Kelly A. Servage

ORCID: 0000-0001-7183-2865
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About
Contact & Profiles
Research Areas
  • Selenium in Biological Systems
  • Endoplasmic Reticulum Stress and Disease
  • Mass Spectrometry Techniques and Applications
  • Autophagy in Disease and Therapy
  • Analytical Chemistry and Chromatography
  • Legionella and Acanthamoeba research
  • Extracellular vesicles in disease
  • MicroRNA in disease regulation
  • Redox biology and oxidative stress
  • Advanced Proteomics Techniques and Applications
  • Ubiquitin and proteasome pathways
  • Cancer Research and Treatments
  • Calcium signaling and nucleotide metabolism
  • ATP Synthase and ATPases Research
  • Genomics and Chromatin Dynamics
  • Heat shock proteins research
  • RNA Research and Splicing
  • Nanoplatforms for cancer theranostics
  • RNA and protein synthesis mechanisms
  • Protein Kinase Regulation and GTPase Signaling
  • Vibrio bacteria research studies
  • RNA Interference and Gene Delivery
  • RNA modifications and cancer
  • Plant-Microbe Interactions and Immunity
  • DNA Repair Mechanisms

Southwestern Medical Center
2018-2025

The University of Texas Southwestern Medical Center
2018-2025

Howard Hughes Medical Institute
2017-2025

Purdue University West Lafayette
2024

University of Maine
2024

Texas A&M University
2013-2016

Past experimental results and molecular dynamics simulations provide evidence that, under some conditions, electrospray ionization (ESI) of biomolecules produces ions that retain elements solution phase structures. However, there is a dearth information regarding the question raised by Breuker McLafferty, "for how long, what to extent, can structure be retained without solvent?" (Proc. Natl. Acad. Sci. U.S.A. 2008, 105, 18145). Here, we use cryogenic ion mobility-mass spectrometry...

10.1021/ja4114193 article EN Journal of the American Chemical Society 2013-12-06

Divergent protein kinase SidJ is a produced by Legionella pneumophila that orchestrates this intracellular pathogen's establishment within the host cell. prevents lysosome fusion with vacuole, which bacterium resides and replicates. also modulates toxicity of SidE family ubiquitin ligases catalyze phosphoribosyl-linked ubiquitination. Black et al. discovered activated calmodulin. Furthermore, although has pseudokinase fold, it does not phosphorylate proteins but polyglutamylates them...

10.1126/science.aaw7446 article EN Science 2019-05-23

Cancer evolves through a multistep process that occurs by the temporal accumulation of genetic mutations. Tumor-derived exosomes are emerging contributors to tumorigenesis. To understand how might contribute cell transformation, we utilized classic two-step NIH/3T3 transformation assay and observed isolated from pancreatic cancer cells, but not normal human can initiate malignant these transformed cells formed tumors in vivo. However, unable transform alone or act as promoter transformation....

10.7554/elife.40226 article EN cc-by eLife 2019-05-28

Coordinated assembly and disassembly of integrin-mediated focal adhesions (FAs) is essential for cell migration. Many studies have shown that FA requires Ca2+ influx, however our understanding this process remains incomplete. Here, we show influx via STIM1/Orai1 calcium channels, which cluster near FAs, leads to activation the GTPase Arf5 Ca2+-activated GEF IQSec1, both IQSec1 are adhesion disassembly. We further forms a complex with lipid transfer protein ORP3, triggers PKC-dependent...

10.7554/elife.54113 article EN cc-by eLife 2020-04-01

During homeostasis, the endoplasmic reticulum (ER) maintains productive transmembrane and secretory protein folding that is vital for proper cellular function. The ER-resident HSP70 chaperone, BiP, plays a pivotal role in sensing ER stress to activate unfolded response (UPR). BiP function regulated by bifunctional enzyme FicD mediates AMPylation deAMPylation of changes stress. AMPylated acts as molecular rheostat regulate UPR signaling, yet little known about consequences loss. In this...

10.1101/2024.01.22.576705 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2024-01-23

<div>Abstract<p>Evolutionarily conserved selenoprotein O (SELENOO) catalyzes a posttranslational protein modification known as AMPylation that is essential for the oxidative stress response in bacteria and yeast. Given experienced blood limits survival of metastasizing melanoma cells, SELENOO might be able to affect metastatic potential. However, further work needed elucidate substrates functional relevance mammalian homolog SELENOO. In this study, we revealed promotes cancer...

10.1158/0008-5472.c.7700625 preprint EN 2025-03-03

The Legionella SidE effectors ubiquitinate host proteins independently of the canonical E1-E2 cascade. Here we engineer ligases to develop a modular proximity ligation approach for identification targets small molecules and proteins, which call SidBait. We validate method with known molecule-protein interactions use it identify CaMKII as an off-target interactor breast cancer drug ribociclib. Structural analysis activity assays confirm that ribociclib binds active site inhibits its activity....

10.1101/2025.03.20.644192 preprint EN cc-by bioRxiv (Cold Spring Harbor Laboratory) 2025-03-22

Evaporation of water from extensively hydrated protons and peptides formed by electrospray ionization (ESI) has been examined for the first time cryogenic ion mobility-mass spectrometry (IM-MS). The extent hydration was controlled using a heated capillary inlet operated between 340 391 K. Cold cluster ions in source region were transported into low temperature (∼80 K) IM drift tube an electrostatic guide where they separated on basis size-to-charge via low-energy collisions with helium gas....

10.1021/jp311278a article EN The Journal of Physical Chemistry A 2013-01-16

ConspectusElectrospray ionization (ESI) combined with ion mobility-mass spectrometry (IM-MS) is adding new dimensions, that is, structure and dynamics, to the field of biological mass spectrometry. There increasing evidence gas-phase ions produced by ESI can closely resemble their solution-phase structures, but correlating these structures be complicated owing number competing effects contributing structural preferences, including both inter- intramolecular interactions. Ions encounter...

10.1021/acs.accounts.6b00177 article EN Accounts of Chemical Research 2016-06-23

In response to environmental, developmental, and pathological stressors, cells engage homeostatic pathways maintain their function. Among these pathways, the Unfolded Protein Response protects from accumulation of misfolded proteins in ER. Depending on ER stress levels, ER-resident Fic protein catalyzes AMPylation or de-AMPylation BiP, major chaperone regulator Response. This work elucidates importance reversible BiP maintaining Drosophila visual system stress. After 72 hr constant light,...

10.7554/elife.38752 article EN cc-by eLife 2018-07-17
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