Zobrazeno 1 - 10
of 40
pro vyhledávání: '"Rivka L Isaacson"'
Autor:
John F Darby, Ewelina M Krysztofinska, Peter J Simpson, Aline C Simon, Pawel Leznicki, Newran Sriskandarajah, David S Bishop, Lisa R Hale, Caterina Alfano, Maria R Conte, Santiago Martínez-Lumbreras, Arjun Thapaliya, Stephen High, Rivka L Isaacson
Publikováno v:
PLoS ONE, Vol 9, Iss 11, p e113281 (2014)
The BAG6 complex resides in the cytosol and acts as a sorting point to target diverse hydrophobic protein substrates along their appropriate paths, including proteasomal degradation and ER membrane insertion. Composed of a trimeric complex of BAG6, T
Externí odkaz:
https://doaj.org/article/8e8a952f4dc54536822cf9d134d1aff8
Autor:
Pawel Leznicki, Quentin P Roebuck, Lydia Wunderley, Anne Clancy, Ewelina M Krysztofinska, Rivka L Isaacson, Jim Warwicker, Blanche Schwappach, Stephen High
Publikováno v:
PLoS ONE, Vol 8, Iss 3, p e59590 (2013)
The BAG6 protein is a subunit of a heterotrimeric complex that binds a range of membrane and secretory protein precursors localized to the cytosol, enforcing quality control and influencing their subsequent fate.BAG6 has an N-terminal ubiquitin-like
Externí odkaz:
https://doaj.org/article/64d12d24e67b4b8f877d17a4d74feb1f
Autor:
Katherine M. Collins, Nicola J. Evans, James H. Torpey, Jonathon M. Harris, Bethany A. Haynes, Amy H. Camp, Rivka L. Isaacson
Publikováno v:
Microorganisms, Vol 11, Iss 4, p 1077 (2023)
Bacteria use an array of sigma factors to regulate gene expression during different stages of their life cycles. Full-length, atomic-level structures of sigma factors have been challenging to obtain experimentally as a result of their many regions of
Externí odkaz:
https://doaj.org/article/ed100fc3cbe0477ca839ee631769f03e
Publikováno v:
Open Biology, Vol 11, Iss 10 (2021)
Open Biology
Open Biology
Our notions of protein function have long been determined by the protein structure–function paradigm. However, the idea that protein function is dictated by a prerequisite complementarity of shapes at the binding interface is becoming increasingly
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dc7277e6771600687d809c24ca35306e
https://royalsocietypublishing.org/doi/10.1098/rsob.210222
https://royalsocietypublishing.org/doi/10.1098/rsob.210222
Autor:
Rivka L. Isaacson, Ann Witheridge
Publikováno v:
PLoS Biology, Vol 17, Iss 12, p e3000577 (2019)
PLoS Biology
PLoS Biology
Viewing the Invisible is a multimedia collaboration that explores common methodology between arts and sciences. Portraits of science influencers were painted while dialogue between artist and subject was filmed. Here, we show the implementation of ou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4417da2207978c9ccfd113ad0eefd616
https://doaj.org/article/3a180a316da14450b36be4f4a89579e7
https://doaj.org/article/3a180a316da14450b36be4f4a89579e7
Autor:
Ann Hochschild, Caterina Alfano, Ewelina M. Krysztofinska, Rivka L. Isaacson, Cinthia P. Garcia, Anna F. Wang Erickson, Padraig Deighan, Kelsey Barrasso, Santiago Martínez-Lumbreras, Richard Losick, Arjun Thapaliya, Amy H. Camp, Shanshan Chen
Publikováno v:
Wang Erickson, A F, Deighan, P, Chen, S, Barrasso, K, Garcia, C P, Martínez-Lumbreras, S, Alfano, C, Krysztofinska, E M, Thapaliya, A, Camp, A H, Isaacson, R L, Hochschild, A & Losick, R 2017, ' A Novel RNA Polymerase-binding Protein that interacts with a Sigma-Factor Docking Site ', Molecular Microbiology . https://doi.org/10.1111/mmi.13724
Sporulation in Bacillus subtilis is governed by a cascade of alternative RNA polymerase sigma factors. We previously identified a small protein Fin that is produced under the control of the sporulation sigma factor σ(F) to create a negative feedback
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::82a07e2951497dcbc147b45bdebb8c04
https://doi.org/10.1111/mmi.13724
https://doi.org/10.1111/mmi.13724
Publikováno v:
Advances in Protein Chemistry and Structural Biology
SGTA is a co-chaperone that, in collaboration with the complex of BAG6/UBL4A/TRC35, facilitates the biogenesis and quality control of hydrophobic proteins, protecting them from the aqueous cytosolic environment. This work includes targeting tail-anch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::f04d0c70636250c155afb38129b1687d
https://pubmed.ncbi.nlm.nih.gov/30635083
https://pubmed.ncbi.nlm.nih.gov/30635083
Autor:
Irene Díaz-Moreno, Rivka L. Isaacson
Publikováno v:
Frontiers Research Topics ISBN: 9782889457878
Frontiers in Molecular Biosciences
Frontiers in Molecular Biosciences
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b016573856fc66628fe204775c850e6e
https://doi.org/10.3389/978-2-88945-787-8
https://doi.org/10.3389/978-2-88945-787-8
SGTA is a co-chaperone that, in collaboration with the complex of BAG6/UBL4A/TRC35, facilitates the biogenesis and quality control of hydrophobic proteins, protecting them from the aqueous cytosolic environment. This work includes targeting tail-anch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::41d8c6a38adfe55c48ca034846e290af
https://doi.org/10.1016/bs.apcsb.2018.11.002
https://doi.org/10.1016/bs.apcsb.2018.11.002
Autor:
Rivka L. Isaacson, Irene Díaz-Moreno
Publikováno v:
idUS. Depósito de Investigación de la Universidad de Sevilla
instname
Frontiers in Molecular Biosciences, Vol 5 (2019)
instname
Frontiers in Molecular Biosciences, Vol 5 (2019)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba89c8fd1035f2ac580109c42e1db571