Scott A. Coonrod

Oolemmal proteomics.

CABYR, a novel calcium-binding tyrosine phosphorylation-regulated fibrous sheath protein involved in capacitation.

TACC3 expression and localization in the murine egg and ovary.

SLLP1, a unique, intra-acrosomal, non-bacteriolytic, c lysozyme-like protein of human spermatozoa.

Oolemmal proteomics--identification of highly abundant heat shock proteins and molecular chaperones in the mature mouse egg and their localization on the plasma membrane.

ePAD, an oocyte and early embryo-abundant peptidylarginine deiminase-like protein that localizes to egg cytoplasmic sheets.

SAMP14, a novel, acrosomal membrane-associated, glycosylphosphatidylinositol-anchored member of the Ly-6/urokinase-type plasminogen activator receptor superfamily with a role in sperm-egg interaction.

Structural requirements for the inhibitory action of the CD9 large extracellular domain in sperm/oocyte binding and fusion.

Dynamic alterations of specific histone modifications during early murine development.

Human PAD4 regulates histone arginine methylation levels via demethylimination.

Regulation of coactivator complex assembly and function by protein arginine methylation and demethylimination.

Mouse SLLP1, a sperm lysozyme-like protein involved in sperm-egg binding and fertilization.

Peptidylarginine deiminase (PAD) is a mouse cortical granule protein that plays a role in preimplantation embryonic development.

Antibodies to two ZP3 B cell epitopes affect zona pellucida assembly.

Role for PADI6 and the cytoplasmic lattices in ribosomal storage in oocytes and translational control in the early mouse embryo.

Histone hypercitrullination mediates chromatin decondensation and neutrophil extracellular trap formation.

Use of proteomics to identify highly abundant maternal factors that drive the egg-to-embryo transition.

Potential role for peptidylarginine deiminase 2 (PAD2) in citrullination of canine mammary epithelial cell histones.

Potential role for MATER in cytoplasmic lattice formation in murine oocytes.

Regulation of mouse oocyte microtubule and organelle dynamics by PADI6 and the cytoplasmic lattices.

Genome-wide analysis reveals PADI4 cooperates with Elk-1 to activate c-Fos expression in breast cancer cells.

Synthesis and screening of a haloacetamidine containing library to identify PAD4 selective inhibitors.

Potential role for PADI-mediated histone citrullination in preimplantation development.

Role for peptidylarginine deiminase enzymes in disease and female reproduction.

Peptidylarginine deiminase 2-catalyzed histone H3 arginine 26 citrullination facilitates estrogen receptor α target gene activation.

Potential role for PAD2 in gene regulation in breast cancer cells.

Potential role of peptidylarginine deiminase enzymes and protein citrullination in cancer pathogenesis.

Identification of PADI2 as a potential breast cancer biomarker and therapeutic target.

D-amino acid based protein arginine deiminase inhibitors: Synthesis, pharmacokinetics, and in cellulo efficacy.

Identification of macrophage extracellular trap-like structures in mammary gland adipose tissue: a preliminary study.

Dysregulation of PAD4-mediated citrullination of nuclear GSK3β activates TGF-β signaling and induces epithelial-to-mesenchymal transition in breast cancer cells.

The role of MATER in endoplasmic reticulum distribution and calcium homeostasis in mouse oocytes.

A novel role for protein arginine deiminase 4 in pluripotency: the emerging role of citrullinated histone H1 in cellular programming.

Transient estrogen receptor binding and p300 redistribution support a squelching mechanism for estradiol-repressed genes.

Targeted H3R26 deimination specifically facilitates estrogen receptor binding by modifying nucleosome structure.

PAD2 overexpression in transgenic mice promotes spontaneous skin neoplasia.

Design, synthesis, and biological evaluation of tetrazole analogs of Cl-amidine as protein arginine deiminase inhibitors.

Protein arginine deiminase 2 binds calcium in an ordered fashion: implications for inhibitor design.