Zobrazeno 1 - 10
of 69
pro vyhledávání: '"Leo Spyracopoulos"'
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-15 (2018)
Abstract The ubiquitin proteasome system (UPS) signals for degradation of proteins through attachment of K48-linked polyubiquitin chains, or alterations in protein-protein recognition through attachment of K63-linked chains. Target proteins are ubiqu
Externí odkaz:
https://doaj.org/article/847413dcf7314bdbbe3d72508e66203f
Publikováno v:
Cell Reports, Vol 22, Iss 2, Pp 383-395 (2018)
Summary: Ring1-YY1-binding protein (RYBP) is a member of the non-canonical polycomb repressive complex 1 (PRC1), and like other PRC1 members, it is best described as a transcriptional regulator. However, several PRC1 members were recently shown to fu
Externí odkaz:
https://doaj.org/article/fb30547d2923417a8d14199a8aae6f6e
Publikováno v:
Molecules, Vol 23, Iss 11, p 2825 (2018)
Interleukin-8 (CXCL8), a potent neutrophil-activating chemokine, exerts its function by activating the CXCR1 receptor that belongs to class A G protein-coupled receptors (GPCRs). Receptor activation involves interactions between the CXCL8 N-terminal
Externí odkaz:
https://doaj.org/article/960a057752684c29940bb8e2111e5c5d
Publikováno v:
The Journal of Physical Chemistry B. 124:2984-2993
Protein turnover in cells is regulated by the ATP dependent activity of the Hsp90 chaperone. In concert with accessory proteins, ATP hydrolysis drives the obligate Hsp90 dimer through a cycle betwe...
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cbf91d7943b34979e832a96c8a0e7494
https://doi.org/10.1021/acs.jpcb.0c00626
https://doi.org/10.1021/acs.jpcb.0c00626
Publikováno v:
The Journal of Physical Chemistry B. 123:3665-3671
19F NMR spectroscopy is a powerful tool for the study of the structures, dynamics, and interactions of proteins bearing cysteine residues chemically modified with a trifluoroacetone group (CYF residue). 19F NMR relaxation rates for the fluoromethyl g
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::238c6ced5b8454638daf65149ef78db1
https://doi.org/10.1021/acs.jpcb.9b01741
https://doi.org/10.1021/acs.jpcb.9b01741
Autor:
Annemarie Wolmarans, Suad Rashid, Leo Spyracopoulos, Brian L. Lee, Paul LaPointe, Benjamin Wajda
Publikováno v:
Biochemistry. 58:1869-1877
Hsp90 is a crucial chaperone whose ATPase activity is fundamental for stabilizing and activating a diverse array of client proteins. Binding and hydrolysis of ATP by dimeric Hsp90 drive a conformational cycle characterized by fluctuations between a c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::faa905c77a90de18115482c670f0c10f
https://doi.org/10.1021/acs.biochem.9b00144
https://doi.org/10.1021/acs.biochem.9b00144
Publikováno v:
The journal of physical chemistry. B. 124(15)
Protein turnover in cells is regulated by the ATP dependent activity of the Hsp90 chaperone. In concert with accessory proteins, ATP hydrolysis drives the obligate Hsp90 dimer through a cycle between open and closed states that is critical for assist
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4a7e6398c8b597c15397b48acef0f0cb
https://pubmed.ncbi.nlm.nih.gov/32212608
https://pubmed.ncbi.nlm.nih.gov/32212608
Publikováno v:
The Journal of Physical Chemistry B. 123:776-786
Cullin-RING ubiquitin ligases are a diverse family of ubiquitin ligases that catalyze the synthesis of K48-linked polyubiquitin (polyUb) chains on a variety of substrates, ultimately leading to their degradation by the proteasome. The cullin-RING enz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7cf2258a3910cb6659da81937cfce531
https://doi.org/10.1021/acs.jpcb.8b10706
https://doi.org/10.1021/acs.jpcb.8b10706
Publikováno v:
Cell Reports, Vol 22, Iss 2, Pp 383-395 (2018)
Summary: Ring1-YY1-binding protein (RYBP) is a member of the non-canonical polycomb repressive complex 1 (PRC1), and like other PRC1 members, it is best described as a transcriptional regulator. However, several PRC1 members were recently shown to fu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::10492e75396b0e52135cf9cc152044b7
https://doi.org/10.1016/j.celrep.2017.12.047
https://doi.org/10.1016/j.celrep.2017.12.047
Publikováno v:
J Mol Biol
Cells are exposed to thousands of DNA damage events on a daily basis. This damage must be repaired to preserve genetic information and prevent development of disease. The most deleterious damage is a double-strand break (DSB), which is detected and r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46b663f6afad6c55bc8fdbcb10c5261a
https://doi.org/10.1016/j.jmb.2017.05.029
https://doi.org/10.1016/j.jmb.2017.05.029