Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Meredith B Metzger"'
Autor:
Meredith B Metzger, Jessica L Scales, Mitchell F Dunklebarger, Jadranka Loncarek, Allan M Weissman
Publikováno v:
eLife, Vol 9 (2020)
Maintaining the essential functions of mitochondria requires mechanisms to recognize and remove misfolded proteins. However, quality control (QC) pathways for misfolded mitochondrial proteins remain poorly defined. Here, we establish temperature-sens
Externí odkaz:
https://doaj.org/article/e73bf037a4654b3184751ac95f8c9224
Publikováno v:
G3: Genes, Genomes, Genetics, Vol 7, Iss 11, Pp 3731-3743 (2017)
Protein degradation by the ubiquitin-proteasome system is essential to many processes. We sought to assess its involvement in the turnover of mitochondrial proteins in Saccharomyces cerevisiae. We find that deletion of a specific ubiquitin ligase (E3
Externí odkaz:
https://doaj.org/article/6bf360f5c7e64a50a9d7fde51015da84
Publikováno v:
Acta Crystallographica. Section F, Structural Biology Communications
A 1.7 Å resolution co-crystal structure of U7BR from Schizosaccharomyces pombe in complex with Ubc7 is reported. Structural comparisons and biochemistry suggest that U7BR presents a steric impediment to E1 binding and inhibits E1-mediated charging,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e956b8a84be04c211071e14d6b53c4d0
https://doi.org/10.1107/s2053230x19009786
https://doi.org/10.1107/s2053230x19009786
Autor:
Allan M. Weissman, Mitchell F Dunklebarger, Jessica L Scales, Jadranka Loncarek, Meredith B. Metzger
Publikováno v:
eLife, Vol 9 (2020)
eLife
eLife
Maintaining the essential functions of mitochondria requires mechanisms to recognize and remove misfolded proteins. However, quality control (QC) pathways for misfolded mitochondrial proteins remain poorly defined. Here, we establish temperature-sens
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e273f7c64bccd5669740adac382e1f2
https://elifesciences.org/articles/51065
https://elifesciences.org/articles/51065
Publikováno v:
G3: Genes, Genomes, Genetics, Vol 7, Iss 11, Pp 3731-3743 (2017)
Protein degradation by the ubiquitin-proteasome system is essential to many processes. We sought to assess its involvement in the turnover of mitochondrial proteins in Saccharomyces cerevisiae. We find that deletion of a specific ubiquitin ligase (E3
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec1c07ad0e55df30fe9e26573da28e07
http://g3journal.org/lookup/doi/10.1534/g3.117.300227
http://g3journal.org/lookup/doi/10.1534/g3.117.300227
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1843:47-60
RING finger domain and RING finger-like ubiquitin ligases (E3s), such as U-box proteins, constitute the vast majority of known E3s. RING-type E3s function together with ubiquitin-conjugating enzymes (E2s) to mediate ubiquitination and are implicated
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c7d193ef7679c2c966a84637b7ee15e
https://doi.org/10.1016/j.bbamcr.2013.05.026
https://doi.org/10.1016/j.bbamcr.2013.05.026
Publikováno v:
Journal of Cell Science. 125:531-537
The post-translational attachment of ubiquitin, a highly conserved 76-amino-acid polypeptide, directs myriad eukaryotic proteins to a variety of fates and functions. Ubiquitylation is best-known for targeting proteins for degradation by the 26S prote
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d1ce252b39d8a1f20671d786079f07c0
https://doi.org/10.1242/jcs.091777
https://doi.org/10.1242/jcs.091777
Autor:
G. Michael Preston, Jeffrey L. Brodsky, Susan Michaelis, Christopher J. Guerriero, Meredith B. Metzger
Publikováno v:
Molecular Cell. 70:242-253.e6
Summary Misfolded proteins in the endoplasmic reticulum (ER) are destroyed by ER-associated degradation (ERAD). Although the retrotranslocation of misfolded proteins from the ER has been reconstituted, how a polypeptide is initially selected for ERAD
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce0bc1c99ff700ea1b6d62229d115b2e
https://doi.org/10.1016/j.molcel.2018.03.016
https://doi.org/10.1016/j.molcel.2018.03.016
Insights into Ubiquitination from the Unique Clamp-like Binding of the RING E3 AO7 to the E2 UbcH5B*
Autor:
Meredith B. Metzger, Daniel K. Stringer, Jess Li, Allan M. Weissman, Jennifer Mariano, Yu-He Liang, Yien Che Tsai, Ventzislava A. Hristova, Shengjian Li, Xinhua Ji, Paul A. Randazzo
RING proteins constitute the largest class of E3 ubiquitin ligases. Unlike most RINGs, AO7 (RNF25) binds the E2 ubiquitin-conjugating enzyme, UbcH5B (UBE2D2), with strikingly high affinity. We have defined, by co-crystallization, the distinctive mean
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::af940272e730a82913133b796ed68b0c
https://europepmc.org/articles/PMC4683248/
https://europepmc.org/articles/PMC4683248/
