Paula J. Olsiewski

Last updated
Paula J. Olsiewski
NationalityAmerican
Alma materYale College,
Massachusetts Institute of Technology
SpouseJohn Healey
Scientific career
Fieldsbiochemist
InstitutionsAlfred P. Sloan Foundation; Johns Hopkins Center for Health Security

Paula J. Olsiewski is an American biochemist who is a Contributing Scholar at the Johns Hopkins Center for Health Security. [1] She was a Program Director at the Alfred P. Sloan Foundation, where she created and directed the Foundation's programs in the Microbiology of the Built Environment, the Chemistry of Indoor Environments and Civic Initiatives. She directed the Biosecurity program [2] [3] [4] until its conclusion in 2011 and the Synthetic Biology program until its conclusion in 2014.

Contents

Education

Olsiewski holds a bachelor's degree in chemistry from Yale College, and a Doctor of Philosophy in biological chemistry from the Massachusetts Institute of Technology (1979) with a thesis on D-amino acid dehydrogenase evolution, supervised by Christopher T. Walsh.[ citation needed ] From 1980 to 1982 she was a Postdoctoral Fellow in the lab of William H. Beers at New York University.[ citation needed ]

Biotech and biomedical commercial development

Olsiewski directed commercial development for in vitro diagnostic products at Enzo Biochem, (NYSE:ENZ), a biotechnology company focused on the manipulation and modification of nucleic acids to produce therapeutic and diagnostic products. [5] She directed the New York City Biotechnology Initiative, a state funded program to improve the region's ability to grow biotechnology companies by fostering relationships between industry and academia. She also established and directed the Technology Development Office at the Hospital for Special Surgery. [6]

Board and advisory committee roles

Olsiewski is chair of the Board of Scientific Counselors Homeland Security Research Subcommittee at the U.S. Environmental Protection Agency, and on the board of directors at the Critical Path Institute. In 2001 she served on the Board of Advisors for the WMD Center's Bio-Response Report Card. [7] From 2003 to 2009 she was a member of the MIT Corporation. [8] She was the first alumna to serve as President of the MIT Alumni Association (2003-2004), and served on the advisory board of the MIT Initiative on Faculty Race and Diversity [9] (2008-2009). She was a member of the Committee on Advances in Technology and the Prevention of Their Application to Next Generation Biowarfare Threats, which produced the National Research Counsel Report “Globalization, Biosecurity, and the Future of Life Sciences” [10] (2006). From 2005 to 2012 she served on the advisory board for the National Consortium for the Study of Terrorism and Responses to Terrorism (START).

Selected writings & publications

Her most cited papers, according to Google Scholar: [11]

Awards and honors

In 1995, Olsiewski won the MIT Henry B. Kane '24 Award, which is given in recognition of exception service and accomplishments in the area of fundraising. [12] In 2000, she received the MIT Bronze Beaver Alumni Award, which is given in recognition of distinguished service - it is the highest honor the Alumni Association bestows upon any of its members. [13] Also in 2000, she received the Yale Class Distinguished Service Award, which is selected by the class leadership and bestowed to recognize and thank classmates who have dedicated time, energy and enthusiasm to the Class. [14] In 2018, Olsiewski was elected as a AAAS Fellow in the Chemical Sciences division. [15] In 2022, the International Society of Indoor Air Quality and Climate inducted Olsiewski as a new Academy Fellow [16] and awarded her their Special Award ″in recognition of her advocacy and support of basic research for the microbiology and chemistry of the indoor environment.″ [17]

Related Research Articles

<span class="mw-page-title-main">Alanine</span> Α-amino acid that is used in the biosynthesis of proteins

Alanine (symbol Ala or A), or α-alanine, is an α-amino acid that is used in the biosynthesis of proteins. It contains an amine group and a carboxylic acid group, both attached to the central carbon atom which also carries a methyl group side chain. Consequently, its IUPAC systematic name is 2-aminopropanoic acid, and it is classified as a nonpolar, aliphatic α-amino acid. Under biological conditions, it exists in its zwitterionic form with its amine group protonated (as −NH3+) and its carboxyl group deprotonated (as −CO2−). It is non-essential to humans as it can be synthesised metabolically and does not need to be present in the diet. It is encoded by all codons starting with GC (GCU, GCC, GCA, and GCG).

<span class="mw-page-title-main">Threonine</span> Amino acid

Threonine is an amino acid that is used in the biosynthesis of proteins. It contains an α-amino group, a carboxyl group, and a side chain containing a hydroxyl group, making it a polar, uncharged amino acid. It is essential in humans, meaning the body cannot synthesize it: it must be obtained from the diet. Threonine is synthesized from aspartate in bacteria such as E. coli. It is encoded by all the codons starting AC.

Pyruvic acid (IUPAC name: 2-oxopropanoic acid, also called acetoic acid) (CH3COCOOH) is the simplest of the alpha-keto acids, with a carboxylic acid and a ketone functional group. Pyruvate, the conjugate base, CH3COCOO−, is an intermediate in several metabolic pathways throughout the cell.

<span class="mw-page-title-main">Malate dehydrogenase</span> Class of enzymes

Malate dehydrogenase (EC 1.1.1.37) (MDH) is an enzyme that reversibly catalyzes the oxidation of malate to oxaloacetate using the reduction of NAD+ to NADH. This reaction is part of many metabolic pathways, including the citric acid cycle. Other malate dehydrogenases, which have other EC numbers and catalyze other reactions oxidizing malate, have qualified names like malate dehydrogenase (NADP+).

<span class="mw-page-title-main">Homoserine</span> Chemical compound

Homoserine (also called isothreonine) is an α-amino acid with the chemical formula HO2CCH(NH2)CH2CH2OH. L-Homoserine is not one of the common amino acids encoded by DNA. It differs from the proteinogenic amino acid serine by insertion of an additional -CH2- unit into the backbone. Homoserine, or its lactone form, is the product of a cyanogen bromide cleavage of a peptide by degradation of methionine.

<span class="mw-page-title-main">Glucose-6-phosphate dehydrogenase</span> Enzyme involved in the production of energy by cells

Glucose-6-phosphate dehydrogenase (G6PD or G6PDH) (EC 1.1.1.49) is a cytosolic enzyme that catalyzes the chemical reaction

The branched-chain α-ketoacid dehydrogenase complex is a multi-subunit complex of enzymes that is found on the mitochondrial inner membrane. This enzyme complex catalyzes the oxidative decarboxylation of branched, short-chain alpha-ketoacids. BCKDC is a member of the mitochondrial α-ketoacid dehydrogenase complex family comprising pyruvate dehydrogenase and alpha-ketoglutarate dehydrogenase, key enzymes that function in the Krebs cycle.

<span class="mw-page-title-main">Pyruvate dehydrogenase</span> Class of enzymes

Pyruvate dehydrogenase is an enzyme that catalyzes the reaction of pyruvate and a lipoamide to give the acetylated dihydrolipoamide and carbon dioxide. The conversion requires the coenzyme thiamine pyrophosphate.

<span class="mw-page-title-main">Dihydrolipoamide dehydrogenase</span> Protein-coding gene in the species Homo sapiens

Dihydrolipoamide dehydrogenase (DLD), also known as dihydrolipoyl dehydrogenase, mitochondrial, is an enzyme that in humans is encoded by the DLD gene. DLD is a flavoprotein enzyme that oxidizes dihydrolipoamide to lipoamide.

D-amino-acid dehydrogenase is a bacterial enzyme that catalyses the oxidation of D-amino acids into their corresponding oxoacids. It contains both flavin and nonheme iron as cofactors. The enzyme has a very broad specificity and can act on most D-amino acids.

<span class="mw-page-title-main">HSD17B1</span> Protein-coding gene in the species Homo sapiens

17β-Hydroxysteroid dehydrogenase 1 (17β-HSD1) is an enzyme that in humans is encoded by the HSD17B1 gene. This enzyme oxidizes or reduces the C17 hydroxy/keto group of androgens and estrogens and hence is able to regulate the potency of these sex steroids

<span class="mw-page-title-main">AKR1C1</span> Protein-coding gene in the species Homo sapiens

Aldo-keto reductase family 1 member C1 also known as 20α-hydroxysteroid dehydrogenase, 3α-hydroxysteroid dehydrogenase, and dihydrodiol dehydrogenase 1/2 is an enzyme that in humans is encoded by the AKR1C1 gene.

<span class="mw-page-title-main">PDK2</span> Protein-coding gene in the species Homo sapiens

Pyruvate dehydrogenase kinase isoform 2 (PDK2) also known as pyruvate dehydrogenase lipoamide kinase isozyme 2, mitochondrial is an enzyme that in humans is encoded by the PDK2 gene. PDK2 is an isozyme of pyruvate dehydrogenase kinase.

<span class="mw-page-title-main">Helen M. Berman</span> American chemist

Helen Miriam Berman is a Board of Governors Professor of Chemistry and Chemical Biology at Rutgers University and a former director of the RCSB Protein Data Bank. A structural biologist, her work includes structural analysis of protein-nucleic acid complexes, and the role of water in molecular interactions. She is also the founder and director of the Nucleic Acid Database, and led the Protein Structure Initiative Structural Genomics Knowledgebase.

<span class="mw-page-title-main">BCKDK</span> Protein-coding gene in the species Homo sapiens

Branched chain ketoacid dehydrogenase kinase (BCKDK) is an enzyme encoded by the BCKDK gene on chromosome 16. This enzyme is part of the mitochondrial protein kinases family and it is a regulator of the valine, leucine, and isoleucine catabolic pathways. BCKDK is found in the mitochondrial matrix and the prevalence of it depends on the type of cell. Liver cells tend to have the lowest concentration of BCKDK, whereas skeletal muscle cells have the highest amount. Abnormal activity of this enzyme often leads to diseases such as maple syrup urine disease and cachexia.

Michelle C. Y. Chang is a Professor of Chemistry and Chemical and Biomolecular Engineering at the University of California, Berkeley, and is a recipient of several young scientist awards for her research in biosynthesis of biofuels and pharmaceuticals.

D-amino acid dehydrogenase (quinone) (EC 1.4.5.1, DadA) is an enzyme with systematic name D-amino acid:quinone oxidoreductase (deaminating). This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Paula T. Hammond</span> American chemical engineer (born 1963)

Paula Therese Hammond is a David H. Koch Professor in Engineering and the Head of the Department of Chemical Engineering at the Massachusetts Institute of Technology (MIT). She was the first woman and person of color appointed as head of the Chemical Engineering department. Her laboratory designs polymers and nanoparticles for drug delivery and energy-related applications including batteries and fuel cells.

Bradley Lether Pentelute is currently a professor of chemistry at the Massachusetts Institute of Technology (MIT). His research program lies at the intersection of chemistry and biology and develops bioconjugation strategies, cytosolic delivery platforms, and rapid flow synthesis technologies to optimize the production, achieve site-specific modification, enhance stability, and modulate function of a variety of bioactive agents. His laboratory successfully modified proteins via cysteine-containing “pi-clamps” made up of a short sequence of amino acids, and delivered large biomolecules, such as various proteins and drugs, into cells via the anthrax delivery vehicle. Pentelute has also made several key contributions to automated synthesis technologies in flow. These advances includes the invention of the world's fastest polypeptide synthesizer. This system is able to form amide bonds at a more efficient rate than standard commercial equipment and has helped in the process of understanding protein folding and its mechanisms. This automated flow technology was recently used to achieve total chemical synthesis of protein chains up to 164 amino acids in length that retained the structure and function of native variants obtained by recombinant expression. The primary goal of his endeavor is to use these processes to create designer biologics that can be used to treat diseases and solve the manufacturing problem for on-demand personalized therapies, such as cancer vaccines.

Barbara Imperiali is a Professor of Biology and Chemistry at Massachusetts Institute of Technology and Affiliate Member of the Broad Institute. She is an elected member of the National Academy of Sciences and a Fellow of the Royal Society of Chemistry.

References

  1. ↑ "Biography of Paula Olsiewski with the Center for Health Security". Johns Hopkins Center for Health Security. Retrieved 2020-12-02.
  2. ↑ Gronvall, G.K. (2012). Preparing for Bioterrorism: The Sloan Foundation's Leadership in Biosecurity. Center for Biosecurity of UPMC.
  3. ↑ Hitchcock, P.J.; Mair, M; Inglesby, TV; Henderson, DA; O'Toole, T; Ahern-Seronde, J; Bahnfleth, WP; Brennan, T; Burroughs, HE; Davidson, C; Delp, W; Ensor, DS; Gomory, R; Olsiewski, P; Samet, JM; Smith, WM; Streifel, AJ; White, RH; Woods, JE (2006). "Improving Performance of HVAC Systems to Reduce Exposure to Aerosolized Infectious Agents in Buildings; Recommendations to Reduce Risks Posed by Biological Attacks". Biosecurity and Bioterrorism. 4 (1): 41–54. doi:10.1089/bsp.2006.4.41. PMID   16545023.
  4. ↑ Morse, S.S.; Garwin, R.L.; Olsiewski, P.J. (2006). "Next Flu Pandemic: What to Do Until the Vaccine Arrives?". Science. 314 (5801): 929. doi:10.1126/science.1135823. PMID   17095681. S2CID   20519907.
  5. ↑ "Staff Directory". www.sloan.org. Archived from the original on 2012-09-14.
  6. ↑ "Staff Directory". www.sloan.org. Archived from the original on 2012-09-14.
  7. ↑ Bio Response Report Card 2011.[ verification needed ]
  8. ↑ "The MIT Corporation, Corporational Membership, Historical" . Retrieved February 24, 2017.
  9. ↑ MIT Report on the Initiative for Faculty Race and Diversity (PDF).[ verification needed ]
  10. ↑ Academies, Committee on Advances in Technology and the Prevention of Their Application to Next Generation Biowarfare Threats ; Development, Security, and Cooperation Policy and Global Affairs Division ; Board on Global Health, Institute of Medicine ; Institute of Medicine and National Research Council of the National (2006). Globalization, biosecurity, and the future of the life sciences. Washington, D.C.: National Academies Press. ISBN   0-309-65418-1.{{cite book}}: |first1= has generic name (help)CS1 maint: multiple names: authors list (link)[ verification needed ]
  11. ↑ "Google Scholar: "PJ Olsiewski"" . Retrieved Aug 10, 2016.
  12. ↑ "MIT ALUMNI ASSOCIATION HENRY B. KANE '24 AWARD WINNERS" (PDF). Retrieved February 24, 2017.
  13. ↑ "MIT ALUMNI ASSOCIATION BRONZE BEAVER AWARD WINNERS" (PDF). Retrieved February 24, 2017.
  14. ↑ "Yale Class Award Recipients" . Retrieved February 24, 2017.
  15. ↑ "AAAS Honors Accomplished Scientists as 2018 Elected Fellows" . Retrieved November 28, 2018.
  16. ↑ "International Society of Indoor Air Quality and Climate New Academy Fellows" . Retrieved June 28, 2022.
  17. ↑ "International Society of Indoor Air Quality and Climate Special Awards" . Retrieved June 28, 2022.
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