Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Annika Scior"'
Autor:
Barbara Mlody, Josef Priller, Manuel Iburg, Janine Kirstein, Alexander Buntru, Maria Lucia Pigazzini, Katrin Juenemann, Anne Ast, Alessandro Prigione, Erich E. Wanker, Annika Scior, Kristin Arnsburg, Dmytro Puchkov
Publikováno v:
EMBO J
Huntington9s disease (HD) is a neurodegenerative disorder caused by an expanded CAG trinucleotide repeat in the huntingtin gene ( HTT ). Molecular chaperones have been implicated in suppressing or delaying the aggregation of mutant Htt. Using in vitr
Publikováno v:
Essays in biochemistry. 60(2):153-161
Nature has evolved several mechanisms to detoxify intracellular protein aggregates that arise upon proteotoxic challenges. These include the controlled deposition of misfolded proteins at distinct cellular sites, the protein disaggregation and refold
Autor:
Steffen Preissler, Julia Reuther, Miriam Koch, Annika Scior, Elke Deuerling, Michael Bruderek, Tancred Frickey
Publikováno v:
The EMBO Journal. 34:1905-1924
Translation of aberrant or problematic mRNAs can cause ribosome stalling which leads to the production of truncated or defective proteins. Therefore, cells evolved cotranslational quality control mechanisms that eliminate these transcripts and target
Autor:
Bernd Bukau, Richard I. Morimoto, Kristin Arnsburg, Anna Szlachcic, Annika Scior, D. Lys Guilbride, Nadinath B. Nillegoda, Janine Kirstein
Publikováno v:
Aging cell, Early View
Aging Cell
Aging Cell
Summary Protein aggregation is enhanced upon exposure to various stress conditions and aging, which suggests that the quality control machinery regulating protein homeostasis could exhibit varied capacities in different stages of organismal lifespan.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8cbbe21911b52952315bacbdaf6db4dc
Wiley Online Library
Wiley Online Library
Publikováno v:
The EMBO Journal. 32:1451-1468
The adaptation of protein synthesis to environmental and physiological challenges is essential for cell viability. Here, we show that translation is tightly linked to the protein folding environment of the cell through the functional properties of th
Autor:
Xuechao Gao, Matthias P. Mayer, Janine Kirstein, Bernd Bukau, Kristin Arnsburg, Florian Stengel, Antonia Stank, Ruedi Aebersold, Mykhaylo Berynskyy, Annika Scior, Rebecca C. Wade, Anna Szlachcic, D. Lys Guilbride, Nadinath B. Nillegoda, Richard I. Morimoto
Publikováno v:
Nature, 524(7564):247–251
Protein aggregates are the hallmark of stressed and ageing cells, and characterize several pathophysiological states1, 2. Healthy metazoan cells effectively eliminate intracellular protein aggregates3, 4, indicating that efficient disaggregation and/
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c357cad2dfa2b8ad02a0f055a6753fc8
Autor:
Elke Deuerling, Annika Scior
Publikováno v:
The Molecular Chaperones Interaction Networks in Protein Folding and Degradation ISBN: 9781493911295
Cells coordinate chaperones at the exit site of the ribosome. Albeit the types and mechanisms of ribosome-associated chaperones differ in the three kingdoms of life, they all share the ability to protect nascent polypeptides from off pathways such as
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4e2103746b0cdb29a583efbfcc4f9762
https://doi.org/10.1007/978-1-4939-1130-1_2
https://doi.org/10.1007/978-1-4939-1130-1_2
Autor:
Steffen Preissler, Marc Erhardt, Annika Scior, Yulia Ilina, Ansgar Koplin, Elke Deuerling, Miriam Koch
Publikováno v:
The Journal of Cell Biology
In addition to assisting with protein folding, SSB and NAC also regulate ribosome biogenesis (see also companion paper from Albanèse et al. in this issue).
The yeast Hsp70/40 system SSB–RAC (stress 70 B–ribosome-associated complex) binds to
The yeast Hsp70/40 system SSB–RAC (stress 70 B–ribosome-associated complex) binds to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41cd4245d2a586a947612eff629c6147
Autor:
Bernd Bukau, Annika Scior, Steffen Preissler, Ansgar Koplin, Janina Horst, Elke Deuerling, Jocelyne Fiaux
Yeast Zuotin and Ssz are members of the conserved Hsp40 and Hsp70 chaperone families, respectively, but compared with canonical homologs, they atypically form a stable heterodimer termed ribosome-associated complex (RAC). RAC acts as co-chaperone for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1bd357ef97fa47638d677d1502a83ee9
https://europepmc.org/articles/PMC2823442/
https://europepmc.org/articles/PMC2823442/
Publikováno v:
BMC Biotechnology
BMC Biotechnology, Vol 11, Iss 1, p 87 (2011)
BMC Biotechnology, Vol 11, Iss 1, p 87 (2011)
Background Highly repetitive nucleotide sequences are commonly found in nature e.g. in telomeres, microsatellite DNA, polyadenine (poly(A)) tails of eukaryotic messenger RNA as well as in several inherited human disorders linked to trinucleotide repe