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H

Hai Rao

Researcher at University of Texas Health Science Center at San Antonio

Publications -  50
Citations -  7484

Hai Rao is an academic researcher from University of Texas Health Science Center at San Antonio. The author has contributed to research in topics: Ubiquitin & Ubiquitin ligase. The author has an hindex of 21, co-authored 46 publications receiving 6870 citations. Previous affiliations of Hai Rao include University of British Columbia & Boston University.

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Journal ArticleDOI

Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition)

Daniel J. Klionsky, +2522 more
- 21 Jan 2016 - 
TL;DR: In this paper, the authors present a set of guidelines for the selection and interpretation of methods for use by investigators who aim to examine macro-autophagy and related processes, as well as for reviewers who need to provide realistic and reasonable critiques of papers that are focused on these processes.
Journal ArticleDOI

Degradation of a cohesin subunit by the N-end rule pathway is essential for chromosome stability

Hai Rao, +3 more
- 19 Apr 2001 - 
TL;DR: It is shown that the SCC1 fragment is short-lived, being degraded by the ubiquitin/proteasome-dependent N- end rule pathway, and is the first physiological substrate of the N-end rule pathway that is targeted through its N-terminal residue.
Journal ArticleDOI

The origin recognition complex interacts with a bipartite DNA binding site within yeast replicators

Hai Rao, +1 more
- 14 Mar 1995 - 
TL;DR: Mutation of nucleotides in the B1 element suggests that this element has other functions in the initiation of DNA replication besides participating in the ORC-DNA interaction, supported by DNase I footprint analyses.
Journal ArticleDOI

Recognition of Specific Ubiquitin Conjugates Is Important for the Proteolytic Functions of the Ubiquitin-associated Domain Proteins Dsk2 and Rad23

Hai Rao, +1 more
- 05 Apr 2002 - 
TL;DR: This work characterized a family of proteins that preferentially binds ubiquitylated substrates and multi-Ub chains through a motif termed theubiquitin-associated domain (UBA), and shows that Saccharomyces cerevisiae cells lacking two of these UBA proteins, Dsk2 and Rad23, are deficient in protein degradation mediated by the UFD pathway.
Journal ArticleDOI

Multiple interactions of Rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis

Ikjin Kim, +2 more
- 30 Apr 2004 - 
TL;DR: It is demonstrated that the UBL motif of Rad23 also binds Ufd2, an E4 enzyme essential for ubiquitin chain assembly onto its substrates, suggesting that UBL-mediated interactions may contribute to the substrate specificity of these adaptors.