Hening Lin
· ProfessorUniversity of Chicago · Department of Chemistry
Active 1997–2026
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About
Hening Lin, PhD, is an investigator whose research focuses on enzymes that post-translationally modify proteins. His work centers on nicotinamide adenine dinucleotide (NAD)-consuming enzymes, including sirtuins and ADP-ribosyltransferases, as well as the ZDHHC family of palmitoyltransferases. Lin and his team employ a multidisciplinary approach combining organic chemistry, biochemistry, cell biology, and mouse genetics to discover new enzymatic activities and to understand the physiological functions of these enzymes. A particular emphasis of their research is on the regulation of these enzymes, as understanding their regulation often reveals key physiological roles. This knowledge enables the development of small molecule inhibitors that have potential as therapeutics for treating human diseases.
Research topics
- Biochemistry
- Biology
- Cell biology
- Chemistry
- Cancer research
- Genetics
- Computational biology
Selected publications
Journal of the American Chemical Society · 2025-09-05 · 6 citations
articleOpen accessMost eukaryotic membranes comprise phospholipids bearing two hydrophobic tails, but N-acylphosphatidylethanolamine (NAPE) stands out as a long-known but poorly understood phospholipid with three hydrophobic groups. What little attention NAPE has received has been devoted to understanding its metabolic functions as a precursor to N-acylethanolamine (NAE), a bioactive lipid that acts as an endocannabinoid. Yet, levels of NAPE increase during myocardial infarction and ischemia, suggesting potential…
bioRxiv (Cold Spring Harbor Laboratory) · 2026-04-28
articleOpen accessSenior authorAbstract Coenzyme A (CoA) is an essential cofactor required for numerous metabolic reactions, yet its ability to bind and regulate proteins remains poorly defined. Using a proteomic approach, we identified malic enzyme 2 (ME2) as a CoA-binding protein. ME2 uses NAD(P) + to convert malate to pyruvate, generating NAD(P)H to support energy production and redox homeostasis. ME2 binds CoA at an allosteric site previously thought to bind NAD(P) + . Reduced CoA has minimal effect on ME2 activity, but t…
eLife · 2026-01-19
articleOpen accessLegionella pneumophila is an opportunistic bacterial pathogen that causes Legionnaires’ disease. To establish an intracellular niche conducive to replication, L. pneumophila translocates a diverse array of effector proteins that manipulate various host cellular processes, including the actin cytoskeleton. In a screen for effectors that alter actin dynamics, we identified a Legionella effector, Lfat1 (lpg1387), which colocalizes with the actin cytoskeleton in eukaryotic cells. Lfat1 specifically…
2026-01-28
peer-reviewOpen accessMethods in enzymology on CD-ROM/Methods in enzymology · 2026-01-01
book-chapterSenior authorCorresponding
Recent grants
Metabolite Sensing and Regulation of Protein Function
NIH · $1.9M · 2019–2024
SIRT6 and lysine fatty acylation in macrophage inflammation
NIH · $2.0M · 2016–2021
Distance-Hi-C: Creating Photo Activated X-linkers To Define Nuclear Architecture
NIH · $3.6M · 2015–2020
Frequent coauthors
- 56 shared
Jun Young Hong
Cornell University
- 46 shared
Xiaoyu Zhang
- 35 shared
Ji Cao
Zhejiang University
- 34 shared
Miao Wang
Hangzhou Normal University
- 32 shared
Ari Melnick
Cornell University
- 31 shared
Bin He
Guiyang Medical University
- 27 shared
Quan Hao
Institute of Soil and Water Conservation
- 27 shared
Nicole A. Spiegelman
Cornell University
Labs
Awards & honors
- Cornell University - Howard Hughes Medical Institute Investi…
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