Gren Institute, Stockholm University, Stockholm, Sweden., Eriksson J; Department of Medical Biochemistry and Microbiology, Uppsala University, Uppsala, Sweden., Guy L; Department of Medical Biochemistry and Microbiology, Uppsala University, Uppsala, Sweden., Rosengren KJ; School of Biomedical Sciences, The University of Queensland, Brisbane, QLD, Australia., Lindås AC; Department of Molecular Bioscience, The Wenner-Gren Institute, Stockholm University, Stockholm, Sweden., Chi CN; Department of Medical Biochemistry and Microbiology, Uppsala University, Uppsala, Sweden. chi.celestine@imbim.uu.se.

Publikováno v: Communications biology [Commun Biol] 2021 Sep 01; Vol. 4 (1), pp. 1024. Date of Electronic Publication: 2021 Sep 01.

Evaluating the low-rank coal degradation efficiency bioaugmented with activated sludge.

Autor: Kozhakhmetova, Marzhan¹ (AUTHOR) marzhanur.7@mail.ru, Akimbekov, Nuraly^1,2,3 (AUTHOR), Digel, Ilya⁴ (AUTHOR), Tastambek, Kuanysh^1,2,5 (AUTHOR)

Publikováno v: Scientific Reports. 6/27/2024, Vol. 14 Issue 1, p1-14. 14p.

The plastic energy landscape of protein folding: a triangular folding mechanism with an equilibrium intermediate for a small protein domain

Autor: Haq SR, Jürgens MC, Chi CN, Koh CS, Elfström L, Selmer M, Gianni S, Jemth P.

Publikováno v: The Journal of biological chemistry
(2010).
info:cnr-pdr/source/autori:Haq SR, Jürgens MC, Chi CN, Koh CS, Elfström L, Selmer M, Gianni S, Jemth P./titolo:The plastic energy landscape of protein folding: a triangular folding mechanism with an equilibrium intermediate for a small protein domain./doi:/rivista:The Journal of biological chemistry (Print)/anno:2010/pagina_da:/pagina_a:/intervallo_pagine:/volume

Protein domains usually fold without or with only transiently populated intermediates, possibly to avoid misfolding, which could result in amyloidogenic disease. Whether observed intermediates are productive and obligatory species on the folding reac

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=cnr_________::452114a9abdd90bf39062379c2c569e2
http://www.cnr.it/prodotto/i/11781

Energetic pathway sampling in a protein interaction domain.

Autor: Hultqvist G; Department of Medical Biochemistry and Microbiology, Uppsala University, BMC Box 582, SE-75123 Uppsala, Sweden., Haq SR, Punekar AS, Chi CN, Engström Å, Bach A, Strømgaard K, Selmer M, Gianni S, Jemth P

Publikováno v: Structure (London, England : 1993) [Structure] 2013 Jul 02; Vol. 21 (7), pp. 1193-1202.

Interactions outside the boundaries of the canonical binding groove of a PDZ domain influence ligand binding.

Autor: Chi CN; Department of Medical Biochemistry and Microbiology, Uppsala University, SE-75123 Uppsala, Sweden., Haq SR, Rinaldo S, Dogan J, Cutruzzolà F, Engström Å, Gianni S, Lundström P, Jemth P

Publikováno v: Biochemistry [Biochemistry] 2012 Nov 06; Vol. 51 (44), pp. 8971-9. Date of Electronic Publication: 2012 Oct 23.