Zobrazeno 1 - 10
of 37
pro vyhledávání: '"Jakob Dogan"'
Publikováno v:
Communications Biology, Vol 5, Iss 1, Pp 1-11 (2022)
Reconstruction of an ancient nuclear coactivator binding domain (NCBD) of CREB-binding protein from a bilaterian animal ancestor living 600 million years ago reveals conserved dynamic properties in human NCBD.
Externí odkaz:
https://doaj.org/article/b3678dcf1c654474a6663ba47b10204e
Autor:
Greta Hultqvist, Emma Åberg, Carlo Camilloni, Gustav N Sundell, Eva Andersson, Jakob Dogan, Celestine N Chi, Michele Vendruscolo, Per Jemth
Publikováno v:
eLife, Vol 6 (2017)
Protein-protein interactions involving intrinsically disordered proteins are important for cellular function and common in all organisms. However, it is not clear how such interactions emerge and evolve on a molecular level. We performed phylogenetic
Externí odkaz:
https://doaj.org/article/4ec0392854ce45d69e6b992fc968cade
Evolution of proteins is constrained by their structure and function. While there is a consensus that the plasticity of intrinsically disordered proteins relaxes the structural constraints on evolution there is a paucity of data on the molecular deta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::87922ed7967e434b8fab9c195ee6b0d3
https://doi.org/10.1101/2021.06.10.447870
https://doi.org/10.1101/2021.06.10.447870
Autor:
Jakob Dogan, Ida Nyqvist
Publikováno v:
Scientific Reports
Scientific Reports, Vol 9, Iss 1, Pp 1-9 (2019)
Scientific Reports, Vol 9, Iss 1, Pp 1-9 (2019)
The interaction between the C-terminal transactivation domain of HIF-1α (CTAD-HIF-1α) and the transcriptional adapter zinc binding 1 (TAZ1) domain of CREB binding protein participate in the initiation of gene transcription during hypoxia. Unbound C
Autor:
Ida Lindström, Jakob Dogan
Publikováno v:
ACS Chemical Biology. 13:1218-1227
Intrinsically disordered proteins (IDPs) are abundant in the eukaryotic proteome. However, little is known about the role of subnanosecond dynamics and the conformational entropy that it represents in protein-protein interactions involving IDPs. Usin
Autor:
Ida Lindström, Jakob Dogan
Publikováno v:
Biochemistry. 56:4145-4153
A significant fraction of the eukaryotic proteome consists of proteins that are either partially or completely disordered under native-like conditions. Intrinsically disordered proteins (IDPs) are common in protein-protein interactions and are involv
Publikováno v:
The journal of physical chemistry. B. 123(13)
The globular transcriptional adapter zinc binding 1 (TAZ1) domain of CREB binding protein participates in protein-protein interactions that are involved in transcriptional regulation. TAZ1 binds numerous targets, of which many are intrinsically disor
Autor:
Per, Jemth, Elin, Karlsson, Beat, Vögeli, Brenda, Guzovsky, Eva, Andersson, Greta, Hultqvist, Jakob, Dogan, Peter, Güntert, Roland, Riek, Celestine N, Chi
Publikováno v:
Science Advances
Structural snapshots characterize six hundred million years of evolution of intrinsically disordered proteins.
In every established species, protein-protein interactions have evolved such that they are fit for purpose. However, the molecular det
In every established species, protein-protein interactions have evolved such that they are fit for purpose. However, the molecular det
Publikováno v:
Scientific Reports
Scientific Reports, Vol 8, Iss 1, Pp 1-8 (2018)
Scientific Reports, Vol 8, Iss 1, Pp 1-8 (2018)
Intrinsically disordered proteins (IDPs) are common in eukaryotes. However, relatively few experimental studies have addressed the nature of the rate-limiting transition state for the coupled binding and folding reactions involving IDPs. By using sit
Publikováno v:
Biochemistry. 54:4741-4750
Intrinsically disordered proteins (IDPs) are abundant in the proteome and involved in key cellular functions. However, experimental data about the binding kinetics of IDPs as a function of different environmental conditions are scarce. We have perfor