جستجوی استاد راهنمای دانشگاهی

Daniel Finleyمشاهده پروفایل

استاد

• Ubiquitin-Proteasome Pathway
• Proteostasis
• Protein Degradation
• +۷ مورد دیگر

Daniel Finley is a Professor of Cell Biology at Harvard Medical School (HMS), leading the Finley Lab focused on the ubiquitin-proteasome pathway and related regulatory mechanisms. He holds academic appointments within the Department of Cell Biology and sits on the Scientific Advisory Boards of Proteostasis and X-Chem Pharmaceuticals. His research investigates proteasome function, ubiquitin-like proteins, and proteostasis roles in diseases like Alzheimer’s and ALS. Dr. Finley earned his undergraduate degree in biochemistry from Harvard University and a Ph.D. in molecular biology from MIT. After postdoctoral training at MIT, he joined HMS in 1988. His lab explores topics including erythroid proteome remodeling, mitochondrial dysfunction, and neurodegenerative disease mechanisms. Key research areas include: (1) Ubiquitin-proteasome pathway regulation, (2) Proteasome structure/function, (3) Nonproteolytic roles of ubiquitination, and (4) Pathophysiological roles of proteostasis defects in diseases. His work bridges basic cell biology with translational medicine, particularly in neurodegeneration and anemia. Finley has secured NIH funding for projects like 'Regulation of Proteasome Activity' (R35GM145246) and 'Erythrocyte maturation through global proteome remodeling' (R01HL153970). Collaborations with industry and academic partners extend his impact in drug discovery and proteasome-targeted therapies. His lab’s contributions include defining ubiquitin chain editing mechanisms, identifying USP14’s role in mitophagy, and elucidating proteostasis defects in Alzheimer's models. Research tools developed include advanced cryo-EM analyses of proteasomal structures and functional assays for ubiquitin system enzymes.

Thibault Mayorمشاهده پروفایل

استاد

• Protein Homeostasis
• Ubiquitin Proteasome System
• Neurodegenerative Diseases
• +۷ مورد دیگر

Thibault Mayor is a Professor in the Department of Biochemistry and Molecular Biology and the Michael Smith Laboratories at the University of British Columbia (Vancouver). His research focuses on understanding how cells manage misfolded proteins, with implications for neurodegenerative diseases like Parkinson's and Alzheimer's. He holds academic affiliations with the Centre for High-Throughput Biology (CHiBi) and has been recognized with awards including the UBC Killam Teaching Award (2020). Education: BSc, University of Geneva, Switzerland (1997) PhD, University of Geneva & Max Planck Institute of Biochemistry, Germany (2001) Postdoctoral Fellow, California Institute of Technology (2002) Research Interests: Mayor's lab investigates protein homeostasis, ubiquitin-proteasome system dynamics, and the molecular mechanisms underlying protein aggregation in aging and disease. Projects include proteomic approaches to identify aggregation-prone proteins and develop microbial cell factories for protein production. Grants & Awards: CIHR Project Grant ($730K, 2018) Michael Smith Foundation Career Award (2012) UBC Killam Teaching Award (2020) Labs & Collaborations: The Mayor Lab is part of the Michael Smith Laboratories and collaborates with computational biologists like Jörg Gsponer. They maintain active partnerships in proteomics and systems biology, contributing to initiatives like the BC Proteomics Network.

David S. Eisenbergمشاهده پروفایل

استاد

• Protein Aggregation
• Amyloid Structures
• Prion Diseases
• +۵ مورد دیگر

David S. Eisenberg is a Professor of Chemistry and Biochemistry and Biological Chemistry at the University of California, Los Angeles, where he also serves as Director of the UCLA-DOE Institute for Genomics and Proteomics and as an HHMI Investigator. His research focuses on protein interactions, particularly the structural basis for conversion of normal proteins to the amyloid state and conversion of prions to the infectious state. Dr. Eisenberg earned his undergraduate degree in biochemical sciences from Harvard College and his D.Phil. degree in theoretical chemistry from Oxford University on a Rhodes Scholarship. His postdoctoral research was on ice and water with Walter Kauzmann at Princeton and in protein crystallography with Richard Dickerson. He joined the UCLA faculty after his postdoctoral studies. Dr. Eisenberg and his research group focus on protein interactions in amyloid and prion diseases. These diseases involve protein aggregation where normal functional proteins convert to abnormal aggregated forms. Systemic amyloid diseases like dialysis-related amyloidosis result from fiber accumulation until organ failure, while neurodegenerative diseases like Alzheimer's, Parkinson's, ALS, and prion conditions appear to be caused by smaller oligomers. In 2005, his team determined the atomic-level structure for the amyloid fiber spine, revealing a 'steric zipper' of two parallel beta sheets packed across a dry interface. Since then, they've determined approximately 90 amyloid spines from 15 disease-related proteins. In 2010, they identified the structure of a toxic amyloid-related oligomer consisting of six anti-parallel beta strands forming a cylindrical barrel. His recent publications demonstrate continued innovation in amyloid research, with focus areas including structural prediction of amyloid formation, mechanisms of tau fibril disassembly in Alzheimer's disease, cryo-EM analysis of amyloid polymorphism, and structure-based design of inhibitors for amyloid toxicity. His work integrates computational, structural, and biochemical approaches to understand protein aggregation across multiple disease contexts. Dr. Eisenberg has received numerous prestigious awards and honors: National Academy of Sciences Member American Philosophical Society Member Institute of Medicine Member Howard Hughes Medical Institute Investigator Biophysical Society Emily M. Gray Award Harvard Westheimer Medal UCLA Seaborg Medal Technion - Israel Institute of Technology Harvey Prize in Human Health As Director of the UCLA-DOE Institute for Genomics and Proteomics and an HHMI Investigator, Dr. Eisenberg leads significant research initiatives in protein structure and aggregation. His laboratory combines X-ray crystallography, bioinformatics, and biochemical techniques to investigate protein interactions, with particular emphasis on amyloid-forming proteins and their role in disease. The Eisenberg Lab, located in Boyer Hall at UCLA, maintains an active research program investigating the structural basis of protein aggregation. The lab continues to build on its landmark discoveries of amyloid structures while exploring new frontiers in understanding protein misfolding diseases and developing potential therapeutic interventions.

Roberta Sinatraمشاهده پروفایل

استاد

• Computational Social Science
• Network Science
• Data Science
• +۳ مورد دیگر

Roberta Sinatra is a Professor in Social Data Science at the University of Copenhagen, with part-time affiliations at ITU Copenhagen, ISI Foundation (Italy), and CSH (Austria). She co-founded the NERDS Research Group at ITU and co-leads the Pioneer Centre for AI in Copenhagen. Research Interests: Her work spans computational social science, network science, and data science, focusing on fairness in AI, scientific careers, and human mobility. Recent projects include analyzing child protection algorithms and modeling urban bicycle networks. Scientific Awards: ERC Consolidator Grant Villum Young Investigator Grant Complex Systems Society Junior Prize DPG Young Scientist Award for Socio- and Econophysics Sapere Aude: Starting Grant Publications: Her research, often in top-tier venues like Nature and Science , explores interdisciplinary themes, including AI ethics, gender disparities in science, and social network dynamics. Labs & Teams: She leads research initiatives at the Center for Social Data Science (KU) and co-founded the NERDS Research Group at ITU, fostering international collaboration in network science and AI ethics.

Waldemar Kolanusمشاهده پروفایل

استاد

• Molecular Immunology
• Cell Signaling
• Signal Transduction Pathways
• +۴ مورد دیگر

Prof. Waldemar Kolanus leads the Molecular Immunology and Cell Biology department at the University of Bonn's Life & Medical Sciences Institute (LIMES) . His research bridges immunoregulation , stem cell dynamics , and metabolic stress responses in immune cells. Unit 2 member at LIMES Principal investigator in SFB 704 and ImmunoSensation Cluster Leads a multidisciplinary lab with postdocs, PhD students, and technical staff His work focuses on intracellular signaling pathways connecting immune activation to tissue homeostasis, particularly through: Cytohesin proteins in integrin-mediated adhesion and migration TRIM71 in stem cell regulation and congenital hydrocephalus High-salt environments affecting macrophage function Publication trends show expertise in immune cell migration , genetic models , and chemical inhibition , with frequent use of mice and zebrafish for in vivo studies. Key articles explore: TRIM71's dual role in auditory development and germ cell maintenance Cytohesin family's Golgi regulation and insulin signaling Ruxolitinib's off-target migration inhibition of dendritic cells Contact details: Address: LIMES Institute, Carl-Troll-Straße 31, Bonn Email: kolanus.sekretariat@uni-bonn.de Phone: +49 228 73-62788

Amit R. Reddiمشاهده پروفایل

استاد

• Biochemistry
• Metalloproteins in biological regulation and disease
• Heme trafficking and signaling
• +۴ مورد دیگر

Amit R. Reddi is a Professor at the Department of Chemistry, Georgia Institute of Technology. His research focuses on metalloproteins, particularly the mechanisms of heme trafficking and redox signaling in relation to cancer, neurodegenerative disorders, and infectious diseases. He has received numerous awards for both research and teaching excellence. Education : B.A. from Carleton College (2003) Ph.D. from Columbia University (2008) NIH Postdoctoral Fellowship at Johns Hopkins University (2013) Research Interests : The Reddi laboratory investigates cellular mechanisms of metalloprotein activation and inter-biomolecular communication in metabolic and signaling pathways critical to human health. Key projects explore heme trafficking pathways and the role of Cu/Zn Superoxide Dismutase (SOD1) in redox signaling, with implications for cancer, neurodegenerative diseases, and microbial pathogenesis. Scientific Awards : Vasser Woolley Faculty Fellowship (2021) Student Recognition of Excellence in Teaching Class of 1934 Award (2021) CTL/BP Junior Faculty Excellence in Teaching Award (2019) Bergmann Memorial Award (2018) Blanchard Professorship (2016) NSF CAREER Award (2015) NIH NRSA Post-doctoral Fellowship (2008-2011) Grants & Fellowships : NSF CAREER Award (2015) Sigma Xi Grants-In-Aid-of-Research (2003) NIH Cancer Research Training Award Fellowship (1999-2001)

Kathrin Langمشاهده پروفایل

استاد

• Chemical Biology
• Protein Engineering
• Genetic Code Expansion
• +۳ مورد دیگر

Kathrin Lang is a Full Professor at the Department of Chemistry and Applied Biosciences, ETH Zurich, and Head of the Organic Chemistry Laboratory. Her research focuses on chemical biology, particularly the development of tools for genetic code expansion to incorporate non-canonical amino acids into proteins and advance bioorthogonal chemistries for studying biological processes. Keywords: Genetic Code Expansion, Bioorthogonal Chemistry, Protein Engineering, Ubiquitylation Networks, Post-Translational Modifications. Lang’s work emphasizes proximity-triggered crosslinking reactions, bioorthogonal labeling, and in vivo chemistries to address challenges in protein interaction mapping and structural elucidation. Her group’s recent publications highlight methodologies for dual protein labeling, deciphering ubiquitin code, and enhancing cycloaddition reactivity. Current projects include exploring cyclopropene-fused dibenzocyclooctynes for improved labeling and investigating methylated lysine as a conformational regulator in Hsp90. Funding sources include the ERC (Ubl-tool), DFG (SFB1035, SPP1926), and ETH Zurich. She contributes to education through courses like Genetic Code Expansion for Studying Posttranslational Modifications and Chemical Biology and Synthetic Biochemistry . Collaborative efforts span structural biology, microbiology, and synthetic biochemistry, with applications in ubiquitin research and cellular imaging.

Donald Rioمشاهده پروفایل

استاد

• Nucleic Acid Transactions
• Transposable Elements
• RNA Binding Proteins
• +۳ مورد دیگر

Donald Rio holds the Richard and Rhoda Goldman Distinguished Chair in the Biological Sciences and is a Professor of Biochemistry, Biophysics, and Structural Biology. He is affiliated with the Division of Biochemistry and Molecular Biology and the Center for Integrative Genetics. His lab focuses on nucleic acid transactions, including transposable element mobilization (P elements) and RNA binding protein mechanisms controlling alternative splicing. Research highlights include studies on THAP9 proteins in humans/zebrafish, cryo-EM structural analysis of transposase-DNA complexes, and splicing regulation in neurodegenerative diseases like ALS and Parkinson’s. His work combines biochemical, genetic, and computational approaches, including the development of the Junction Usage Model (JUM) for splicing analysis. Research interests span transposition mechanisms linked to HIV integration, immune system recombination, and evolutionary genome dynamics. His team investigates how RNA binding proteins like hnRNPA1 influence splicing in disease contexts, with projects involving CRISPR-based models and patient RNA-seq data analysis. Collaborations include studies on splicing accuracy across tissues and age, and the impact of splicing defects in neurodegenerative disorders. Key awards include the Goldman Chair. His lab’s contributions bridge fundamental molecular mechanisms with translational applications in genetic disease modeling and drug discovery. Recent work focuses on isogenic stem cell models (iSCORE-PD) for Parkinson’s research and structural biology insights into transposase function. Grants and projects involve NIH funding for ALS splicing studies and collaborations with institutions like the Buck Institute. His lab actively publishes in top journals such as Genome Research , PNAS , and Nature , with a strong emphasis on cryo-EM and bioinformatic methods.

Katherine J. Franzمشاهده پروفایل

استاد

• Bioinorganic Chemistry
• Metal Homeostasis
• Antimicrobial Agents
• +۴ مورد دیگر

Katherine J. Franz is a Professor of Chemistry at Duke University, affiliated with the Trinity College of Arts & Sciences and the Duke Cancer Institute. She holds a Ph.D. from MIT (2000) and a B.A. from Wellesley College (1995). Her research focuses on bioinorganic chemistry, particularly metal ion coordination in biological systems, with applications in antimicrobial therapies, cancer metallomics, and neurodegenerative diseases. Key projects include developing prochelators targeting fungal and bacterial pathogens, studying copper's role in antifungal drug efficacy, and designing light-activated metal complexes for controlled drug release. Dr. Franz has received numerous awards including the Camille Dreyfus Teacher-Scholar Award (2009), Sloan Research Fellowship (2008), and the NSF CAREER Award (2005). She leads a lab with 6 current students/mentees and has secured grants from NIH, NSF, and the US-Israel Binational Science Foundation. Her lab's work spans from fundamental metalloprotein studies to translational drug development, emphasizing interdisciplinary approaches in chemistry and biology. Education: Ph.D. in Chemistry, MIT, 2000 B.A. in Chemistry, Wellesley College, 1995 Research Interests: Metal homeostasis in pathogens, copper's role in antifungal resistance, prodrug design for targeted therapy, and mechanistic studies of metalloproteins. Grants: Tri-Institutional Molecular Mycology Training Program (NIH, 2024–2029) Duke PREP Biomedical Sciences Program (NIGMS, 2022–2027) Copper-Mucin Interaction Study (BSF, 2022–2026) Her lab's publications (n=15+ since 2020) highlight breakthroughs in prodrug selectivity, copper-induced protein toxicity, and histatin antifungal mechanisms. The Franz Lab actively collaborates with clinicians and computational scientists to advance therapeutic strategies addressing unmet medical needs in infectious diseases and cancer.

James Shorterمشاهده پروفایل

استاد

• Protein Folding and Proteostasis
• Neurodegenerative Diseases
• Prion and Amyloid Biology
• +۷ مورد دیگر

James Shorter is a Professor of Biochemistry and Biophysics at the Perelman School of Medicine, University of Pennsylvania. He is affiliated with multiple prestigious institutes, including the Institute on Aging (IOA), the Institute for Translational Medicine and Therapeutics (ITMAT), the Penn Center for AIDS Research (CFAR), the Chemistry-Biology Interface (CBI), and the Penn Institute for RNA Innovation. He mentors several training programs such as the Penn Summer Undergraduate Internship Program (SUIP), PennPREP, and the Translational Research Immersion Program (TRIP), and serves as a Primary Trainer at the Center for Neurodegenerative Research (CNDR). Ph.D. in Cell Biology, University of London, 2000 M.A. in Biology, University of Oxford, 1995 Dr. Shorter’s research focuses on protein homeostasis, particularly the mechanisms of protein disaggregation and the role of prion-like domains in neurodegenerative diseases such as ALS, Alzheimer’s, Parkinson’s, and frontotemporal lobar degeneration. His lab investigates the Hsp104 disaggregase from yeast and has engineered variants to combat human proteinopathies. They also identified the mammalian disaggregase system (Hsp110/Hsp70/Hsp40) and explore how small molecules and nuclear import receptors can reverse pathological phase transitions of RNA-binding proteins like TDP-43 and FUS. His work bridges structural biology, genetics, and translational neuroscience. His recent publications highlight trends in targeting TDP-43 and FUS proteinopathies, engineering Hsp104 for selective detoxification, understanding mitochondrial disaggregases like Skd3, and modulating phase transitions with nuclear import receptors. His research spans from fundamental mechanisms of protein folding to therapeutic development for neurodegenerative diseases. Faculty Member, Institute on Aging (IOA) Faculty Member, Institute for Translational Medicine and Therapeutics (ITMAT) Mentor, Penn Summer Undergraduate Internship Program (SUIP) Primary Trainer, Center for Neurodegenerative Research (CNDR) Faculty Member, Penn Center for AIDS Research (CFAR) Member, Penn Institute for RNA Innovation Mentor, Translational Research Immersion Program (TRIP) Dr. Shorter advises numerous graduate students and postdoctoral researchers through the Biochemistry and Molecular Biophysics, Pharmacology, Neuroscience, and Cell and Molecular Biology graduate groups. His lab receives funding from NIH and other sources to support research on protein disaggregation, phase separation, and neurodegenerative disease mechanisms. He has trained many scientists now active in academia and biotech. His lab, located in Stellar-Chance Laboratories, operates at the intersection of biochemistry, cell biology, and translational medicine, with active projects on Hsp104 engineering, mitochondrial proteostasis, and the role of RNA-binding proteins in disease. The lab collaborates widely across Penn and with international partners to advance understanding and treatment of protein misfolding disorders.

Alexander J. Harteminkمشاهده پروفایل

استاد

• Computational Biology
• Machine Learning
• Genomics
• +۵ مورد دیگر

Professor Alexander J. Hartemink holds dual appointments in the Department of Computer Science and Department of Biology at Duke University, Trinity College of Arts & Sciences. He is also a Bass Fellow in Computer Science. His research focuses on computational biology, machine learning, and systems biology, with applications to genomics, epigenomics, and transcriptional regulation. Hartemink leads the Duke Office of University Scholars and Fellows and has directed the Computational Biology and Bioinformatics graduate program. He earned a PhD from MIT (2001), MPhil from the University of Oxford (1996), and BS from Duke (1994). Research Interests His work integrates computational methods to study chromatin dynamics, transcriptional networks, and epigenetic mechanisms. Key areas include modeling chromatin accessibility, predicting transcription factor binding, and understanding cell-cycle regulation. Techniques employed include Bayesian networks, dynamic systems modeling, and machine learning algorithms. Publications & Trends Recent work emphasizes single-cell multi-omics integration, chromatin occupancy modeling (RoboCOP framework), and transcriptional regulation in response to genetic perturbations. Themes include epigenetic plasticity, disease-associated enhancers, and systems-level analysis of gene expression. Awards & Grants Hartemink has received the Sloan Research Fellowship (2005) and NSF CAREER Award (2004). Active grants include NIH funding for chromatin-transcription interplay studies and NSF support for regulatory genome research. He collaborates on projects like the Data+ initiative, promoting interdisciplinary data science. Affiliations & Labs Associated with Duke’s Center for Genomic and Computational Biology and Center for Advanced Genomic Technologies. His lab develops computational tools for genomic analysis, including software for chromatin modeling and epigenetic data integration.

• Neurodegenerative Diseases
• Motor Neuron Disease (MND)
• Frontotemporal Dementia (FTD)
• +۷ مورد دیگر

Dr. Rebecca San Gil is a Lecturer at the School of Medical Sciences , University of Sydney, Australia. She leads the NeuroMolecular Discovery Group within the Neuroscience theme and is a member of the Charles Perkins Centre . Her research focuses on the molecular mechanisms underlying neurodegenerative diseases such as motor neuron disease (MND) and frontotemporal dementia (FTD) , with an emphasis on protein aggregation, stress responses, and therapeutic discovery. PhD, University of Wollongong (2018) Postdoctoral Research, Queensland Brain Institute (2018–2025) Endeavour Research Fellow (University College London) Her research spans molecular biology , neurosciences , and biochemistry , integrating techniques like genome-wide CRISPR screening , multi-omics analysis , and translational research . Key themes include the role of molecular chaperones , heat shock response , and protein folding dynamics in mitigating neurodegeneration. Dr. San Gil’s recent publications (2016–2025) highlight her work on TDP-43 pathology , heat shock proteins , and therapeutic strategies across ALS/FTD models. She has received awards such as the FightMND Early Career Research Fellow and the Sydney Dementia Network Future Research Leader Award (Travel Support Scheme) in 2025. Scientific Awards : FightMND Early Career Research Fellow, Sydney Dementia Network Future Research Leader Award (2025) Dr. San Gil actively mentors researchers like Celine CHYE and collaborates with institutions globally. Her team welcomes new members to explore neurodegenerative disease biology and therapeutic discovery .

Katherine Rushمشاهده پروفایل

استادیار

• Biochemistry
• Metalloenzymology
• Bioinorganic Chemistry
• +۵ مورد دیگر

Katherine Rush is an Assistant Professor in the Department of Chemistry and Biochemistry at Auburn University. Her research focuses on metalloenzyme catalysis, bioinorganic chemistry, and X-ray spectroscopic techniques. She has held academic positions including Visiting Assistant Professor at Reed College (2020–2022) and Postdoctoral Fellow at Oregon Health and Science University (2018–2023). She earned a Ph.D. in Chemical Biology from the University of Michigan (2013–2018) and a B.S. in Chemistry from the University of Tennessee (2010–2013). Research Interests: Rush’s laboratory investigates the molecular mechanisms of metalloenzymes involved in thyroid hormone regulation, oxygen activation, and antimicrobial natural product biosynthesis. A key focus is selenium-containing amino acids as tools for element-specific spectroscopic characterization. Techniques employed include X-ray absorption spectroscopy (XAS), biochemical assays (SDS-PAGE, Western blotting), and analytical methods (ICP-OES, LC-MS). Teaching: She instructs BCHE 7270 – Biochemical Research Techniques, emphasizing hands-on experience with advanced biochemical methodologies. Grants & Advising: While specific grants are not listed, her research reflects significant interdisciplinary collaboration in environmental and biomedical chemistry. No current advisees are explicitly noted. Labs/Teams: The Rush Lab at Auburn University specializes in integrating spectroscopic and biochemical approaches to study metalloenzymes, particularly targeting systems relevant to human health such as copper-dependent monooxygenases and selenium-labeled proteins.

Silvia Cavagneroمشاهده پروفایل

استاد

• Protein Folding
• Biomolecular Spectroscopy
• Neurodegenerative Diseases
• +۴ مورد دیگر

Silvia Cavagnero is a Professor in the Department of Chemistry at the University of Wisconsin–Madison, with a research focus on protein folding and misfolding in cellular contexts. Her work integrates biomolecular spectroscopy, chemical biology, and computational methods to address fundamental questions in structural biology. B.S., First University of Rome ‘La Sapienza’ (1988) M.S., University of Arizona (1990) Ph.D., California Institute of Technology (1996) Her research explores the role of molecular chaperones like Hsp70 in protein biogenesis, the development of laser-driven NMR techniques for enhanced sensitivity, and the implications of protein aggregation in neurodegenerative diseases. Key projects include cotranslational folding studies at ribosomal exit tunnels and hyperpolarization methods for low-concentration NMR analysis. The 15 most recent publications highlight interdisciplinary advances in NMR spectroscopy optimization Protein folding kinetics Cryo-EM structural analysis Chaperone-client interactions Hsp70 antimicrobial design Hydration dynamics in folding Scientific contributions include A Prize for Going in Vivo (2017) Recognition for Diversity and Inclusion Efforts Students from the Cavagnero Group have pursued careers in academia, pharmaceutical industries, and national laboratories. Her lab emphasizes interdisciplinary training, blending physical chemistry, biology, and computational analysis.

Peter Chienمشاهده پروفایل

استاد مدعو

• Regulated Proteolysis
• Protein Quality Control
• Bacterial Cell Cycle Regulation
• +۴ مورد دیگر

Peter Chien is an Adjunct Professor in the Department of Biochemistry and Molecular Biology at the University of Massachusetts Amherst. His research focuses on regulated protein degradation and quality control in bacteria, with a particular emphasis on mechanisms governing proteolysis during the bacterial cell cycle. PhD, University of California, San Francisco Postdoctoral Training, Massachusetts Institute of Technology The Chien Lab employs interdisciplinary approaches including biochemistry, structural biology, and cell biology to study proteolytic mechanisms in Caulobacter crescentus. Their work explores how AAA+ proteases like ClpXP and Lon recognize substrates with precision and how this impacts cellular regulatory networks. Recent research trends from the lab include investigations into Lon protease modulation , DNA damage responses , protein homeostasis under stress , and genetic regulators of proteostasis . Studies often integrate structural analysis with functional assays to uncover molecular principles of protease specificity. The lab is affiliated with multiple graduate programs, including the Molecular and Cellular Biology (MCB) program, Chemistry-Biology Interface Program, Biotechnology Training Program, and the Institute for Applied Life Sciences at UMass Amherst.