About

Matthew Griffin is an Assistant Professor at the University of California, Irvine, within the Department of Chemistry. He is affiliated with the School of Physical Sciences and is involved in research through the Griffin Lab. His contact information includes an email at griffin@uci.edu and a phone number 949-824-7640. His office is located in 2131 Natural Sciences II at UC Irvine. The page indicates his role as a faculty member, but does not provide specific details about his research focus, background, or key contributions.

Research topics

• Biology
• Immunology
• Internal medicine
• Medicine
• Oncology
• Cancer research
• Biochemistry
• Microbiology
• Genetics

Selected publications

• Functional analysis of O-GlcNAcylation by networking of OGT interactors and substrates

  Nature Chemical Biology · 2026-02-03 · 2 citations

  articleOpen access1st authorCorresponding

  The post-translational modification (PTM) of proteins by O-linked β-N-acetyl-D-glucosamine (O-GlcNAcylation) is widely found across the proteome and regulates diverse cellular processes, from transcription and translation to signal transduction and metabolism. However, most functional studies to date have focused on individual modifications, overlooking other simultaneous O-GlcNAcylation events that work together to coordinate cellular activities. Here we describe networking of O-GlcNAc transferase interactors and substrates (NOTISE), a systems-level approach that monitors O-GlcNAcylation rapidly and comprehensively across the proteome to reveal important functional and regulatory relationships. The NOTISE method integrates affinity purification–mass spectrometry and site-specific chemoproteomic technologies with network generation to connect putative upstream regulators and downstream targets of O-GlcNAcylation. The resulting data-rich networks identify critical conserved activities of O-GlcNAcylation and tissue-specific functions. This holistic and unbiased approach provides a broadly applicable framework to catalyze investigations into the functional roles of coordinated, multisubstrate PTMs in specific cellular and physiological contexts. Functional studies of O-GlcNAcylation have often focused on individual modifications. Now, a systems-level approach has identified simultaneous O-GlcNAcylation events that coordinate cellular activities and tissue-specific functions.

  PublisherDOI

• Flow Cytometric Screening Reveals Nucleic Acid Dyes Aberrantly Stain Peptidoglycan Sacculi

  ACS Infectious Diseases · 2026-02-25

  articleOpen accessSenior authorCorresponding

  Flow cytometry is an essential tool to discern phenotypic and functional differences in single cell mixtures. Most efforts to develop and deploy multicolor flow panels have focused on mammalian cells, whereas a more limited palette of tools exists for microbiota and pathogen-focused analyses. Here, we describe a systematic screen of commercially available nucleic acid dyes to aid in the development of multicolor panels for both Gram-negative and Gram-positive bacteria. We found that dyes show responses that varied by orders of magnitude across two model bacteria. When examining whether dyes can help to discriminate intact cells from noncellular debris, we discovered that certain compounds also bind to purified peptidoglycan with intensities comparable to those observed with bacterial binding. Together, these data will aid in the selection of specific reagents to use in the development of larger scale, multicolor panels for microbial flow cytometry.

  PublisherDOI

• Molecular Reporters for Mammalian Sugars via Hydrogen Bonding Auxiliaries

  ChemRxiv · 2026-03-23

  articleOpen access

  Glycans are essential transmitters of biological information. However, their complex and dynamic structures remain difficult to characterize, posing a major barrier to fully understanding their biological functions. Here, we demonstrate that hydrogen bonding auxiliaries positioned adjacent to the boron site of turn-on fluorogenic phenylboronic acid reporters serve as key modulators of sensitivity to mammalian sugars, providing a new design principle analogous to the hydrogen bonding networks found in lectin binding pockets. We show that these auxiliaries tune sensitivity both globally and for individual mammalian sugars and reveal a striking differential turn-on response between the anomeric forms of monosaccharides. The versatility of these selective and reversible molecular reporters is demonstrated through in-gel glycoprotein imaging, flow cytometry, and cell-surface visualization, establishing them as a generalizable chemical platform for interrogating mammalian glycans.

  PublisherOA PDFDOI

• Exploration of protein degradability enables fully endogenous MrTAC degraders

  Chem · 2026-03-01

  article
  PublisherDOI

• Microbial metabolite L-rhamnose glycates intracellular mammalian proteins

  ChemRxiv · 2026-02-18

  articleOpen accessSenior author

  Host organisms surveil their resident microbiota through the detection of specific microbial metabolites. These molecular patterns are often sensed through noncovalent interactions with pattern recognition receptors. Here, we demonstrate that the non-mammalian monosaccharide L-rhamnose (L-Rha) interacts with host proteins covalently through protein glycation. Through in vitro models of glycation, we find that L-Rha reacts with protein residues and forms advanced glycation end products that can be sensed by host receptors. Using a nonnatural L-Rha analog along with flow cytometry, we show widespread modification of the mammalian proteome across multiple cell lines that mimic the composition of the intestinal wall. Chemoproteomic identification of L-Rha glycation targets reveals that L-Rha enters cells and forms covalent adducts with intracellular proteins enriched within the endoplasmic reticulum and mitochondrion. Together, our work uncovers a potential new mechanism for microbiota-mediated host modification via the innate reactivity of microbially generated reducing sugars.

  PublisherOA PDFDOI

• Call for Papers: The Role of Microbiota in Infection and Immunity

  ACS Infectious Diseases · 2024-10-30

  paratext1st authorCorresponding
  PublisherDOI

• Discovering microbiota functions via chemical probe incorporation for targeted sequencing

  Current Opinion in Chemical Biology · 2024-11-30 · 1 citations

  reviewOpen accessSenior authorCorresponding

  Our microbiota plays crucial roles in immune development and homeostasis and has been implicated in virtually all major diseases of the 21st century. Nevertheless, our understanding of the exact microbial functions that underlie these correlations remains extremely limited, due in large part to the difficulty of profiling cellular activities within non-model organisms and complex communities. Over the past decade, new flow cytometric approaches have been developed to distinguish specific microbial populations based on their interactions with metabolite analogs, modified biomolecules, and reactive compounds. By selecting and separating active microbes via fluorescence-activated cell sorting, PRobe INcorporation for Targeted sequencing (PRINT-seq) has inspired innovative approaches to identify and characterize functional members of our microbiota. Here, we provide a broad overview of this evolving technology and summarize how this method has been recently employed as a diagnostic fingerprint for diverse microbial activities.

  PublisherDOI

• Antimicrobial overproduction sustains intestinal inflammation by inhibiting Enterococcus colonization

  Cell Host & Microbe · 2023-08-30 · 57 citations

  articleOpen access
  PublisherOA PDFDOI

• Functional glycoproteomics by integrated network assembly and partitioning

  bioRxiv (Cold Spring Harbor Laboratory) · 2023-06-14 · 7 citations

  preprintOpen access1st authorCorresponding

  SUMMARY The post-translational modification (PTM) of proteins by O-linked β- N -acetyl-D-glucosamine (O-GlcNAcylation) is widespread across the proteome during the lifespan of all multicellular organisms. However, nearly all functional studies have focused on individual protein modifications, overlooking the multitude of simultaneous O-GlcNAcylation events that work together to coordinate cellular activities. Here, we describe N etworking of I nteractors and S ubstrat E s (NISE), a novel, systems-level approach to rapidly and comprehensively monitor O-GlcNAcylation across the proteome. Our method integrates affinity purification-mass spectrometry (AP-MS) and site-specific chemoproteomic technologies with network generation and unsupervised partitioning to connect potential upstream regulators with downstream targets of O-GlcNAcylation. The resulting network provides a data-rich framework that reveals both conserved activities of O-GlcNAcylation such as epigenetic regulation as well as tissue-specific functions like synaptic morphology. Beyond O-GlcNAc, this holistic and unbiased systems-level approach provides a broadly applicable framework to study PTMs and discover their diverse roles in specific cell types and biological states.

  PublisherOA PDFDOI

• <i>N</i>-Arylpyrazole NOD2 Agonists Promote Immune Checkpoint Inhibitor Therapy

  ACS Chemical Biology · 2023-05-12 · 11 citations

  articleOpen access1st author

  The characterization of microbiota mechanisms in health and disease has reinvigorated pattern recognition receptors as prominent targets for immunotherapy. Notably, our recent studies on Enterococcus species revealed peptidoglycan remodeling and activation of NOD2 as key mechanisms for microbiota enhancement of immune checkpoint inhibitor therapy. Inspired by this work and other studies of NOD2 activation, we performed in silico ligand screening and developed N-arylpyrazole dipeptides as novel NOD2 agonists. Importantly, our N-arylpyrazole NOD2 agonist is enantiomer-specific and effective at promoting immune checkpoint inhibitor therapy and requires NOD2 for activity in vivo. Given the significant functions of NOD2 in innate and adaptive immunity, these next-generation agonists afford new therapeutic leads and adjuvants for a variety of NOD2-responsive diseases.

  PublisherOA PDFDOI

Frequent coauthors

• Howard C. Hang

  Harvard University

  42 shared

• Linda C. Hsieh–Wilson

  California Institute of Technology

  19 shared

• Howard C. Hang

  Scripps Research Institute

  18 shared

• Xiaohui Zhao

  Zhejiang University

  8 shared

• Kathryn R. Stein

  Icahn School of Medicine at Mount Sinai

  8 shared

• Shannon E. Stone

  7 shared

• Juliel Espinosa

  Rockefeller University

  6 shared

• Taku Tsukidate

  6 shared

Labs

• Griffin LabPI