Shelbi Christgen

ORCID: 0000-0003-1145-4430
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About
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Research Areas
  • Inflammasome and immune disorders
  • interferon and immune responses
  • Enzyme Structure and Function
  • Immune Response and Inflammation
  • Bacterial Genetics and Biotechnology
  • RNA and protein synthesis mechanisms
  • Cell death mechanisms and regulation
  • Biochemical and Molecular Research
  • Mass Spectrometry Techniques and Applications
  • Amino Acid Enzymes and Metabolism
  • Plant nutrient uptake and metabolism
  • DNA Repair Mechanisms
  • Burkholderia infections and melioidosis
  • Chemical Synthesis and Analysis
  • Biotin and Related Studies
  • Electrochemical Analysis and Applications
  • Chromosomal and Genetic Variations
  • Electrochemical sensors and biosensors
  • Neutrophil, Myeloperoxidase and Oxidative Mechanisms
  • Protein Structure and Dynamics
  • Heat shock proteins research
  • Gastroesophageal reflux and treatments
  • Genomics and Phylogenetic Studies
  • Histiocytic Disorders and Treatments
  • Legume Nitrogen Fixing Symbiosis

St. Jude Children's Research Hospital
2019-2022

University of Nebraska–Lincoln
2014-2021

Missouri Western State University
2015

Programmed cell death plays crucial roles in organismal development and host defense. Recent studies have highlighted mechanistic overlaps extensive, multifaceted crosstalk between pyroptosis, apoptosis, necroptosis, three programmed pathways traditionally considered autonomous. The growing body of evidence, conjunction with the identification molecules controlling concomitant activation all by pathological triggers, has led to concept PANoptosis. During PANoptosis, inflammatory occurs...

10.3389/fcimb.2020.00237 article EN cc-by Frontiers in Cellular and Infection Microbiology 2020-05-29

Cell death provides host defense and maintains homeostasis. Zα-containing molecules are essential for these processes. Z-DNA binding protein 1 (ZBP1) activates inflammatory cell death, PANoptosis, whereas adenosine deaminase acting on RNA (ADAR1) serves as an editor to maintain Here, we identify characterize ADAR1's interaction with ZBP1, defining its role in regulation tumorigenesis. Combining interferons (IFNs) nuclear export inhibitors (NEIs) ZBP1-dependent PANoptosis. ADAR1 suppresses...

10.1016/j.celrep.2021.109858 article EN cc-by Cell Reports 2021-10-01

10.1016/bs.mie.2019.03.004 article EN Methods in enzymology on CD-ROM/Methods in enzymology 2019-01-01

The bifunctional flavoenzyme proline utilization A (PutA) catalyzes the two-step oxidation of to glutamate using separate dehydrogenase (PRODH) and l-glutamate-γ-semialdehyde active sites. Because PutAs catalyze sequential reactions, they are good systems for studying how metabolic enzymes communicate via substrate channeling. Although mechanistically similar, vary widely in domain architecture, oligomeric state, quaternary structure, these variations represent different structural solutions...

10.1074/jbc.m117.786855 article EN cc-by Journal of Biological Chemistry 2017-04-19

Burkholderia infections can result in serious diseases with high mortality, such as melioidosis, and they are difficult to treat antibiotics. Innate immunity is critical for cell-autonomous clearance of intracellular pathogens like by regulating programmed cell death. Inflammasome-dependent inflammatory cytokine release death contribute host protection against pseudomallei thailandensis; however, the contribution apoptosis necroptosis not known. Here, we found that bone marrow-derived...

10.1128/mbio.01059-21 article EN mBio 2021-06-22

Proline utilization A (PutA) is a bifunctional enzyme that catalyzes the oxidation of proline to glutamate. Structures type PutAs have revealed catalytic core consisting dehydrogenase (PRODH) and Δ(1)-pyrroline-5-carboxylate (P5CDH) modules connected by substrate-channeling tunnel. Type B also C-terminal domain unknown function (CTDUF) absent in PutAs. Small-angle X-ray scattering (SAXS), mutagenesis, kinetics are used determine contributions this PutA structure function. The 1127-residue...

10.1021/bi500693a article EN publisher-specific-oa Biochemistry 2014-08-19

Escherichia coli proline utilization A (EcPutA) is the archetype of trifunctional PutA flavoproteins, which function both as regulators operon and bifunctional enzymes that catalyze four-electron oxidation to glutamate. EcPutA shifts from a self-regulating transcriptional repressor enzyme in process known functional switching. The flavin redox state dictates EcPutA. Upon oxidation, becomes reduced, triggering conformational change causes dissociate put regulon bind cellular membrane. Major...

10.1021/acs.biochem.7b01008 article EN Biochemistry 2017-11-01

Proline utilization A from Escherichia coli (EcPutA) is a multifunctional flavoenzyme that oxidizes proline to glutamate through dehydrogenase (PRODH) and Δ1-pyrroline-5-carboxylate (P5CDH) activities, while also switching roles as DNA-bound transcriptional repressor membrane-bound catabolic enzyme. This phenomenon, termed functional switching, occurs redox-mediated mechanism in which flavin reduction triggers conformational change increases EcPutA membrane binding affinity. Structural...

10.1021/acs.biochem.7b00046 article EN Biochemistry 2017-05-30

The upregulation of interferon (IFN)-inducible GTPases in response to pathogenic insults is vital host defense against many bacterial, fungal, and viral pathogens. Several IFN-inducible play key roles mediating inflammasome activation providing protection after bacterial or fungal infections, though their role infection less clear. Among the GTPases, expression immunity-related (IRGs) varies widely across species for unknown reasons. Here, we report that IRGB10, but not IRGM1, IRGM2, IRGM3,...

10.1002/eji.202149305 article EN European Journal of Immunology 2021-10-25

Helicobacters have been associated with many diseases; including inflammatory bowel disease (Shomer, N et. al. 1997 Infec & Immun 65: 4858‐64). It is thought that the chronic response experienced by host in to Helicobacter infection cause of subsequent (Maggio‐Price L 2006 Cancer Research 66: 828‐38). One preferred respiratory substrates amino acid proline. In some bacteria, proline metabolized utilization A (PutA). PutAs shown utilize substrate channeling between two active site...

10.1096/fasebj.29.1_supplement.573.49 article EN The FASEB Journal 2015-04-01
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