Zobrazeno 1 - 10
of 16
pro vyhledávání: '"David Balchin"'
Autor:
Anna Maria Eisele-Bürger, Frederik Eisele, Sandra Malmgren Hill, Xinxin Hao, Kara L. Schneider, Rahmi Imamoglu, David Balchin, Beidong Liu, F. Ulrich Hartl, Peter V. Bozhkov, Thomas Nyström
Publikováno v:
Cell Reports, Vol 42, Iss 11, Pp 113372- (2023)
Summary: Metacaspases are ancestral homologs of caspases that can either promote cell death or confer cytoprotection. Furthermore, yeast (Saccharomyces cerevisiae) metacaspase Mca1 possesses dual biochemical activity: proteolytic activity causing cel
Externí odkaz:
https://doaj.org/article/9af3080157bc43d7b143e62b2b0ce9aa
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
The Hsp70 system prevents protein aggregation and increases folding yields, but it is unknown whether it also enhances the rate of folding. Here the authors combine refolding assays, FRET and hydrogen/deuterium exchange-mass spectrometry measurements
Externí odkaz:
https://doaj.org/article/6125957e2a10438cac86795beb9c3d88
Autor:
Anna anon, Frederik Eisele, Sandra M. Hill, Xinxin Hao, Kara L. Schneider, Rahmi Imamoglu, David Balchin, Beidong Liu, Franz-Ulrich Hartl, Peter Bozhkov, Thomas Nyström
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7cfa6e7c80811039b880f081250c022d
https://doi.org/10.2139/ssrn.4408793
https://doi.org/10.2139/ssrn.4408793
Autor:
Thomas E. Wales, Aleksandra Pajak, Alžběta Roeselová, Santosh Shivakumaraswamy, Steven Howell, F. Ulrich Hartl, John R. Engen, David Balchin
The cellular environment is critical for efficient protein maturation, but how proteins fold during biogenesis remains poorly understood. We used hydrogen/deuterium exchange (HDX) mass spectrometry (MS) to define, at peptide resolution, the cotransla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::33c19d7da51045713204ed5d76c4b002
https://doi.org/10.1101/2022.09.23.509153
https://doi.org/10.1101/2022.09.23.509153
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
Nature Communications
NATURE COMMUNICATIONS
Nature Communications
NATURE COMMUNICATIONS
The ATP-dependent Hsp70 chaperones (DnaK in E. coli) mediate protein folding in cooperation with J proteins and nucleotide exchange factors (E. coli DnaJ and GrpE, respectively). The Hsp70 system prevents protein aggregation and increases folding yie
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d50306326c7c258494a2c5b5da90c803
http://link.springer.com/article/10.1038/s41467-019-14245-4
http://link.springer.com/article/10.1038/s41467-019-14245-4
Publikováno v:
FEBS Letters
Molecular chaperones are highly conserved proteins that promote proper folding of other proteins in vivo. Diverse chaperone systems assist de novo protein folding and trafficking, the assembly of oligomeric complexes, and recovery from stress-induced
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::927c9bb47369f31efc7387db54934814
https://pubmed.ncbi.nlm.nih.gov/32446288
https://pubmed.ncbi.nlm.nih.gov/32446288
Publikováno v:
Journal of molecular biology. 432(7)
The cylindrical chaperonin GroEL and its cofactor GroES mediate ATP-dependent protein folding in Escherichia coli by transiently encapsulating non-native substrate in a nano-cage formed by the GroEL ring cavity and the lid-shaped GroES. Mechanistic s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::33599d6447269f51da953f4021cf7491
https://pubmed.ncbi.nlm.nih.gov/32135190
https://pubmed.ncbi.nlm.nih.gov/32135190
Autor:
F. Ulrich Hartl, David Balchin, Courtney L. Klaips, Andreas Bracher, Leonie Mönkemeyer, Roman Körner
Publikováno v:
Molecular cell. 74(1)
Summary Eukaryotic elongation factor 2 (eEF2) is an abundant and essential component of the translation machinery. The biogenesis of this 93 kDa multi-domain protein is assisted by the chaperonin TRiC/CCT. Here, we show in yeast cells that the highly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40bf4ae236bc77b20ac9434f6b2c0cc3
https://pubmed.ncbi.nlm.nih.gov/30876804
https://pubmed.ncbi.nlm.nih.gov/30876804
Publikováno v:
Cell. 174(6)
The hetero-oligomeric chaperonin of eukarya, TRiC, is required to fold the cytoskeletal protein actin. The simpler bacterial chaperonin system, GroEL/GroES, is unable to mediate actin folding. Here, we use spectroscopic and structural techniques to d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77a82c23236af7ebba94b6970ee29a80
https://pubmed.ncbi.nlm.nih.gov/30100183
https://pubmed.ncbi.nlm.nih.gov/30100183
Autor:
Christos Gatsogiannis, Anne Kuhlee, Daniel Roderer, Manajit Hayer-Hartl, Stefan Raunser, Evelyn Schubert, David Balchin, Felipe Merino
Publikováno v:
Nature. 563(7730)
Tc toxins secrete toxic enzymes into host cells using a unique syringe-like injection mechanism. They are composed of three subunits, TcA, TcB and TcC. TcA forms the translocation channel and the TcB-TcC heterodimer functions as a cocoon that shields
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c47523b44a9ff7136110cc1a7b56a5c5
https://pubmed.ncbi.nlm.nih.gov/30232455
https://pubmed.ncbi.nlm.nih.gov/30232455