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Daniel P. Orban

Researcher at University of Michigan

Publications -  5
Citations -  5357

Daniel P. Orban is an academic researcher from University of Michigan. The author has contributed to research in topics: Autophagy & Ubiquitin ligase. The author has an hindex of 4, co-authored 5 publications receiving 4912 citations. Previous affiliations of Daniel P. Orban include Life Sciences Institute & University of Osnabrück.

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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 Article

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

Daniel J. Klionsky, +2459 more
- 01 Jan 2016 - 
Journal ArticleDOI

Erratum to: Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition) (Autophagy, 12, 1, 1-222, 10.1080/15548627.2015.1100356

Daniel J. Klionsky, +2522 more
- 01 Jan 2016 - 
TL;DR: Author(s): Klionsky, DJ; Abdelmohsen, K; Abe, A; Abedin, MJ; Abeliovich, H; A Frozena, AA; Adachi, H, Adeli, K, Adhihetty, PJ; Adler, SG; Agam, G; Agarwal, R; Aghi, MK; Agnello, M; Agostinis, P; Aguilar, PV; Aguirre-Ghis
Journal ArticleDOI

Atg23 and Atg27 Act at the Early Stages of Atg9 Trafficking in S. cerevisiae

Steven K. Backues, +7 more
- 01 Feb 2015 - 
TL;DR: Four proteins are defined as the core minimal machinery necessary and sufficient for the trafficking of Atg9 to the phagophore assembly site (PAS) and a model is proposed that ties together previous observations regarding the role of AtG9 in autophagosome formation is proposed.
Journal ArticleDOI

CUET-ting edge research

Daniel P. Orban, +1 more
- 01 Jan 2014 - 
TL;DR: The deletion of CUE5 as well as the expression of Cue5 mutants with a nonfunctional AIM- or CUE-domain result in the accumulation of ubiquitinated proteins, leading to the conclusion that Cue5 functions as a ubiquitin-Atg8 receptor similar to SQSTM1 in mammals.