Zobrazeno 1 - 10
of 106
pro vyhledávání: '"Elisha Haas"'
Autor:
Joseph D. Racca, Deepak Chatterjee, Yen-Shan Chen, Ratan K. Rai, Yanwu Yang, Millie M. Georgiadis, Elisha Haas, Michael A. Weiss
Publikováno v:
Frontiers in Endocrinology, Vol 13 (2022)
Y-encoded transcription factor SRY initiates male differentiation in therian mammals. This factor contains a high-mobility-group (HMG) box, which mediates sequence-specific DNA binding with sharp DNA bending. A companion article in this issue describ
Externí odkaz:
https://doaj.org/article/b100fc8439af4539b9f3a1c25f9920c3
Publikováno v:
PLoS ONE, Vol 10, Iss 12, p e0143732 (2015)
Most active biopolymers are dynamic structures; thus, ensembles of such molecules should be characterized by distributions of intra- or intermolecular distances and their fast fluctuations. A method of choice to determine intramolecular distances is
Externí odkaz:
https://doaj.org/article/15e5c1440ba64002820e70bb4b8966b0
Male sex determination in mammals is initiated by SRY, a Y-encoded architectural transcription factor. The protein contains a high-mobility-group (HMG) box that mediates sequence-specific DNA bending. Mutations in SRY causing XY gonadal dysgenesis (S
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3bea60502a4cb4d1704ad1beff80b5e1
https://doi.org/10.1101/2021.05.05.442830
https://doi.org/10.1101/2021.05.05.442830
Publikováno v:
Biophysical Journal. 121:187a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4354d5dd63cddd5efd73b3fd2766bcb2
https://doi.org/10.1016/j.bpj.2021.11.1814
https://doi.org/10.1016/j.bpj.2021.11.1814
Publikováno v:
Biophysical Journal. 112:1786-1796
The investigation of the mechanism of protein folding is complicated by the context dependence of the rates of intramolecular contact formation. Methods based on site-specific labeling and ultrafast spectroscopic detection of fluorescence signals wer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e420ad5cd74c1bb48712ca30b77bdb9
https://doi.org/10.1016/j.bpj.2017.01.037
https://doi.org/10.1016/j.bpj.2017.01.037
Publikováno v:
The journal of physical chemistry. B. 123(21)
This Feature Article presents a view of the protein folding transition based on the hypothesis that Nature has built features within the sequences that enable a Shortcut to efficient folding. Nature's Shortcut is proposed to be the early establishmen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d760a5112d96ac964e616002305d775
https://pubmed.ncbi.nlm.nih.gov/30901220
https://pubmed.ncbi.nlm.nih.gov/30901220
Publikováno v:
Biophysical Journal. 118:216a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5d29ff497cb1d04280f1b4d82ba0efe9
https://doi.org/10.1016/j.bpj.2019.11.1287
https://doi.org/10.1016/j.bpj.2019.11.1287
Publikováno v:
ChemPhysChem
In the absence of a stable fold, transient secondary structure kinetics define the native state of the prototypical and pharmacologically relevant intrinsically disordered protein (IDP) α-Synuclein (aS). Here, we investigate kinetics preventing orde
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4ad5b1e25ecefdde50b9cae049d581d
https://hdl.handle.net/21.11116/0000-0001-DB29-B21.11116/0000-0002-5133-921.11116/0000-0002-5134-8
https://hdl.handle.net/21.11116/0000-0001-DB29-B21.11116/0000-0002-5133-921.11116/0000-0002-5134-8
Autor:
Fang Huang, Werner M. Nau, Roy N. Dsouza, Thomas Schwarzlose, Elisha Haas, Xiaojuan Wang, Maik H. Jacob
Publikováno v:
The journal of physical chemistry. B. 122(16)
Protein folding can be described as a probabilistic succession of events in which the peptide chain forms loops closed by specific amino acid residue contacts, herein referred to as loop nodes. To measure loop rates, several photophysical methods hav
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af138e95b1b180125bdc327124ae9619
https://pubmed.ncbi.nlm.nih.gov/29617564
https://pubmed.ncbi.nlm.nih.gov/29617564
Publikováno v:
Bio-Algorithms and Med-Systems. 10:169-193
The protein folding problem would be considered “solved” when it will be possible to “read genes”, i.e., to predict the native fold of proteins, their dynamics, and the mechanism of fast folding based solely on sequence data. The long-term go
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::70d7cbf6ba8272e5bdfa423ca60a9b52
https://doi.org/10.1515/bams-2014-0018
https://doi.org/10.1515/bams-2014-0018