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Neela H. Yennawar
Researcher at Pennsylvania State University
Publications - 59
Citations - 1980
Neela H. Yennawar is an academic researcher from Pennsylvania State University. The author has contributed to research in topics: Branched chain aminotransferase & Active site. The author has an hindex of 20, co-authored 53 publications receiving 1580 citations. Previous affiliations of Neela H. Yennawar include Wake Forest University.
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Journal ArticleDOI
Crystal structure and activities of EXPB1 (Zea m 1), a β-expansin and group-1 pollen allergen from maize
Neela H. Yennawar,Lian-Chao Li,David M. Dudzinski,David M. Dudzinski,Akira Tabuchi,Daniel J. Cosgrove +5 more
TL;DR: In this paper, the authors determined the structure of EXPB1 by x-ray crystallography to 2.75-A resolution and proposed a model of expansin action, which facilitates the local movement and stress relaxation of arabinoxylan-cellulose networks within the wall by noncovalent rearrangement of its target.
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Transaminase inhibition by 2-hydroxyglutarate impairs glutamate biosynthesis and redox homeostasis in glioma
Samuel K. McBrayer,Jared R. Mayers,Gabriel J. DiNatale,Diana D. Shi,Januka Khanal,Abhishek A. Chakraborty,Kristopher A. Sarosiek,Kimberly J. Briggs,Alissa Robbins,Tomasz Sewastianik,Sarah J. Shareef,Sarah J. Shareef,Benjamin A. Olenchock,Seth J. Parker,Kensuke Tateishi,Kensuke Tateishi,Jessica B. Spinelli,Jessica B. Spinelli,Mirazul Islam,Mirazul Islam,Marcia C. Haigis,Ryan E. Looper,Keith L. Ligon,Bradley E. Bernstein,Bradley E. Bernstein,Ruben D. Carrasco,Ruben D. Carrasco,Daniel P. Cahill,John M. Asara,Christian M. Metallo,Neela H. Yennawar,Matthew G. Vander Heiden,Matthew G. Vander Heiden,William G. Kaelin,William G. Kaelin +34 more
TL;DR: It is found that (R)-2HG potently inhibits the 2OG-dependent transaminases BCAT1 and BCAT2, likely as a bystander effect, thereby decreasing glutamate levels and increasing dependence on glutaminase for the biosynthesis of glutamate and one of its products, glutathione.
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Structural basis for methyl transfer by a radical SAM enzyme
Amie K. Boal,Tyler L. Grove,Monica I. McLaughlin,Neela H. Yennawar,Squire J. Booker,Amy C. Rosenzweig +5 more
TL;DR: RlmN accomplishes its complex reaction with structural economy, harnessing the two most important reactivities of SAM within a single site to methylate RNA.
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Structural basis for entropy-driven cellulose binding by a type-A cellulose-binding module (CBM) and bacterial expansin
TL;DR: The molecular target of expansin and the specific molecular interactions of a type-A CBM with cellulose are clarified and a unique form of ligand-mediated dimerization is revealed, with the oligosaccharide sandwiched between two D2 domains in opposite polarity.
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X-ray crystal structure of gamma -chymotrypsin in hexane
TL;DR: The electron density for the peptide bound in the active site has been dramatically altered in hexane and appears to be tetrahedral at the carbon that is covalently bound to Ser 195.