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Krishnadev Oruganty

Researcher at University of Georgia

Publications -  15
Citations -  750

Krishnadev Oruganty is an academic researcher from University of Georgia. The author has contributed to research in topics: Protein structure & Protein kinase domain. The author has an hindex of 11, co-authored 15 publications receiving 620 citations. Previous affiliations of Krishnadev Oruganty include University of Michigan.

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Journal ArticleDOI

Deciphering the structural basis of eukaryotic protein kinase regulation.

TL;DR: Biochemical and structural analysis of two features of kinase structure, the “R-spine” and “Shell,” afford a detailed insight into the regulation of eukaryotic protein kinases.
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The entropic force generated by intrinsically disordered segments tunes protein function

TL;DR: It is shown that the entropic force produced by an intrinsically disordered carboxy terminus (ID-tail) shifts the conformational ensemble of human UDP-α-d-glucose-6-dehydrogenase (UGDH) towards a substate with a high affinity for an allosteric inhibitor.
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Mitochondrial ADCK3 Employs an Atypical Protein Kinase-like Fold to Enable Coenzyme Q Biosynthesis

TL;DR: It is found that multiple UbiB-specific features are poised to inhibit protein kinase activity, including an N-terminal domain that occupies the typical substrate binding pocket and a unique A-rich loop that limits ATP binding by establishing an unusual selectivity for ADP.
Proceedings ArticleDOI

Relation extraction from clinical texts using domain invariant convolutional neural network

TL;DR: The results indicate that convolution neural network can be a good model for relation exaction in clinical text without being dependent on expert's knowledge on defining quality features.
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The Tribbles 2 (TRB2) pseudokinase binds to ATP and autophosphorylates in a metal-independent manner.

TL;DR: It is reported that the human pseudokinase TRB2 retains the ability to both bind and hydrolyse ATP weakly in vitro and it is established that the nucleotide-binding site of an 'analogue-sensitive'TRB2 mutant can be targeted with specific bulky ligands of the pyrazolo-pyrimidine (PP) chemotype.