Kate Carroll

Last updated
Kate S. Carroll
Alma mater Mills College (BA)
Stanford University (PhD)
University of California, Berkeley (PostDoc)
Awards Special Fellow Award (2006)
Scientist Development Award (2008)
Camille Dreyfus Teacher-Scholar Awards (2010)
Pfizer Award in Enzyme Chemistry (2013)
Scientific career
Fields Biochemistry
Institutions University of Michigan
University of Florida
Thesis Molecular cooperation in mannose 6-phosphate receptor transport
Doctoral advisor Suzanne Pfeffer
Other academic advisorsCarolyn Bertozzi
Website www.katecarrolllab.com/kate-carroll

Kate Carroll (born 1974) is an American professor of chemistry, chemical biology, and biochemistry at Florida Atlantic University. She was previously a tenure-track assistant professor at the University of Michigan [1] and was a Professor at Scripps Research in Jupiter, FL from 2010 - 2024

Contents

Education

Carroll received a BA in Chemistry from Mills College in 1996 and her PhD in Chemistry from Stanford University in 2003, studying with Suzanne Pfeffer. [2] Her graduate research involved studying protein regulation of genes such as Rab9. She completed postdoctoral studies with Carolyn R. Bertozzi in 2006.

Research

Carroll has developed protein cysteine oxidation as a new paradigm for the regulation of cell signaling pathways. Her group has also examined sulfa- and thioreductase activity in Mycobacterium as potential drug targets to treat diseases like tuberculosis. Carroll incorporates tools such as proteomic labeling and chemical probes to decipher how oxidation of target cysteines in proteins by reactive oxygen species (ROS) leads to downstream changes in cell cycle regulation. [3]

Volunteer service

Carroll served as the Vice-Chair for the 2018 Gordon Research Conference in Thiol-Based Redox Regulation and Signaling. She will serve as the Chair in 2020.

She serves as an Editorial board member to scientific journals including Journal of Biological Chemistry, Molecular Biosystems, and Cell Chemical Biology.

Awards

Related Research Articles

<span class="mw-page-title-main">Coenzyme A</span> Coenzyme, notable for its synthesis and oxidation role

Coenzyme A (CoA, SHCoA, CoASH) is a coenzyme, notable for its role in the synthesis and oxidation of fatty acids, and the oxidation of pyruvate in the citric acid cycle. All genomes sequenced to date encode enzymes that use coenzyme A as a substrate, and around 4% of cellular enzymes use it (or a thioester) as a substrate. In humans, CoA biosynthesis requires cysteine, pantothenate (vitamin B5), and adenosine triphosphate (ATP).

<span class="mw-page-title-main">Protein disulfide-isomerase</span> Class of enzymes

Protein disulfide isomerase, or PDI, is an enzyme in the endoplasmic reticulum (ER) in eukaryotes and the periplasm of bacteria that catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold. This allows proteins to quickly find the correct arrangement of disulfide bonds in their fully folded state, and therefore the enzyme acts to catalyze protein folding.

<span class="mw-page-title-main">Thioredoxin</span> Class of reduction–oxidation proteins

Thioredoxin is a class of small redox proteins known to be present in all organisms. It plays a role in many important biological processes, including redox signaling. In humans, thioredoxins are encoded by TXN and TXN2 genes. Loss-of-function mutation of either of the two human thioredoxin genes is lethal at the four-cell stage of the developing embryo. Although not entirely understood, thioredoxin is linked to medicine through their response to reactive oxygen species (ROS). In plants, thioredoxins regulate a spectrum of critical functions, ranging from photosynthesis to growth, flowering and the development and germination of seeds. Thioredoxins play a role in cell-to-cell communication.

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<span class="mw-page-title-main">GLRX2</span> Protein-coding gene in the species Homo sapiens

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In organic chemistry, S-nitrosothiols, also known as thionitrites, are organic compounds or functional groups containing a nitroso group attached to the sulfur atom of a thiol. S-Nitrosothiols have the general formula R−S−N=O, where R denotes an organic group. Originally suggested by Ignarro to serve as intermediates in the action of organic nitrates, endogenous S-nitrosothiols were discovered by Stamler and colleagues (S-nitrosoalbumin in plasma and S-nitrosoglutathione in airway lining fluid) and shown to represent a main source of NO bioactivity in vivo. More recently, S-nitrosothiols have been implicated as primary mediators of protein S-nitrosylation, the oxidative modification of cysteine thiol that provides ubiquitous regulation of protein function.

<span class="mw-page-title-main">RoGFP</span> Prodified GFP protein that exhibits different fluorescent properties when oxidized and reduced

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References

  1. "Kate Carroll | Kate Carroll Lab". Kate Carroll Lab | Scripps | Florida | Chemical Biology | Cysteine. Retrieved 2018-10-20.
  2. "Molecular cooperation in mannose 6-phosphate receptor transport in SearchWorks catalog". searchworks.stanford.edu. Retrieved 2018-10-20.
  3. Conte, Mauro Lo; Carroll, Kate S. (2013-09-13). "The Redox Biochemistry of Protein Sulfenylation and Sulfinylation". Journal of Biological Chemistry. 288 (37): 26480–26488. doi: 10.1074/jbc.R113.467738 . ISSN   0021-9258. PMC   3772195 . PMID   23861405.
  4. "News and Events | Scripps Research".