Stephen D. Ayers

ORCID: 0000-0003-1390-8969
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About
Contact & Profiles
Research Areas
  • Peroxisome Proliferator-Activated Receptors
  • Thyroid Disorders and Treatments
  • Growth Hormone and Insulin-like Growth Factors
  • Estrogen and related hormone effects
  • Epigenetics and DNA Methylation
  • Hormonal Regulation and Hypertension
  • Lipid metabolism and biosynthesis
  • Adipose Tissue and Metabolism
  • Genomics and Chromatin Dynamics
  • Cancer, Lipids, and Metabolism
  • Metabolism, Diabetes, and Cancer
  • RNA and protein synthesis mechanisms
  • Drug Transport and Resistance Mechanisms
  • NF-κB Signaling Pathways
  • Cholesterol and Lipid Metabolism
  • RNA Research and Splicing
  • Phytoestrogen effects and research
  • Fibroblast Growth Factor Research
  • Animal Genetics and Reproduction
  • Pharmacogenetics and Drug Metabolism
  • Metabolism and Genetic Disorders
  • CRISPR and Genetic Engineering
  • Effects and risks of endocrine disrupting chemicals
  • Protein Kinase Regulation and GTPase Signaling
  • Genetic and Clinical Aspects of Sex Determination and Chromosomal Abnormalities

Houston Methodist
2011-2015

Personalis (United States)
2014

Methodist Hospital
2011-2014

Cornell University
2007-2012

Methodist Hospital
2011

Children's Cancer Center
2011

Baylor College of Medicine
2011

Birmingham City Hospital
2007

Case Western Reserve University
2007

The recent discovery that peroxisome proliferator-activated receptor γ (PPARγ) targeted anti-diabetic drugs function by inhibiting Cdk5-mediated phosphorylation of the has provided a new viewpoint to evaluate and perhaps develop improved insulin-sensitizing agents. Herein we report development novel thiazolidinedione retains similar efficacy as rosiglitazone in mice yet does not elicit weight gain or edema, common side effects associated with full PPARγ activation. Further characterization...

10.1074/jbc.m111.332106 article EN cc-by Journal of Biological Chemistry 2012-05-15

FABP4 delivers specific ligands from the cytosol to nuclear receptor PPARγ in nucleus, thereby facilitating ligation and enhancing transcriptional activity of receptor. Here, we delineate structural features that underlie nucleocytoplasmic transport FABP4. The primary sequence does not harbor a readily identifiable localization signal (NLS). However, such could be found three-dimensional structure protein was mapped three basic residues form functional NLS stabilized by FABP4/PPARγ ligand...

10.1021/bi700047a article EN Biochemistry 2007-05-22

Many pathogens colonize different anatomical sites, but the selective pressures contributing to survival in diverse niches are poorly understood. Group A Streptococcus (GAS) is a human-adapted bacterium that causes range of infections. Much effort has been expended dissect molecular basis invasive (sterile-site) infections, little known about genomes strains causing pharyngitis (streptococcal "sore throat"). Additionally, there essentially nothing genetic relationships between populations...

10.1073/pnas.1016282108 article EN Proceedings of the National Academy of Sciences 2011-03-07

Peroxisome proliferator-activated receptors (PPARs) are members of a superfamily nuclear transcription factors. They involved in mediating numerous physiological effects humans, including glucose and lipid metabolism. PPARα ligands effectively treat dyslipidemia have significant antiinflammatory anti-atherosclerotic activities. These their ligand-dependent activity make obvious targets for drug design. Here, we present the structure human complex with WY14643, member fibrate class drug,...

10.1016/j.jmb.2013.05.010 article EN publisher-specific-oa Journal of Molecular Biology 2013-05-21

The peroxisome proliferator-activated receptor γ (PPARγ) is a target for treatment of type II diabetes and other conditions. PPARγ full agonists, such as thiazolidinediones (TZDs), are effective insulin sensitizers anti-inflammatory agents, but their use limited by adverse side effects. Luteolin flavonoid with actions that binds but, unlike TZDs, does not promote adipocyte differentiation. However, previous reports suggested variously luteolin agonist or an antagonist. We show exhibits weak...

10.1124/mol.111.076216 article EN Molecular Pharmacology 2012-03-05

Thyroid hormone (TH) receptors (TRs) play central roles in metabolism and are major targets for pharmaceutical intervention. Presently, however, there is limited information about genome wide localizations of TR binding sites. Thus, complexities genomic distribution links between TRβ events gene regulation not fully appreciated. Here, we employ a BioChIP approach to capture genome-wide liver cell line (HepG2). Like other NRs, appears widely distributed throughout the genome. Nevertheless,...

10.1371/journal.pone.0081186 article EN PLoS ONE 2014-02-18

Nuclear receptors (NRs) play crucial roles in the regulation of hepatic cholesterol synthesis, metabolism, and conversion to bile acids, but their actions cholangiocytes have not been examined. In this study, we investigated NRs cholangiocyte physiology metabolism flux. We examined expression other genes involved homeostasis freshly isolated cultured murine found that these cells express a specific subset NRs, including liver X receptor (LXR) β peroxisome proliferator-activated (PPAR) δ....

10.1002/hep.25919 article EN Hepatology 2012-06-22

Thyroid hormone (TH) acts through specific receptors (TRs), which are conditional transcription factors, to induce fibroblast growth factor 21 (FGF21), a peptide that is usually induced by fasting and influences lipid carbohydrate metabolism via local hepatic systemic endocrine effects. While TH FGF21 display overlapping actions when administered, including reductions in serum lipids, according the current models these hormones act independently vivo. In this study, we examined mechanisms of...

10.1530/joe-14-0440 article EN Journal of Endocrinology 2014-12-11

Gene expression is tightly regulated by transcription factors and cofactors that function directly or indirectly interacting with DNA of the genome. Understanding how where these proteins bind provides essential information to uncover genetic regulatory mechanisms. We have developed a new method study DNA-protein interaction in vivo called adenine methyltransferase (Dam)IP, which based on fusing protein interest mutant form Dam from Escherichia coli. showed previously DamIP can efficiently...

10.1210/me.2011-1080 article EN Molecular Endocrinology 2011-12-30

10.1016/j.bpj.2010.12.559 article EN publisher-specific-oa Biophysical Journal 2011-02-01
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