I am a PhD protein biologist and MD candidate working across proteomics, comparative biology, and translational neuroscience. Twelve years of protein-biology research coalesce with clinical training and independent computational work to inspire creative new ways to understand proteins and advance protein-based therapeutics.
| Research focus | Resolving protein populations by molecular ageProteome Birthdating barcodes proteins by their time of synthesis, enabling both conventional global turnover analysis and age-resolved investigation of specific protein subpopulations. The full temporal labeling series is encoded within a single biological sample, with the potential for extension to single cells. Combined with my experience in comparative biology, translational neuroscience, and independent computation, this framework is a catalyst for the protein-based drug-development programs I aim to help design and implement. |
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| Training | University of Rochester Medical Scientist Training ProgramPhD, Cellular, Developmental & Molecular Biology · 2025University of RochesterMD candidate · expected May 2027University of Rochester School of Medicine & Dentistry |
| Clinical lens | Neuro-oncologyLongitudinal neuro-oncology experience grounds my protein-biology work in unanswered patient-centered questions at the intersection of neurology and oncology. I provide patients with warm and unhurried attention, caring for the whole person while striving to embody Rochester’s Biopsychosocial Model. |
| Evidence | Proteome Birthdating Bio-protocol Comparative SIRT6 |
Scene 1 · Intracellular proteome
A living cellular landscape: ions cross membrane channels, cargo moves through nuclear pores, vesicles travel along cytoskeletal tracks, and organelles pulse around a crowded proteome.
My path through protein biology began with ER-associated degradation in 2014 and quickly became an irrational passion for ubiquitin biology that has guided me ever since. During my PhD in the Ghaemmaghami and Gorbunova laboratories, I developed Proteome Birthdating to barcode proteins by their time of synthesis, or molecular age. I now bring that strong molecular foundation to my clinical training as an MD candidate at the University of Rochester School of Medicine & Dentistry.
University of RochesterGhaemmaghami and Gorbunova laboratoriesDissertationProteome Birthdating for Temporally Resolved Insights into Mammalian Aging
University of Rochester School of Medicine & DentistryMedical Scientist Training ProgramClinical focusNeurology · oncology · neuro-oncology
Longitudinal experience with Nimish A. Mohile spanning clinic, tumor board, and division presentations.
URMC Human Structure & Function tutor · 2020–2021. I enjoy turning complex molecular and clinical concepts into clear, visual, usable explanations through tutoring, scientific animation, and interactive tools.
Twelve years investigating how cells detect, modify, and degrade proteins.
Targeted degradation, proteomics, proteostasis, and computationally enabled discovery.
| 2014 | Rutgers RWJMS · introduction to ubiquitinKiran Madura laboratory · Studied Ubc7 and ER-associated degradation. |
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| 2015–2018 | UCLA · protein biologyJames A. Wohlschlegel laboratory · Characterized the KCTD7 interactome and investigated ubiquitin–proteasome–autophagy crosstalk in pediatric neurodegenerative epilepsy. |
| 2016–2018 | UCLA · translational neuroscienceS. Thomas Carmichael laboratory · Contributed to a hydrogel-delivered interneuron-progenitor therapy for cortical stroke through animal efficacy studies, behavioral analysis, and immunohistochemistry. |
| 2018–2019 | UCLA · iPSC-derived cell therapyWilliam E. Lowry laboratory · Generated patient-derived glial progenitors across five donor lines. |
| 2019–present | University of Rochester · MD/PhD trainingSina Ghaemmaghami and Vera Gorbunova laboratories · Proteome Birthdating for Temporally Resolved Insights into Mammalian Aging · PhD 2025 · MD expected May 2027. |
| Where I’m headed | Protein-based drug developmentBringing ubiquitin biology, proteomics, clinical training, and independent computation together to help design and implement protein-based drug-development programs. |
Selected photographs from the laboratories and training communities that shaped my path.
ABTA Medical Student Summer Fellowship · AAN Medical Student Research Scholarship · US HUPO Travel Award · Invited Bio-protocol Webinar.
Scene 2 · Ribosome assembly
The large and small ribosomal subunits assemble around messenger RNA, ready to translate its sequence into a protein.
A through-line across my portfolio: a protein’s cellular context helps shape its structure, function, interaction network, and potential contribution to disease.
Within a cell, proteins have distinct and highly variable half-lives, producing molecular ages that range from seconds to years. Yet how a protein’s age shapes its interactions with the cellular environment remains largely unexplored. To investigate the age selectivity of cellular pathways, I developed Proteome Birthdating, a mass spectrometry–based methodology that barcodes proteins according to their time of synthesis and encodes multiple labeling time points within a single biological sample and, in theory, within individual cells. The approach provides conventional turnover measurements while also resolving the age distributions of specific protein subpopulations. In its first use case, we conducted an age census of the human ubiquitinome. In human fibroblasts, our data indicated that newly synthesized proteins comprised the majority of ubiquitinated molecules and the bulk of measured proteasomal flux.
Complementary structural proteomics revealed that these rapidly degraded proteins often occupy non-native conformations and are ubiquitinated at lysines normally buried within their native structures. I have also published an accompanying practical Bio-protocol that translates Proteome Birthdating into an end-to-end workflow spanning cell culture, sequential isotopic labeling, protein extraction and digestion, peptide cleanup, LC-MS/MS acquisition, data processing, and interpretation. Together, these studies connect molecular age, structural integrity, and ubiquitin selection while establishing Proteome Birthdating as a robust and generalizable framework for investigating the age selectivity of diverse cellular pathways.
Comparative biology reframes evolutionary diversity as a set of natural experiments. Mammals are particularly informative for studying longevity because they are phylogenetically related yet differ by more than 100-fold in maximum lifespan and span an extraordinary range of body sizes. Moreover, the longest-lived mammals occupy distinct evolutionary lineages, suggesting that longevity can arise through multiple biological routes. In one comparative study, we used a targeted proteomic approach across mammalian species to demonstrate that the presence and use of phosphorylation sites in the SIRT6 C-terminal domain correlate with maximum lifespan. Follow-up biochemical and computational studies suggested that this hyperphosphorylation may enhance PARP1 interaction. Further, targeted perturbation of one of these sites in human SIRT6 shifted cellular resistance to oxidative stress in both directions. This work illustrates how comparative proteomics can move from an evolutionary association to a specific molecular mechanism with potential therapeutic relevance.
A second emerging comparative thread uses the amyloidosis-prone rodent Octodon degus as a model of putative proteostatic deficiency. Here we set out to ask how long-lived mammals maintain their proteomes across extraordinary lifespans, particularly in post-mitotic neurons and the astrocytes that support them.
Working in translational neuroscience has taught me to move between molecular mechanisms, model systems, therapeutic design, and, ultimately, the patients these efforts are meant to serve. At UCLA, in the laboratory of James A. Wohlschlegel, I characterized the KCTD7 interactome and investigated crosstalk among the ubiquitin–proteasome and autophagy–lysosome systems in pediatric neurodegenerative epilepsy. This work helped define KCTD7 deficiency as a distinct, early-onset neurodegenerative disorder and implicated a conserved autophagy–lysosome defect in its pathogenesis.
Simultaneously, in the laboratory of S. Thomas Carmichael, I contributed to the development of a hydrogel-delivered interneuron-progenitor therapy for cortical stroke through animal efficacy studies, behavioral analysis, and immunohistochemistry. After graduating early, I completed a gap year as a Laboratory Assistant I in William E. Lowry’s laboratory, where I generated patient-derived glial progenitors across five donor lines. These cells ultimately formed the basis of preclinical studies evaluating a novel cell-based therapy for white-matter stroke and vascular dementia.
My work spans experimental design, sample preparation, and computational analysis. I have developed quantitative proteomics workflows on Orbitrap and Astral platforms using NeuCode and SILAC metabolic labeling, DDA, DIA, targeted acquisition, and diGly and phosphopeptide enrichment. At the bench, I have cultured primary and immortalized cell lines from more than 20 mammalian species and differentiated iPSC lines from five donors into glial-enriched progenitors.
My broader bench experience includes mass spectrometry sample preparation, CRISPR-based perturbation, immunoprecipitation and co-immunoprecipitation, Western blotting, qPCR, molecular cloning, biochemical activity assays, and immunohistochemistry. I analyze proteomic data using Proteome Discoverer, MaxQuant, DIA-NN, FragPipe, Skyline, and Perseus, then use Python, R, and Mathematica for statistical analysis, kinetic modeling, visualization, and reproducible workflows. For structural questions, I integrate AlphaFold models, PyMOL, and in-house solvent-accessibility analyses. I have applied this toolkit to proteome-wide and targeted turnover measurements, post-translational-modification mapping, comparative proteomics, patient-derived disease models, and translational neuroscience.
Scene 3 · Translation
Translation converts an mRNA sequence into a growing polypeptide or protein.
Three works in development spanning computational biology, experimental design, and molecular storytelling.
Model building, benchmarking, and biological prediction, beginning with unseen-context perturbation response.
A computational biology project on predicting CRISPRi responses in unseen cell contexts, with explicit model design, validation logic, leakage checks, failure analysis, and public-safe results.
Experimental design informed by molecular age, beginning with Proteome Birthdating.
An applied Proteome Birthdating workbench that moves from a biological question to a sequential labeling scheme and modeled molecular-age cohorts, supported by a half-life inventory, kinetic fitting, and candidate-degron scan.
Visual stories about protein lifetimes and the molecular events that shape disease and treatment.
An unfinished protein acquires a K48 chain, reaches the proteasome, and receives a deubiquitinase-mediated reprieve in this mechanism-first rough cut.
Scene 4 · Ribosome-associated quality control
After a stalled ribosome is split, NEMF and Listerin help mark an aberrant nascent protein with ubiquitin for degradation.
My publications span proteomics, comparative biology, and translational neuroscience. Together, they reflect rigorous training and a unique, dynamic toolset for translating basic protein insights toward therapeutic discovery.
From ERAD and E3 adaptors to turnover and the proteasome.
Primary research paper with a reproducible open protocol.
Mechanistic depth with clinical and translational training.
Targeted protein degradation, proteostasis, and discovery-proteomics roles.
| Year | Authorship | Publication |
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| 2026 | Co-first author | Long-lived mammals contain more phosphorylation sites in the SIRT6 C-terminus that enhance PARP1 interaction and resistance to oxidative stressGeroScience · DOI |
| 2026 | Third author | Structural proteomics reveals that misfolded nascent proteins expose buried lysines for ubiquitination and rapid proteasomal degradationCell Reports · DOI |
| 2026 | Co-author | cGAS-deficient mice display premature aging associated with derepression of LINE1 elements and inflammationNature Aging · DOI |
| 2025 | First author | Proteome Birthdating: A single-sample approach for measuring global turnover dynamics and “protein age”Bio-protocol · DOI |
| 2024 | First author | Proteome birthdating reveals age-selectivity of protein ubiquitinationMolecular & Cellular Proteomics · DOI |
| 2021 | Third author | Reliable generation of glial enriched progenitors from human fibroblast-derived iPSCsStem Cell Research · DOI |
| 2018 | Co-author | KCTD7 deficiency defines a distinct neurodegenerative disorder with a conserved autophagy–lysosome defectAnnals of Neurology · DOI |
| Full list | Profiles | PubMed ORCID Google Scholar ResearchGate |
Scene 5 · 26S proteasome recognition
A K48-linked ubiquitin chain presents the ubiquitinated substrate to the 26S proteasome for recognition, unfolding, and processing.
I am open to a variety of industry or independent opportunities in proteostasis and protein-based therapeutic discovery. I will complete my MD in May 2027 and am available for part-time work until then and full-time work thereafter. Please find all of my relevant links below. I look forward to building something excellent together!
| Email / résumé | michael_meadow@urmc.rochester.eduView résumé |
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| Profiles | PubMed ORCID Google Scholar ResearchGate LinkedIn X Bluesky |
| Availability | Part-time through May 2027; full-time thereafter. |
| Scientific focus | Ubiquitin, proteostasis, and protein-based therapeutic discovery. |
| Role families | Industry and independent research opportunities. |
| Accessibility | Accessibility statement and feedback |
Snow-day specialist and unofficial welcome committee.
Scene 6 · Proteasomal degradation
The 26S proteasome unfolds and degrades the ubiquitinated substrate, releasing short peptides for downstream processing and amino acid recycling.
