Associate Professor of Biology
& Science Education
Principal Investigator, Robert Noyce STEM Teacher Scholarship Program,
Co-Principal Investigator, DoD CESE STEM Scholars Program,
Co-Principal Investigator, NSF CURENet2
Isi Ero-Tolliver, PhD
Associate Professor Dr. Ero-Tolliver
My research interests are in Biological Science, Science Education and Urban Education.
My focus is on learning scientific concepts and processes and then constructing ways to make these ideas more salient to students and teachers.
My focus is to use my skills and technology to create learning opportunities that target and entice minorities into the pipeline of science as a means of progressing towards diversity and equity in education.
Overall my interests are in inquiry-based reasoning in science, science teaching and learning, authentic science, models and modeling, and science teacher education.
Professor Ero-Tolliver's work investigates underrepresented minority (URM) student attitudes and identity towards STEM. Her current research relies on qualitative and quantitative methods to understanding optimum conditions for recruitment, retention and graduation of URMs in STEM disciplines.
Biological Sciences
Science Education
Ero-Tolliver's Biology Learning Lab (BLL): RESEARCH INTERESTS
(Please CLICK THE GREEN RECTANGLES BELOW FOR PICTURES)
Urban Education
MY RESEARCH:
Model-Based Reasoning: A commonality between scientific investigation and science education
TEACHING AND LEARNING SCIENCE THROUGH :
MODEL-BASED AND PROJECT-BASED REASONING
&
BIOLOGICAL SCIENCE RESEARCH
The Ancient Immunoglobulin Domains of Peroxidasin Are Required to Form Sulfilimine Cross-links in Collagen IV
Ero-Tolliver, I., Hudson,B., Bhave, G.
The collagen IV sulfilimine cross-link and its catalyzing enzyme, peroxidasin, represent a dyad critical for tissue development, which is conserved throughout the animal kingdom. Peroxidasin forms novel sulfilimine bonds between opposing methionine and hydroxylysine residues to structurally reinforce the collagen IV scaffold, a function critical for basement membrane and tissue integrity. However, the molecular mechanism underlying cross-link formation remains unclear. In this work, we demonstrate that the catalytic domain of peroxidasin and its immunoglobulin (Ig) domains are required for efficient sulfilimine bond formation. Thus, these molecular features underlie the evolutionarily conserved function of peroxidasin in tissue development and integrity and distinguish peroxidasin from other peroxidases, such as myeloperoxidase (MPO) and eosinophil peroxidase (EPO).
