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Dr Rajan Vyas

vidwan id: 550933
Male

Assistant Professor, Department of Life Sciences
Shiv Nadar University, Gautam Buddha Nagar

Expertise

  • Miscellaneous Biology

Publications

Total Articles 18
Books 0
Proceedings 0

Publications

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Scopus

Citations 489
h-index 11

CrossRef

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Citations 371
h-index 11
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Bio

Life Sciences

Personal Details

  • Male
  • Assistant Professor , Shiv Nadar University, Gautam Buddha Nagar
  • Department of Life Sciences, School of Natural Sciences, Shiv Nadar Institution of Eminence
PhD
Panjab University 2010
Assistant Professor Feb 2020 – Present
Shiv Nadar University, Gautam Buddha Nagar | Department of Life Sciences

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Scholarly Work

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Scholarly Publications

Structural insights into the substrate specificity of SP_0149, the substrate-binding protein of a methionine ABC transporter from Streptococcus pneumoniae

Open Access
Article
Authors: Jha B.;Vyas R.;Bhushan J.;Sehgal D.;Biswal B.K.

The voltage-gated sodium channel pore exhibits conformational flexibility during slow inactivation

Open Access
Article
Authors: Chatterjee S.;Vyas R.;Chalamalasetti S.V.;Sahu I.D.;Clatot J.;Wan X.;Lorigan G.A.;Deschênes I.;Chakrapani S.

Structural basis for the D-stereoselectivity of human DNA polymerase β

Open Access
Article
Authors: Vyas R.;Reed A.J.;Raper A.T.;Zahurancik W.J.;Wallenmeyer P.C.;Suo Z.

Structural insights into the post-chemistry steps of nucleotide incorporation catalyzed by a DNA polymerase

Open Access
Article

VCP recruitment to mitochondria causes mitophagy impairment and neurodegeneration in models of Huntington's disease

Open Access
Article
Authors: Guo X.;Sun X.;Hu D.;Wang Y.J.;Fujioka H.;Vyas R.;Chakrapani S.;Joshi A.U.;Luo Y.;Mochly-Rosen D.;Qi X.

Crystal structures of Mycobacterium tuberculosis HspAT and ArAT reveal structural basis of their distinct substrate specificities

Open Access
Article
Authors: Nasir N.;Anant A.;Vyas R.;Biswal B.K.

Mechanistic Basis for the Bypass of a Bulky DNA Adduct Catalyzed by a Y-Family DNA Polymerase

Open Access
Article

Viewing human DNA polymerase β faithfully and unfaithfully bypass an oxidative lesion by time-dependent crystallography

Open Access
Article