Dr. ANOOP ARUNAGIRI
 
 
First Name
ANOOP
Last Name
ARUNAGIRI
University/Institution
University of Michigan
Email ID
anooparu@umich.edu
City
Ann Arbor
Country
United States
State
Michigan
Zip code
48105
Department
Internal Medicine
Area of Research
Protein misfolding in diabetes
Area of Expertise
Biochemistry
Brief Description of Research Interest:
 

I am Anoop Arunagiri, a Research Investigator in the Arvan Lab in Internal Medicine at the University of Michigan (U-M). I am actively engaged in postdoctoral training since 2016 at the U-M. While my current position is considered a junior faculty level, all of my applications are endorsed by my advisor, Peter Arvan, and my salary is covered through their research funding; which is why I call myself a postdoc. 

My research interests: I am a biochemist doing diabetes research focused on proinsulin misfolding in pancreatic beta cells. Protein folding and aggregation have been my primary areas of interest and expertise. Over the past 15 years, I have explored the fascinating characteristics of protein aggregates, their biological functions, pathological roles, and biomaterial applications. My long-term goal is to study protein folding problems in metabolic disorders and degenerative diseases employing biophysical, biochemical, and cell-biological approaches. Thus far, I have 30 articles to my credit in peer-reviewed journals (please see my CV or the Google Scholar link).

Peer review and editorial services: I have served as a reviewer in more than 20 recognized journals, to name a few, 1) Journal of Biological Chemistry, 2) Biophysical Chemistry, 3) FASEB Journal, 4) Cellular and Molecular Life Sciences, and 5) Autophagy. I currently guest edit special issues in the Frontiers in Molecular Biosciences and Frontiers in Endocrinology.

Regarding communicating science to laypersons, I have participated in several events including 1) Postdoc180 organized by the U-M Office of Graduate & Postdoctoral Studies (2020), 2) Techconnect -- a two-day open-to-public technology outreach exhibition at IIT Bombay, India (2013 and 2014), and one of my publications was showcased as Digest in eLife journal, which is exclusively made for lay audience (Link: https://elifesciences.org/digests/44532/insulin-in-a-tangle).

Following are my Google Scholar, ORCID, and Publons pages/links.

1) Google Scholar page: https://scholar.google.co.in/citations?user=y9ADb94AAAAJ&hl=en
2) ORCID: https://orcid.org/0000-0001-9839-1860
3) Publons: https://publons.com/researcher/1758777/anoop-arunagiri

 
Representative Publications:
 

1) Anoop Arunagiri, Maroof Alam, Leena Haataja, et al, Proinsulin Folding and Trafficking Defects Trigger a Common Pathological Disturbance of Endoplasmic Reticulum Homeostasis (2024), Protein Sci. 2024; 33(4): e4949

2) Xiaoxi Xu, Anoop Arunagiri, Maroof Alam, et al, Nutrient-dependent fluctuation in beta cell proinsulin content (2023), J Biol Chem 2023; 299(7):104836

3) Yu-Jie Chen, Jeffrey Knupp, Anoop Arunagiri, et al. PGRMC1 acts as a size-selective cargo receptor to drive ER-phagic clearance of mutant prohormones (2021), Nat Commun 12, 5991 (2021)

4) Maroof Alam, Anoop Arunagiri, Leena Haataja, et al. Predisposition to Proinsulin Misfolding as a Genetic Risk to Diet-Induced Diabetes (2021), Diabetes 2021; 70(11): 2580-2594

5) Anoop Arunagiri, Leena Haataja, Anita Pottekat, et al. Proinsulin Misfolding is an Early Event in the Progression to Type 2 Diabetes (2019), eLife 2019;8:e44532

6) Anoop Arunagiri, Leena Haataja, Corey N Cunningham, et al. Misfolded Proinsulin in the Endoplasmic Reticulum During Development of Beta Cell Failure in Diabetes (2018), Ann N Y Acad Sci, 1418(1):5-19

7) A Anoop, S Ranganathan, BD Dhaked, et al. Elucidating the role of disulfide bond on amyloid formation and fibril reversibility of somatostatin-14: Relevance to its storage and secretion (2014), J Biol Chem, 289(24):16884-16903

8) NN Jha, A Anoop, S Ranganathan, et al. Characterization of amyloid formation by glucagon-like peptides: role of basic residues in heparin-mediated aggregation (2013), Biochemistry, 52 (49):8800–8810