Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Nicholas O. Bodnar"'
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance Many proteins in the cell are tagged with a polyubiquitin chain, which serves as a recognition signal for degradation by the proteasome. Some tagged substrates bind directly to the proteasome, but others are delivered through shuttling f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45d9da059d87f71cf02dd514c185f699
https://pubmed.ncbi.nlm.nih.gov/32193351
https://pubmed.ncbi.nlm.nih.gov/32193351
Autor:
Evgeny Nudler, Kelly H. Kim, Zhejian Ji, John R. Engen, Thomas E. Wales, Nicholas O. Bodnar, Thomas Walz, Vladimir Svetlov, Tom A. Rapoport
Publikováno v:
Nature structural & molecular biology
Many poly-ubiquitinated proteins are extracted from membranes or complexes by a conserved ATPase, called Cdc48 in yeast and p97/VCP in mammals, before proteasomal degradation1. Each Cdc48 hexamer contains two stacked ATPase rings (D1 and D2) and six
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6b50d53d795a5dcdacc979c6f27fefb9
http://europepmc.org/articles/PMC6044470
http://europepmc.org/articles/PMC6044470
Autor:
Edward C. Twomey, Jarrod A. Marto, Thomas E. Wales, Nicholas O. Bodnar, Tom A. Rapoport, Scott B. Ficarro, John R. Engen, Zhejian Ji
Publikováno v:
Science. 365
Protein unfolding, one substrate at a time Ubiquitin marks proteins for degradation by the proteasome. However, many substrates cannot be directly degraded because they are well folded or are located in cell membranes or in multimeric complexes. Thes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cdec27e7d6e0d1607a3e81516e4ade73
https://doi.org/10.1126/science.aax1033
https://doi.org/10.1126/science.aax1033
Publikováno v:
Mol Cell
Breathing depends on pulmonary surfactant, a mixture of phospholipids and proteins, secreted by alveolar type II cells. Surfactant requires lamellar bodies (LBs), organelles containing densely packed concentric membrane layers, for storage and secret
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::22a38a2162bf2a26954d7bdbc9589e6d
https://doi.org/10.1016/j.molcel.2020.10.042
https://doi.org/10.1016/j.molcel.2020.10.042
Autor:
Tom A. Rapoport, Nicholas O. Bodnar
The Cdc48 ATPase and its cofactors Ufd1/Npl4 (UN) extract polyubiquitinated proteins from membranes or macromolecular complexes, but how they perform these functions is unclear. Cdc48 consists of an N-terminal domain that binds UN and two stacked hex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ff522809dd06cfb81db0af6c32f9d480
https://europepmc.org/articles/PMC5751438/
https://europepmc.org/articles/PMC5751438/
Autor:
Tom A. Rapoport, Nicholas O. Bodnar
Publikováno v:
F1000Research
A conserved AAA+ ATPase, called Cdc48 in yeast and p97 or VCP in metazoans, plays an essential role in many cellular processes by segregating polyubiquitinated proteins from complexes or membranes. For example, in endoplasmic reticulum (ER)-associate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::134fdde84d10e7e2b2dc5c280d69002c
https://doi.org/10.12688/f1000research.11683.1
https://doi.org/10.12688/f1000research.11683.1