Zobrazeno 1 - 7
of 7
pro vyhledávání: '"FA, fluorescence anisotropy"'
Autor:
Karin Musier-Forsyth, Ronald C. Wek, Sheree A. Wek, Marina Bakhtina, William A. Cantara, Nathan T. Kudlapur, Danni Jin
Publikováno v:
The Journal of Biological Chemistry
Aminoacyl-tRNA synthetases (ARSs) catalyze the charging of specific amino acids onto cognate tRNAs, an essential process for protein synthesis. Mutations in ARSs are frequently associated with a variety of human diseases. The human EPRS1 gene encodes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1ce97fb563092e3b298c457fe5bda992
http://europepmc.org/articles/PMC8511952
http://europepmc.org/articles/PMC8511952
Intrinsically disordered substrates dictate SPOP subnuclear localization and ubiquitination activity
Publikováno v:
The Journal of Biological Chemistry
Speckle-type POZ protein (SPOP) is a ubiquitin ligase adaptor that binds substrate proteins and facilitates their proteasomal degradation. Most SPOP substrates present multiple SPOP-binding (SB) motifs and undergo liquid–liquid phase separation wit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::865b2261c9773bb5532b2ebeb6469bac
https://pubmed.ncbi.nlm.nih.gov/33894201
https://pubmed.ncbi.nlm.nih.gov/33894201
Autor:
Peter A. Friedman, Kristian Strømgaard, Tatyana Mamonova, Sofie Bach, W. Bruce Sneddon, Maria Vistrup-Parry
Publikováno v:
The Journal of Biological Chemistry
Vistrup-Parry, M, Sneddon, W B, Bach, S, Strømgaard, K, Friedman, P A & Mamonova, T 2021, ' Multisite NHERF1 phosphorylation controls GRK6A regulation of hormone-sensitive phosphate transport ', Journal of Biological Chemistry, vol. 296, 100473 . https://doi.org/10.1016/j.jbc.2021.100473
Vistrup-Parry, M, Sneddon, W B, Bach, S, Strømgaard, K, Friedman, P A & Mamonova, T 2021, ' Multisite NHERF1 phosphorylation controls GRK6A regulation of hormone-sensitive phosphate transport ', Journal of Biological Chemistry, vol. 296, 100473 . https://doi.org/10.1016/j.jbc.2021.100473
The type II sodium-dependent phosphate cotransporter (NPT2A) mediates renal phosphate uptake. The NPT2A is regulated by parathyroid hormone (PTH) and fibroblast growth factor 23, which requires Na+/H+ exchange regulatory factor-1 (NHERF1), a multidom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2f8aed5c7eaceb38b351bf31d2bca9e9
https://pubmed.ncbi.nlm.nih.gov/33639163
https://pubmed.ncbi.nlm.nih.gov/33639163
Publikováno v:
The Journal of Biological Chemistry
Pseudomonas aeruginosa is an opportunistic pathogen requiring iron for its survival and virulence. P. aeruginosa can acquire iron from heme via the nonredundant heme assimilation system and Pseudomonas heme uptake (Phu) systems. Heme transported by e
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a2b6578adf9125a38db2ca75b56e1c0
https://pubmed.ncbi.nlm.nih.gov/33428928
https://pubmed.ncbi.nlm.nih.gov/33428928
Autor:
Magdaléna Krejčíková, Pavel Brázda, Eliška Šmiřáková, Karel Kubíček, Aiste Kasiliauskaite, Robert Vácha, Richard Štefl, Tomáš Klumpler
Publikováno v:
Journal of Molecular Biology
Transcription elongation factor Spt6 associates with RNA polymerase II (RNAP II) via a tandem SH2 (tSH2) domain. The mechanism and significance of the RNAP II–Spt6 interaction is still unclear. Recently, it was proposed that Spt6-tSH2 is recruited
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::764ba3c34d7f239fbb55e63ba21dede1
https://pubmed.ncbi.nlm.nih.gov/32439331
https://pubmed.ncbi.nlm.nih.gov/32439331
Autor:
Yousuke Takaoka, Kaho Suzuki, Akira Nozawa, Hirotaka Takahashi, Tatsuya Sawasaki, Minoru Ueda
Publikováno v:
The Journal of Biological Chemistry
A network of protein–protein interactions (PPI) is involved in the activation of (+)-7-iso-jasmonoyl-L-isoleucine (JA-Ile), a plant hormone that regulates plant defense responses as well as plant growth and development. In the absence of JA-Ile, in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf465c2e9bd4cbc3eb15dd41f90655cc
https://doi.org/10.1016/j.jbc.2021.101504
https://doi.org/10.1016/j.jbc.2021.101504
Publikováno v:
Febs Letters
Highlights • The interaction between Arabidopsis PEX5 and PEX14N is independent of cargo binding. • The affinity of a PTS1 peptide for PEX5 is unaffected by PEX14N binding. • Arabidopsis PEX5 complexes PTS1 and PTS2 cargoes. • PEX5 and 7 co-i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b10072ccdc555446ba1ec9394ad0f01e