Zobrazeno 1 - 10
of 137
pro vyhledávání: '"James C.A. Bardwell"'
Publikováno v:
Annual Review of Biophysics. 51:409-429
The folding of proteins into their native structure is crucial for the functioning of all biological processes. Molecular chaperones are guardians of the proteome that assist in protein folding and prevent the accumulation of aberrant protein conform
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af68e0965a8edbaceb0d3bfd19b69e4c
https://doi.org/10.1146/annurev-biophys-090121-082906
https://doi.org/10.1146/annurev-biophys-090121-082906
Autor:
James C.A. Bardwell
Publikováno v:
Cell. 185(25)
Chaperones are important for protein folding, but visualizing this process has proven to be exceptionally difficult. In this issue of Cell, Frydman and colleagues have succeeded in watching tubulin being folded by its chaperonin TRiC at near-atomic r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b41a90e5845cf5a3529f5be09f418bd
https://pubmed.ncbi.nlm.nih.gov/36493750
https://pubmed.ncbi.nlm.nih.gov/36493750
Autor:
Vishakha Choudhary, Kevin Wu, Zhiyao Zhang, Mark Dulchavsky, Todd Barkman, James C.A. Bardwell, Frederick Stull
Publikováno v:
The Journal of biological chemistry. 298(8)
The soil-dwelling bacterium Pseudomonas putida S16 can survive on nicotine as its sole carbon and nitrogen source. The enzymes nicotine oxidoreductase (NicA2) and pseudooxynicotine amine oxidase (Pnao), both members of the flavin-containing amine oxi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f695c158be329df4ee5cde23c6b6887
https://pubmed.ncbi.nlm.nih.gov/35835223
https://pubmed.ncbi.nlm.nih.gov/35835223
Publikováno v:
Proceedings of the National Academy of Sciences. 116:23040-23049
The assembly of small disordered proteins into highly ordered amyloid fibrils in Alzheimer’s and Parkinson’s patients is closely associated with dementia and neurodegeneration. Understanding the process of amyloid formation is thus crucial in the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::005700fe77f4427cb3f1a22d8307a3b2
https://doi.org/10.1073/pnas.1913316116
https://doi.org/10.1073/pnas.1913316116
Publikováno v:
Mol Microbiol
OsmY is a widely conserved but poorly understood 20 kDa periplasmic protein. Using a folding biosensor, we previously obtained evidence that OsmY has molecular chaperone activity. To discover natural OsmY substrates, we screened for proteins that are
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9fe44cc56097521c57c751bfe6432447
https://doi.org/10.1111/mmi.14358
https://doi.org/10.1111/mmi.14358
Publikováno v:
BioTechniques, Vol 28, Iss 3, Pp 426-432 (2000)
Externí odkaz:
https://doaj.org/article/f61a15cff6af4e7082fb303b2a9bcb30
Autor:
Ben A. Meinen, Varun V. Gadkari, Rishav Mitra, Brandon T. Ruotolo, Carlo P. M. van Mierlo, James C.A. Bardwell
Publikováno v:
Nature Communications, 12(1)
Nature Communications
Nature Communications 12 (2021) 1
Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
Nature Communications
Nature Communications 12 (2021) 1
Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
ATP-independent chaperones are usually considered to be holdases that rapidly bind to non-native states of substrate proteins and prevent their aggregation. These chaperones are thought to release their substrate proteins prior to their folding. Spy
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce05126cac073c908f08276a5a1f68c7
https://research.wur.nl/en/publications/mechanism-of-the-small-atp-independent-chaperone-spy-is-substrate
https://research.wur.nl/en/publications/mechanism-of-the-small-atp-independent-chaperone-spy-is-substrate
Autor:
Kevin Wu, Changhan Lee, James C.A. Bardwell, Dawid S. Żyła, Rudi Glockshuber, Patrick Betschinger
Publikováno v:
The EMBO Journal, 39 (20)
EMBO J
EMBO J
Bile salts are secreted into the gastrointestinal tract to aid in the absorption of lipids. In addition, bile salts show potent antimicrobial activity in part by mediating bacterial protein unfolding and aggregation. Here, using a protein folding sen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4182869915a84e47a164559fec661637
https://hdl.handle.net/20.500.11850/451440
https://hdl.handle.net/20.500.11850/451440
Publikováno v:
J Biol Chem
Chaperones are essential components of the protein homeostasis network. There is a growing interest in optimizing chaperone function, but exactly how to achieve this aim is unclear. Here, using a model chaperone, the bacterial protein Spy, we demonst
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5814b0118b3b0d3956391d030211b346
https://europepmc.org/articles/PMC7573262/
https://europepmc.org/articles/PMC7573262/
Publikováno v:
Nature chemical biology
Nicotine oxidoreductase (NicA2), a member of the flavin-containing amine oxidase family, is of medical relevance as it shows potential as a therapeutic to aid cessation of smoking due to its ability to oxidize nicotine into a non-psychoactive metabol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f0754edee0faff87c941a3cbf35faee8
https://pubmed.ncbi.nlm.nih.gov/33542535
https://pubmed.ncbi.nlm.nih.gov/33542535