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Cited by 107

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Molecular Mechanisms and Regulation of Specific and Nonspecific Autophagy Pathways in Yeast

Nair, Usha, Klionsky, Daniel J.·2005·Journal of Biological Chemistry
DOI 10.1074/jbc.r500016200
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Abstract

The normal growth and development of eukaryotic cells requires a constant balance between biosynthetic and degradative processes. There are two highly conserved mechanisms for degradation in eukaryotes that are responsible for the majority of protein turnover: one is the ubiquitin-proteasome system and the other is autophagy. Under conditions of normal growth, the bulk of protein degradation occurs via the proteasomal machinery (reviewed in Ref. 1). Proteins that are to be degraded are post-translationally tagged with polyubiquitin and are subsequently broken down via the multisubunit 26 S proteasome present in the cytosol and nucleus.

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Crossref · 10.1074/jbc.r500016200

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2 of 2 references verified0 citation errors · 0 not checkable

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  • Fluorescence stopped-flow and chemical cross-linking assays show that Atg18 oligomerizes upon membrane binding, whereas it is mainly monomeric when unbound.

    “Furthermore, fluorescence stopped-flow [835] and chemical cross-linking assays [836] show that Atg18 oligomerizes upon membrane binding, whereas it is mainly monomeric when unbound.”

    From Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition) 1 (2021) · cites this paper as [835]

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Metadata

Authors
Nair, U., & Klionsky, D. J.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2005-12
Volume
280
Issue
51
Pages
41785-41788
ISSN
0021-9258
DOI
10.1074/jbc.r500016200
Cited by
107
References
2
Language
en
Licence

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