Kate Carroll

Kate Carroll, Ph.D.

Professor

Department: SR-CHEM-CARROLL LAB
Business Phone: (561) 228-2460
Business Email: kate.carroll@ufl.edu

About Kate Carroll

Kate S Carroll is an Associate Professor with Tenure in the Department of Chemistry at The Scripps Research Institute in Jupiter, Florida. She received her BA degree in Biochemistry from Mills College in 1996 and PhD in Biochemistry from Stanford University in 2003. Her postdoctoral work was completed at the University of California, Berkeley, where she was a Damon Runyon-Walter Winchell Chancer Fund Fellow with Prof. Carolyn Bertozzi. She was an assistant professor at the University of Michigan until 2010, when she joined the Chemistry faculty at Scripps. Her research interests span the disciplines of chemistry and biology with an emphasis on studies of sulfur biochemistry pertinent to disease states. Her lab focuses on the development of novel tools to study redox modifications of cysteine thiols, profiling changes in protein oxidation associated with disease, and exploiting this information for development of diagnostic and therapeutic approaches. In addition, her group investigates sulfur pathways that are essential for infection and long-term survival of human pathogens such as Mycobacterium tuberculosis. Dr. Carroll currently serves on the editorial board of Cell Chemical Biology, Molecular Biosystems, Journal of Biology Chemistry, and is a contributing member of ‘Faculty of 1000’. She is also the recipient of the ACS Pfizer Award in Enzyme Chemistry (2013), Camille Dreyfus Teacher-Scholar Award (2010), Scientist Development Award from American Heart Association (2008), and Special Fellow Award from the Leukemia and Lymphoma Society (2006).

Additional Positions:
Associate Professor of Chemistry
2010 – 2013 · Scripps Research
Assistant Professor of Chemistry
2006 – 2010 · University of Michigan
Damon Runyon Postdoctoral Fellow with Dr. Carolyn Bertozzi
2003 – 2006 · University of California, Berkeley

Accomplishments

Recipient
2013 · ACS Pfizer Award in Enzyme Chemistry
Awarded
2010 · Camille Dreyfus Teacher-Scholar Award
Scientist Development Award
2008 · American Heart Association
Special Fellow Award
2006 · Leukemia and Lymphoma Society

Research Profile

The Carroll lab has an proven track record of attacking fundamental problems in redox biology through a powerful, interdisciplinary approach that integrates synthetic chemistry with proteomics, biochemistry, and cell biology.

An overarching goal of our research program is to understand the biological chemistry and molecular mechanisms of redox-based cellular regulation and signal transduction, with particular emphasis on the role of cysteine oxidation, a ubiquitous and conserved mechanism for controlling protein function. We are also exploring the therapeutic potential of redox-regulated protein function by developing an entirely new class of inhibitors that targets oxidized cysteine residues of key proteins involved in human disease, such as kinases and phosphatases. We also investigate sulfur metabolic pathways that are essential for infection and long-term survival of human pathogens, such as Mycobacterium tuberculosis and leverage novel discoveries to develop new antimicrobial therapies.

Ultimately, our goal is to accelerate the discovery of key regulatory nodes of redox-signaling networks, profile changes in protein cysteine oxidation associated with disease, and harness this information for the development of new diagnostic and therapeutic approaches.

Students in the lab receive broad-based training in experimental techniques ranging from synthetic chemistry and mass spectrometry to cellular and in vivo animal studies. Representative skill sets and expertise in the group are given below, and students are encouraged to take multiple apporaches to ask and answer new scientific questions.

— Chemical tool development: Synthetic chemistry with analytical characterization — Cell culture: Mammalian cell lines, bacteria, and primary cultures — Proteomics: Solid-phase capture, fractionation, LC-MS/MS, bioinformatics — Molecular imaging: Confocal microscopy and flow cytometry — Gene discovery: Activity-based protein profiling — Animal studies: Mouse physiology — Molecular biology: Cloning, transfections, RNAi, PCR, and CRISPR — In vitro biochemistry: Protein preparation, purification, and protein engineering

Open Researcher and Contributor ID (ORCID)

0000-0002-7624-9617

Publications

2022
An increase in surface hydrophobicity mediates chaperone activity in N-chlorinated RidA.
Redox biology. [DOI] 10.1016/j.redox.2022.102332. [PMID] 35598378.
2022
Natural Products in Redox Toxicology
Chemical Research in Toxicology. [DOI] 10.1021/acs.chemrestox.2c00184.
2022
Thiol-based chemical probes exhibit antiviral activity against SARS-CoV-2 via allosteric disulfide disruption in the spike glycoprotein
Proceedings of the National Academy of Sciences. [DOI] 10.1073/pnas.2120419119. [PMID] 35074895.
2021
Comments on ‘A critical evaluation of probes for cysteine sulfenic acid’.
Current opinion in chemical biology. [DOI] 10.1016/j.cbpa.2021.01.004. [PMID] 33610081.
2021
Crystal Structure of the [4Fe–4S] Cluster-Containing Adenosine-5′-phosphosulfate Reductase from Mycobacterium tuberculosis
ACS Omega. [DOI] 10.1021/acsomega.1c01043. [PMID] 34095667.
2021
Endogenous SO2-dependent Smad3 redox modification controls vascular remodeling.
Redox biology. [DOI] 10.1016/j.redox.2021.101898. [PMID] 33647858.
2021
Global profiling of distinct cysteine redox forms reveals wide-ranging redox regulation in C. elegans
Nature Communications. [DOI] 10.1038/s41467-021-21686-3. [PMID] 33658510.
2021
Parallel evaluation of nucleophilic and electrophilic chemical probes for sulfenic acid: Reactivity, selectivity and biocompatibility
Redox Biology. [DOI] 10.1016/j.redox.2021.102072. [PMID] 34298464.
2021
Wittig reagents for chemoselective sulfenic acid ligation enables global site stoichiometry analysis and redox-controlled mitochondrial targeting
Nature Chemistry. [DOI] 10.1038/s41557-021-00767-2. [PMID] 34531572.
2020
Activity-Based Sensing for Site-Specific Proteomic Analysis of Cysteine Oxidation
Accounts of Chemical Research. [DOI] 10.1021/acs.accounts.9b00562. [PMID] 31869209.
2020
Call for Papers for the Special Issue on Natural Products in Redox Toxicology
Chemical Research in Toxicology. [DOI] 10.1021/acs.chemrestox.0c00421.
2020
Cysteine sulfenylation by CD36 signaling promotes arterial thrombosis in dyslipidemia
Blood Advances. [DOI] 10.1182/bloodadvances.2020001609. [PMID] 32946569.
2020
Selective Persulfide Detection Reveals Evolutionarily Conserved Antiaging Effects of S-Sulfhydration.
Cell metabolism. [DOI] 10.1016/j.cmet.2019.12.001. [PMID] 31914376.
2019
Diurnal oscillations of endogenous H2O2 sustained by p66Shc regulate circadian clocks
Nature Cell Biology. [DOI] 10.1038/s41556-019-0420-4. [PMID] 31768048.
2019
Mining for protein S-sulfenylation in Arabidopsis uncovers redox-sensitive sites.
Proceedings of the National Academy of Sciences of the United States of America. [DOI] 10.1073/pnas.1906768116. [PMID] 31578252.
2019
Proteome-Wide Analysis of Cysteine S-Sulfenylation Using a Benzothiazine-Based Probe.
Current protocols in protein science. [DOI] 10.1002/cpps.76. [PMID] 30312022.
2019
Redox Pathways in Chemical Toxicology
Chemical Research in Toxicology. [DOI] 10.1021/acs.chemrestox.9b00084.
2019
Selective Persulfide Detection Reveals Evolutionarily Conserved Antiaging Effects of S-Sulfhydration.
Cell metabolism. [DOI] 10.1016/j.cmet.2019.10.007. [PMID] 31735592.
2018
Chemical and Biochemical Mechanisms of Redox-Mediated Toxicology
Chemical Research in Toxicology. [DOI] 10.1021/acs.chemrestox.8b00157.
2018
Chemical proteomics reveals new targets of cysteine sulfinic acid reductase
Nature Chemical Biology. [DOI] 10.1038/s41589-018-0116-2. [PMID] 30177848.
2018
Muc5b overexpression causes mucociliary dysfunction and enhances lung fibrosis in mice.
Nature communications. [DOI] 10.1038/s41467-018-07768-9. [PMID] 30560893.
2017
Diverse Redoxome Reactivity Profiles of Carbon Nucleophiles
Journal of the American Chemical Society. [DOI] 10.1021/jacs.7b01791. [PMID] 28355876.
2016
An immunochemical approach to detect oxidized protein tyrosine phosphatases using a selective C-nucleophile tag.
Molecular bioSystems. [DOI] 10.1039/c5mb00847f. [PMID] 26757830.
2016
First-in-Class Inhibitors of Sulfur Metabolism with Bactericidal Activity against Non-Replicating M. tuberculosis.
ACS chemical biology. [DOI] 10.1021/acschembio.5b00517. [PMID] 26524379.
2016
Functional Site Discovery in a Sulfur Metabolism Enzyme by Using Directed Evolution.
Chembiochem : a European journal of chemical biology. [DOI] 10.1002/cbic.201600264. [PMID] 27411165.
2016
Molecular Basis for Redox Activation of Epidermal Growth Factor Receptor Kinase.
Cell chemical biology. [DOI] 10.1016/j.chembiol.2016.05.017. [PMID] 27427230.
2016
Profiling the Reactivity of Cyclic C-Nucleophiles towards Electrophilic Sulfur in Cysteine Sulfenic Acid.
Chemical science. [PMID] 26819701.
2016
Rational design of reversible and irreversible cysteine sulfenic acid-targeted linear C-nucleophiles.
Chemical communications (Cambridge, England). [DOI] 10.1039/c6cc00228e. [PMID] 26878905.
2016
Reactivity, Selectivity, and Stability in Sulfenic Acid Detection: A Comparative Study of Nucleophilic and Electrophilic Probes.
Bioconjugate chemistry. [DOI] 10.1021/acs.bioconjchem.6b00181. [PMID] 27123991.
2016
The Expanding Landscape of the Thiol Redox Proteome.
Molecular & cellular proteomics : MCP. [DOI] 10.1074/mcp.O115.056051. [PMID] 26518762.
2015
A Chemical Approach for the Detection of Protein Sulfinylation.
ACS chemical biology. [DOI] 10.1021/acschembio.5b00124. [PMID] 26039147.
2015
A universal entropy-driven mechanism for thioredoxin-target recognition.
Proceedings of the National Academy of Sciences of the United States of America. [DOI] 10.1073/pnas.1504376112. [PMID] 26080424.
2015
Chemical approaches to discovery and study of sources and targets of hydrogen peroxide redox signaling through NADPH oxidase proteins.
Annual review of biochemistry. [DOI] 10.1146/annurev-biochem-060614-034018. [PMID] 26034893.
2015
Design, synthesis and evaluation of Fe-S targeted adenosine 5′-phosphosulfate reductase inhibitors.
Nucleosides, nucleotides & nucleic acids. [DOI] 10.1080/15257770.2014.978012. [PMID] 25710356.
2015
DYn-2 Based Identification of Arabidopsis Sulfenomes.
Molecular & cellular proteomics : MCP. [DOI] 10.1074/mcp.M114.046896. [PMID] 25693797.
2015
Global, in situ, site-specific analysis of protein S-sulfenylation.
Nature protocols. [DOI] 10.1038/nprot.2015.062. [PMID] 26086405.
2015
Light-Mediated Sulfenic Acid Generation from Photocaged Cysteine Sulfoxide.
Organic letters. [DOI] 10.1021/acs.orglett.5b02981. [PMID] 26641493.
2015
Site-Specific Proteomic Mapping Identifies Selectively Modified Regulatory Cysteine Residues in Functionally Distinct Protein Networks.
Chemistry & biology. [DOI] 10.1016/j.chembiol.2015.06.010. [PMID] 26165157.
2014
Chemical biology approaches to study protein cysteine sulfenylation.
Biopolymers. [DOI] 10.1002/bip.22255. [PMID] 23576224.
2014
Detection of protein S-sulfhydration by a tag-switch technique.
Angewandte Chemie (International ed. in English). [DOI] 10.1002/anie.201305876. [PMID] 24288186.
2014
Proteomic analysis of peptides tagged with dimedone and related probes.
Journal of mass spectrometry : JMS. [DOI] 10.1002/jms.3336. [PMID] 24719340.
2014
Redox-based probes as tools to monitor oxidized protein tyrosine phosphatases in living cells.
European journal of medicinal chemistry. [DOI] 10.1016/j.ejmech.2014.06.040. [PMID] 24974258.
2014
Site-specific mapping and quantification of protein S-sulphenylation in cells.
Nature communications. [DOI] 10.1038/ncomms5776. [PMID] 25175731.
2014
Sulfenic acid chemistry, detection and cellular lifetime.
Biochimica et biophysica acta. [DOI] 10.1016/j.bbagen.2013.05.040. [PMID] 23748139.
2013
A continuous spectrophotometric assay for adenosine 5′-phosphosulfate reductase activity with sulfite-selective probes.
Analytical biochemistry. [DOI] 10.1016/j.ab.2013.05.007. [PMID] 23711725.
2013
Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery.
Chemical reviews. [DOI] 10.1021/cr300163e. [PMID] 23514336.
2013
Efficient microwave-assisted solid phase coupling of nucleosides, small library generation and mild conditions for release of nucleoside derivatives.
Tetrahedron letters. [PMID] 23794759.
2013
New targets and inhibitors of mycobacterial sulfur metabolism.
Infectious disorders drug targets. [PMID] 23808874.
2013
Persulfide reactivity in the detection of protein s-sulfhydration.
ACS chemical biology. [DOI] 10.1021/cb4001052. [PMID] 23557648.
2013
Redox regulation of protein kinases.
Critical reviews in biochemistry and molecular biology. [DOI] 10.3109/10409238.2013.790873. [PMID] 23639002.
2013
RegB kinase activity is repressed by oxidative formation of cysteine sulfenic acid.
The Journal of biological chemistry. [DOI] 10.1074/jbc.M112.413492. [PMID] 23306201.
2013
Regulation of A20 and other OTU deubiquitinases by reversible oxidation.
Nature communications. [DOI] 10.1038/ncomms2567. [PMID] 23463012.
2013
The redox biochemistry of protein sulfenylation and sulfinylation.
The Journal of biological chemistry. [DOI] 10.1074/jbc.R113.467738. [PMID] 23861405.
2012
Activity of the tetrapyrrole regulator CrtJ is controlled by oxidation of a redox active cysteine located in the DNA binding domain.
Molecular microbiology. [DOI] 10.1111/j.1365-2958.2012.08135.x. [PMID] 22715852.
2012
Chemoselective ligation of sulfinic acids with aryl-nitroso compounds.
Angewandte Chemie (International ed. in English). [DOI] 10.1002/anie.201201812. [PMID] 22644884.
2012
Inactivation of thiol-dependent enzymes by hypothiocyanous acid: role of sulfenyl thiocyanate and sulfenic acid intermediates.
Free radical biology & medicine. [DOI] 10.1016/j.freeradbiomed.2011.12.024. [PMID] 22248862.
2012
Redox regulation of epidermal growth factor receptor signaling through cysteine oxidation.
Biochemistry. [DOI] 10.1021/bi301441e. [PMID] 23186290.
2012
Redox-sensitive sulfenic acid modification regulates surface expression of the cardiovascular voltage-gated potassium channel Kv1.5.
Circulation research. [DOI] 10.1161/CIRCRESAHA.111.263525. [PMID] 22843785.
2011
Chemical ‘omics’ approaches for understanding protein cysteine oxidation in biology.
Current opinion in chemical biology. [DOI] 10.1016/j.cbpa.2010.11.012. [PMID] 21130680.
2011
Deciphering the role of histidine 252 in mycobacterial adenosine 5′-phosphosulfate (APS) reductase catalysis.
The Journal of biological chemistry. [DOI] 10.1074/jbc.M111.238998. [PMID] 21673113.
2011
Geometric and electrostatic study of the [4Fe-4S] cluster of adenosine-5′-phosphosulfate reductase from broken symmetry density functional calculations and extended X-ray absorption fine structure spectroscopy.
Inorganic chemistry. [DOI] 10.1021/ic200446c. [PMID] 21678934.
2011
Isotope-coded chemical reporter and acid-cleavable affinity reagents for monitoring protein sulfenic acids.
Bioorganic & medicinal chemistry letters. [DOI] 10.1016/j.bmcl.2011.04.115. [PMID] 21601453.
2011
Metabolite imaging: knock, nox-ROS there?
Nature chemical biology. [DOI] 10.1038/nchembio.515. [PMID] 21245857.
2011
Peroxide-dependent sulfenylation of the EGFR catalytic site enhances kinase activity.
Nature chemical biology. [DOI] 10.1038/nchembio.736. [PMID] 22158416.
2011
Quantification of protein sulfenic acid modifications using isotope-coded dimedone and iododimedone.
Angewandte Chemie (International ed. in English). [DOI] 10.1002/anie.201007175. [PMID] 21290508.
2011
Redox-based probes for protein tyrosine phosphatases.
Angewandte Chemie (International ed. in English). [DOI] 10.1002/anie.201007871. [PMID] 21504031.
2011
Spectroscopic studies on the [4Fe-4S] cluster in adenosine 5′-phosphosulfate reductase from Mycobacterium tuberculosis.
The Journal of biological chemistry. [DOI] 10.1074/jbc.M110.193722. [PMID] 21075841.
2010
Orchestrating redox signaling networks through regulatory cysteine switches.
ACS chemical biology. [DOI] 10.1021/cb900258z. [PMID] 19957967.
2009
A periplasmic reducing system protects single cysteine residues from oxidation.
Science (New York, N.Y.). [DOI] 10.1126/science.1179557. [PMID] 19965429.
2009
Chemical dissection of an essential redox switch in yeast.
Chemistry & biology. [DOI] 10.1016/j.chembiol.2009.01.003. [PMID] 19230722.
2009
Identification of critical ligand binding determinants in Mycobacterium tuberculosis adenosine-5′-phosphosulfate reductase.
Journal of medicinal chemistry. [DOI] 10.1021/jm900728u. [PMID] 19678707.
2009
Mining the thiol proteome for sulfenic acid modifications reveals new targets for oxidation in cells.
ACS chemical biology. [DOI] 10.1021/cb900105q. [PMID] 19645509.
2009
Profiling protein thiol oxidation in tumor cells using sulfenic acid-specific antibodies.
Proceedings of the National Academy of Sciences of the United States of America. [DOI] 10.1073/pnas.0903015106. [PMID] 19805274.
2008
A chemical approach for detecting sulfenic acid-modified proteins in living cells.
Molecular bioSystems. [DOI] 10.1039/b719986d. [PMID] 18493649.
2008
Expanding the functional diversity of proteins through cysteine oxidation.
Current opinion in chemical biology. [DOI] 10.1016/j.cbpa.2008.07.028. [PMID] 18804173.
2008
Structure-based virtual screening and biological evaluation of Mycobacterium tuberculosis adenosine 5′-phosphosulfate reductase inhibitors.
Journal of medicinal chemistry. [DOI] 10.1021/jm800571m. [PMID] 18855373.
2007
3′-Phosphoadenosine-5′-phosphosulfate reductase in complex with thioredoxin: a structural snapshot in the catalytic cycle.
Biochemistry. [PMID] 17352498.
2006
Substrate recognition, protein dynamics, and iron-sulfur cluster in Pseudomonas aeruginosa adenosine 5′-phosphosulfate reductase.
Journal of molecular biology. [PMID] 17010373.
2005
A conserved mechanism for sulfonucleotide reduction.
PLoS biology. [PMID] 16008502.
2005
Investigation of the iron-sulfur cluster in Mycobacterium tuberculosis APS reductase: implications for substrate binding and catalysis.
Biochemistry. [PMID] 16262264.
An increase in surface hydrophobicity mediates chaperone activity in N-chlorinated proteins
. [DOI] 10.1101/2021.10.26.465855.
Defining and refining the cysteine redoxome with sulfur chemical biology
. [DOI] 10.26434/chemrxiv-2022-pmk47.
Nucleophilic covalent ligand discovery for the cysteine redoxome
. [DOI] 10.26434/chemrxiv-2022-1gmkp.
Nucleophilic covalent ligand discovery for the cysteine redoxome
. [DOI] 10.21203/rs.3.rs-1765196/v1.
Parallel Evaluation of Nucleophilic and Electrophilic Chemical Probes for Sulfenic Acid: Reactivity, Selectivity and Biocompatibility
. [DOI] 10.1101/2021.06.23.449646.
Reaction-based fluorogenic probes for selective detection of cysteinyl oxidation in living cells
. [DOI] 10.21203/rs.3.rs-956877/v1.
Thiol-based mucolytics exhibit antiviral activity against SARS-CoV-2 through allosteric disulfide disruption in the spike glycoprotein
. [DOI] 10.1101/2021.07.01.450701.
Wittig reagents for chemoselective sulfenic acid ligation enables global site stoichiometry analysis and redox-controlled mitochondrial targeting
. [DOI] 10.21203/rs.3.rs-110280/v1.

Grants

Apr 2022 ACTIVE
Chemistry and Biology of Bacterial Sulfonucleotide Reductases
Role: Principal Investigator
Funding: NATL INST OF HLTH NIGMS
Apr 2022 ACTIVE
Redox Modification and Targeting of Mutant KRas in Cancer
Role: Principal Investigator
Funding: NATL INST OF HLTH NCI

Education

Ph.D. in Biochemistry
2003 · Stanford University
Bachelor's of Art in Biochemistry
1996 · Mills College

Contact Details

Phones:
Business:
(561) 228-2460
Emails:
Addresses:
Business Mailing:
130 SCRIPPS WAY # 3A3
JUPITER FL 33458