R
Ravi P. Yadav
Researcher at Roy J. and Lucille A. Carver College of Medicine
Publications - 21
Citations - 350
Ravi P. Yadav is an academic researcher from Roy J. and Lucille A. Carver College of Medicine. The author has contributed to research in topics: Chaperone (protein) & Visual phototransduction. The author has an hindex of 9, co-authored 21 publications receiving 260 citations. Previous affiliations of Ravi P. Yadav include Institute of Medical Sciences, Banaras Hindu University & Banaras Hindu University.
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Journal ArticleDOI
Atomic resolution view into the structure-function relationships of the human myelin peripheral membrane protein P2.
Salla Ruskamo,Ravi P. Yadav,Satyan Sharma,M. Lehtimaki,Saara Laulumaa,Shweta Aggarwal,Mikael Simons,Jochen Bürck,Anne S. Ulrich,André H. Juffer,Inari Kursula,Petri Kursula +11 more
TL;DR: The structure of the human myelin peripheral membrane protein P2 has been refined at 0.93 Å resolution in combination with functional experiments in vitro, in vivo and in silico and fine details of the structure–function relationships in P2 are emerging.
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Neriifolin S, a dimeric serine protease from Euphorbia neriifolia Linn.: Purification and biochemical characterisation.
TL;DR: A dimeric serine protease Neriifolin S of molecular mass 94kDa with milk clotting activity has been purified from the latex of Euphorbia neriifolia by anion exchange and size-exclusion chromatography and is fairly stable toward chemical denaturants, pH and temperature.
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Purification and biochemical characterization of a chymotrypsin-like serine protease from Euphorbia neriifolia Linn.
TL;DR: A high ratio of milk-clotting activity to proteolytic activity as well as stability against variations in pH and temperature, surfactants, oxidizing agents and compatibility with detergent additives make neriifolin an excellent candidate for industrial applications.
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Structure of the dimeric autoinhibited conformation of DAPK2, a pro-apoptotic protein kinase.
TL;DR: The crystal and solution structures of murine DAPK2 in the presence of the autoinhibitory domain are determined, and it is indicated that the dimers of D APK2 are indeed formed through the association of two apposed catalytic domains, as seen in the crystal structure.
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Aryl hydrocarbon receptor-interacting protein-like 1 is an obligate chaperone of phosphodiesterase 6 and is assisted by the γ-subunit of its client.
TL;DR: It is demonstrated that AIPL1 is an obligate chaperone of PDE6 and that it enables low yield functional folding of cone PDE 6C in cultured cells, and it is shown that the AipL1-mediated production of folded PDE7C is markedly elevated in the presence of the inhibitory Pγ-subunit of Pde6.