Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Randi G. Reed"'
Publikováno v:
Cell Reports, Vol 26, Iss 2, Pp 483-495.e5 (2019)
Summary: The 26S proteasome is the central ATP-dependent protease in eukaryotes and is essential for organismal health. Proteasome assembly is mediated by several dedicated, evolutionarily conserved chaperone proteins. These chaperones associate tran
Externí odkaz:
https://doaj.org/article/9e515e8be83e43a681241c3474409c3a
The 26S proteasome is an ∼70 subunit ATP-dependent chambered protease that destroys proteins via multiple highly coordinated processing steps. The smallest and only intrinsically disordered proteasome subunit, Sem1 (DSS1 in metazoans), is critical
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::62bc603b7dc30f3f783670d6b8c664a2
https://doi.org/10.1101/2022.06.27.497739
https://doi.org/10.1101/2022.06.27.497739
Publikováno v:
The FASEB Journal. 35
Autor:
Robert J. Tomko, Randi G. Reed
Publikováno v:
Methods in enzymology. 619
The 26S proteasome is a multisubunit ATP-dependent peptidase complex mediating most regulated protein degradation in eukaryotes. The proteasome undergoes several coordinated conformational changes during catalysis that activate it for substrate proce
Autor:
István Nagy, Florian Beck, Guenter Pfeifer, Wolfgang Baumeister, Robert J. Tomko, Till Rudack, Andreas Schweitzer, Juergen M. Plitzko, Randi G. Reed, Eri Sakata, Markus R. Eisele
Publikováno v:
Cell Reports
Summary The proteasome is the central protease for intracellular protein breakdown. Coordinated binding and hydrolysis of ATP by the six proteasomal ATPase subunits induces conformational changes that drive the unfolding and translocation of substrat
Publikováno v:
Cell reports
Cell Reports, Vol 26, Iss 2, Pp 483-495.e5 (2019)
Cell Reports, Vol 26, Iss 2, Pp 483-495.e5 (2019)
SUMMARY The 26S proteasome is the central ATP-dependent protease in eukaryotes and is essential for organismal health. Proteasome assembly is mediated by several dedicated, evolutionarily conserved chaperone proteins. These chaperones associate trans
Autor:
Claudius Mundoma, Gaurav Ghag, Randi G. Reed, Melissa A. Moss, Nicholas P. van der Munnik, Lauren M. Wolf, Vijayaraghavan Rangachari
Publikováno v:
Protein engineering, designselection : PEDS. 29(5)
Granulins (Grns) are a family of small, cysteine-rich proteins that are generated upon proteolytic cleavage of their precursor, progranulin (Pgrn). All seven Grns (A-G) contain 12 conserved cysteines that form 6 intramolecular disulfide bonds, render