Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Mario J, Avellaneda"'
Autor:
Sander J. Tans, Kamila B. Franke, Mario J. Avellaneda, Vanda Sunderlikova, Axel Mogk, Bernd Bukau
Publikováno v:
Nature. 578:317-320
The ability to reverse protein aggregation is vital to cells1,2. Hsp100 disaggregases such as ClpB and Hsp104 are proposed to catalyse this reaction by translocating polypeptide loops through their central pore3,4. This model of disaggregation is app
Publikováno v:
Communications Chemistry, 3(1)
Communications Chemistry, Vol 3, Iss 1, Pp 1-7 (2020)
Communications Chemistry, Vol 3, Iss 1, Pp 1-7 (2020)
Funder: Nederlandse Organisatie voor Wetenschappelijk Onderzoek (Netherlands Organisation for Scientific Research); doi: https://doi.org/10.13039/501100003246
Many proteins form dynamic complexes with DNA, RNA, and other proteins, which often in
Many proteins form dynamic complexes with DNA, RNA, and other proteins, which often in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0ce382c2516d4756f79b3a03dbec1ff6
Autor:
Yuval Mulla, Mario J Avellaneda, Antoine Roland, Lucia Baldauf, Wonyeong Jung, Taeyoon Kim, Sander J Tans, Gijsje H Koenderink
Molecular catch bonds are ubiquitous in biology and well-studied in the context of leukocyte extravasion1, cellular mechanosensing2,3, and urinary tract infection4. Unlike normal (slip) bonds, catch bonds strengthen under tension. The current paradig
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::da93613b9b4ef17fbaa4b1f629978869
https://doi.org/10.1101/2020.07.27.219618
https://doi.org/10.1101/2020.07.27.219618
Autor:
Vanda Sunderlikova, Andrew Roth, Sander J. Tans, Mario J. Avellaneda, Mohsin M. Naqvi, Eline J. Koers, Hays S. Rye, Guenter Kramer
Unfolded proteins ubiquitously collapse into a compact yet dynamic state1,2. While this compaction is pivotal to protein folding3, aggregation4,5, intrinsic disorder6, and phase separation7, its role in protein quality control mechanisms remains obsc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::674ac0bbcf09312e36124ce52c42896c
https://doi.org/10.1101/2020.06.17.157057
https://doi.org/10.1101/2020.06.17.157057
Publikováno v:
Protein Science. 26:1291-1302
Protein folding is well known to be supervised by a dedicated class of proteins called chaperones. However, the core mode of action of these molecular machines has remained elusive due to several reasons including the promiscuous nature of the intera
Autor:
Mario J, Avellaneda, Kamila B, Franke, Vanda, Sunderlikova, Bernd, Bukau, Axel, Mogk, Sander J, Tans
Publikováno v:
Nature. 578(7794)
The ability to reverse protein aggregation is vital to cells
Autor:
Kamila B. Franke, Axel Mogk, Vanda Sunderlikova, Mario J. Avellaneda, Sander J. Tans, Bernd Bukau
Publikováno v:
Nature. 578:E23-E23
Autor:
Günter Kramer, Alireza Mashaghi, Florian Wruck, David P. Minde, Eline J. Koers, Mario J. Avellaneda, Matthias P. Mayer, Sander J. Tans
Publikováno v:
Journal of Molecular Biology
Chaperones assist in protein folding, but what this common phrase means in concrete terms has remained surprisingly poorly understood. We can readily measure chaperone binding to unfolded proteins, but how they bind and affect proteins along folding
Publikováno v:
Protein science : a publication of the Protein Society. 26(7)
Protein folding is well known to be supervised by a dedicated class of proteins called chaperones. However, the core mode of action of these molecular machines has remained elusive due to several reasons including the promiscuous nature of the intera
Autor:
Juan Jose Miret, Slobodan Vuković, Carlos J. Zapata-Rodríguez, Pablo Cencillo, Mario J. Avellaneda, David Pastor
Publikováno v:
SPIE Proceedings.
Recent disclosures on subwavelength plasmonic crystals, like the potential excitation of a pair of coexisting wave-fields with opposite refraction, only can be understood by considering two dispersion branches with completely different features that