User:Meganlinson01/sandbox

Early Life
Dr. Frank M. Raushel was born on December 12th, 1949 in Hibbing, Minnesota.

Undergraduate Education

 * B. A. Chemistry, 1972, St. Thomas College (magna cum laude)

Graduate Education

 * Ph.D. in Biochemistry with a minor in Chemistry, 1976, University of Wisconsin-Madison. Worked in William Wallace Cleland's group
 * Postdoctoral Fellow in Chemistry, 1976-1980, Pennsylvania State University. Worked in Joseph J. Villafranca's group

Professional Appointments

 * 1972-1973: Research Assistant in the Department of Biochemistry at the University of Wisconsin
 * 1976-1980: Research Associate in the Department of Chemistry at Penn State University
 * 1980-1986: Assistant Professor in the Department of Chemistry at Texas A&M University
 * 1986-1989: Associate Professor in the Department of Chemistry and the Department of Biochemistry at Texas A&M University
 * 1992-1993: Visiting Professor at the Enzyme Institute at the University of Wisconsin
 * 1989-current:	Professor in the Department of Chemistry, Biochemistry, and Biophysics at Texas A&M University [2]

Areas of Research

 * Bioinorganic Chemistry
 * Chemical Biology
 * Chemical Catalysis
 * Organic Chemistry
 * Protein Engineering
 * Enzymes
 * Amino Acids
 * Genes

Current Research
Dr. Frank M. Raushel focuses on Stereochemistry, Enzyme, Biochemistry, Paraoxon and Substrate. His Stereochemistry research incorporates elements of Hydrolase, Protein subunit, Carbamoyl phosphate synthetase and Active site. The concepts of his Active site study are interwoven with issues in Crystallography, Enzyme kinetics, Divalent and Histidine. Raushel currently works on developing an antibacterial vaccine for Campylobacter jejuni (C. jejuni). The non-pathogenic strain of Escherichia Coli (E. coli) is similar to C. jejuni and can be used to test a variety of reaction conditions. Diacyl-phosphatidyl-phospho-Kdo linkages are a potential key to developing this antibacterial vaccine, however, this compound and its linkages have not been elucidated. The Kdo molecules have only been found in bacteria cells and are not present in Eukaryotic cells. There are six enzymes required to catalyze the reaction between biomolecules to synthesize diacyl-phosphatidyl-phospho-Kdo molecules. The first enzyme, KpsF, aids in the synthesis of D-arabinose from D-ribulose. Following KpsF is KdsA which uses PEP to synthesize D-arabinose to Kdo-8P. The next two enzymes are KdsC and KdsB. KdsC synthesizes Kdo-8P into Kdo and then KdsC synthesizes Kdo into Kdo-CMP. The last two enzymes, KpsS and KpsC, synthesize Kdo-CMP into diacyl-phosphatidyl-phospho-Kdo and attach additional Kdo molecules to the product. e. coli.[1]

Publications
Dr. Frank Raushel has 410 scientific publications with 17,945 citations (as of March 2024) according to research.com. The most recent publication is titled "Biosynthesis of Cytidine Diphosphate-6-d-Glucitol for the Capsular Polysaccharides of Campylobacter jejuni" published in February of 2024[3]. Other publication include "A Clinical-Stage Cysteine Protease Inhibitor blocks SARS-CoV-2 Infection of Human and Monkey Cells" that was published in 2021 and has 55 citations. In 2013, Dr. Raushel Published a paper titled "Enzymatic Neutralization of the Chemical Warfare Agent VX: Evolution of Phosphotriesterase for Phosphorothiolate Hydrolysis" that has been cited 87 times, and a paper titled "Catalytic mechanisms for phosphotriesterases" that has been cited 179 times. Dr. Raushel is still continuing his reseach at Texas A&M University and is still publishing his work.

Here are some more publications:
 * Riegert AS, Narindoshvili T, Platzer NE, Raushel FM. Functional Characterization of a HAD Phosphatase Involved in Capsular Polysaccharide Biosynthesis in . Biochemistry. PMID 36214481
 * Riegert AS, Narindoshvili T, Coricello A, Richards NGJ, Raushel FM. Correction to "Functional Characterization of Two PLP-Dependent Enzymes Involved in Capsular Polysaccharide Biosynthesis from ". Biochemistry. 61: 46. PMID 34928582
 * Truong DP, Rousseau S, Machala BW, Huddleston JP, Zhu M, Hull KG, Romo D, Raushel FM, Sacchettini JC, Glasner ME. Second-Shell Amino Acid R266 Helps Determine -Succinylamino Acid Racemase Reaction Specificity in Promiscuous -Succinylamino Acid Racemase/-Succinylbenzoate Synthase Enzymes. Biochemistry. PMID 34845903

Awards and Recognition

 * New Investigator Research Award from NIH
 * Research Career Development Award from NIH
 * Repligen Award in Biological Processes from ACS
 * Fellow of the American Association for the Advancement of Science (AAAS)
 * Fellow of American Chemical Society
 * Distinguished Achievement Award for Research from the Association of Former Students
 * Powell Professor of Science
 * Gordon Hammes ACS Biochemistry Lectureship
 * Southwest Regional ACS Research Award