Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Amanda L. Jonsson"'
Publikováno v:
Protein Eng Des Sel
The Dynameomics project contains native state and unfolding simulations of 807 protein domains, where each domain is representative of a different metafold; these metafolds encompass ~97% of protein fold space. There is a long-standing question in st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09f6dbfd7efca4565c7feaf726c5a276
https://doi.org/10.1093/protein/gzz040
https://doi.org/10.1093/protein/gzz040
Publikováno v:
Essays in Biochemistry
Within every living organism, countless reactions occur every second. These reactions typically occur more rapidly and with greater efficiency than would be possible under the same conditions in the chemical laboratory, and while using only the subse
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5f6b035faf5532f56c0adfc30c547351
https://doi.org/10.1042/ebc20160094
https://doi.org/10.1042/ebc20160094
Publikováno v:
The FASEB Journal. 33
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c1cb0087385513e1ae507bd659f72b43
https://doi.org/10.1096/fasebj.2019.33.1_supplement.462.3
https://doi.org/10.1096/fasebj.2019.33.1_supplement.462.3
Publikováno v:
The FASEB Journal. 32
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8d5abe99063c78585d62f8657a1ae319
https://doi.org/10.1096/fasebj.2018.32.1_supplement.526.37
https://doi.org/10.1096/fasebj.2018.32.1_supplement.526.37
Publikováno v:
Journal of the American Chemical Society. 135:8749-8759
G-protein-coupled receptors (GPCRs) are membrane proteins with critical functions in cellular signal transduction, representing a primary class of drug targets. Acting by direct binding, many drugs modulate GPCR activity and influence the signaling p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f887f44ef0d1e46509c87a628a5f43f
https://doi.org/10.1021/ja404391q
https://doi.org/10.1021/ja404391q
Publikováno v:
Biomolecular Concepts, Vol 1, Iss 5-6, Pp 335-344 (2010)
All currently known structures of proteins together define ‘protein fold space’. To increase the general understanding of protein dynamics and protein folding, we selected a set of 807 proteins and protein domains that represent 95% of the curren
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77a5988dcfc6729c3374663505e36bf1
https://doi.org/10.1515/bmc.2010.032
https://doi.org/10.1515/bmc.2010.032
Publikováno v:
Bioinformatics. 27:46-54
Motivation: The discovery of new protein folds is a relatively rare occurrence even as the rate of protein structure determination increases. This rarity reinforces the concept of folds as reusable units of structure and function shared by diverse pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac22f7258171367dbb36d1982e334433
https://doi.org/10.1093/bioinformatics/btq625
https://doi.org/10.1093/bioinformatics/btq625
Publikováno v:
Protein Science. 16:2233-2239
The folding of WW domains is rate limited by formation of a beta-hairpin comprising residues from strands 1 and 2. Residues in the turn of this hairpin have reported Phi-values for folding close to 1 and have been proposed to nucleate folding. High P
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20d385d8d3f9f894d05d92d1802f8a08
https://doi.org/10.1110/ps.073004907
https://doi.org/10.1110/ps.073004907
Publikováno v:
Journal of Molecular Biology. 360:865-881
The 37-residue Formin-binding protein, FBP28, is a canonical three-stranded beta-sheet WW domain. Because of its small size, it is so insensitive to chemical denaturation that it is barely possible to determine accurately a denaturation curve, as the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca6040a977950e5705926c3014d6f4d2
https://doi.org/10.1016/j.jmb.2006.05.050
https://doi.org/10.1016/j.jmb.2006.05.050
Publikováno v:
Protein engineering, designselection : PEDS. 26(8)
There are over 100 mutations in Cu/Zn superoxide dismutase (SOD1) that result in a subset of familial amyotrophic lateral sclerosis (fALS) cases. The hypothesis that dissociation of the dimer, misfolding of the monomer and subsequent aggregation of m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7ad37792a87c0a4575e8e300be03fe28
https://pubmed.ncbi.nlm.nih.gov/23784844
https://pubmed.ncbi.nlm.nih.gov/23784844