Dhurvas Chandrasekaran Dinesh (0000-0001-9125-4775)

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Experienced postdoctoral researcher (awarded title Dr. rer. nat. in Biochemistry from Martin Luther University Halle-Wittenberg, Germany) in the field of protein structural biology & biochemistry, with a track record of accomplishments at prestigious research institutes. Currently working a Marie Skłodowska-Curie Actions (MSCA) postdoctoral fellow at the Department of Medical Biochemistry and Biophysics, Umeä University, Sweden.

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Umeå Universitet: Umeå, Västerbotten, SE

2025-04-01 to 2027-03-31 | Marie Skłodowska-Curie Actions (MSCA) Postdoctoral Fellow (Medical Biochemistry and Biophysics)

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Dhurvas Chandrasekaran Dinesh

https://orcid.org/0000-0001-9125-4775

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Biography

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Employment (4)

Umeå Universitet: Umeå, Västerbotten, SE

Institute of Organic Chemistry and Biochemistry: Prague, CZ

UF Scripps Biomedical Research: Jupiter, FL, US

Indian Institute of Science Bangalore: Bangalore, Karnataka, IN

Education and qualifications (5)

Leibniz Institute of Plant Biochemistry: Halle, Saxony-Anhalt, DE

Madurai Kamaraj University: Madurai, Tamil Nadu, IN

Dr GR Damodaran College of Science: Coimbatore, Tamil Nadu, IN

Bharathiar University School of Biotechnology and Genetic Engineering: Coimbatore, Tamil Nadu, IN

St Joseph's College of Arts and Science: Cuddalore, Tamil Nadu, IN

Professional activities (3)

Alagappa University: Karaikudi, Tamil Nadu, IN

St Joseph's College of Arts and Science: Cuddalore, Tamil Nadu, IN

St Joseph's College of Arts and Science: Cuddalore, Tamil Nadu, IN

Works (14)

Type II JAK2 Inhibitor CHZ‐868 and HSP90 Inhibitors Are Potent towards the Ruxolitinib Resistant JAK2 Variants in JAK2 Driven Myeloproliferative Neoplasms

SARS-CoV-2 ORF8 dimerization and binding mode analysis with class I MHC: computational approaches to identify COVID-19 inhibitors

Model of abasic site DNA cross-link repair; from the architecture of NEIL3 DNA binding domains to the X-structure model

Structural Understanding of SARS-CoV-2 Drug Targets, Active Site Contour Map Analysis and COVID-19 Therapeutics.

An in silico molecular dynamics simulation study on the inhibitors of SARS-CoV-2 proteases (3CLpro and PLpro) to combat COVID-19

Structure-based virtual screening and molecular dynamics simulation of SARS-CoV-2 Guanine-N7 methyltransferase (nsp14) for identifying antiviral inhibitors against COVID-19

High-Throughput Screening and Quantum Mechanics for Identifying Potent Inhibitors Against Mac1 Domain of SARS-CoV-2 Nsp3

Structural basis of RNA recognition by the SARS-CoV-2 nucleocapsid phosphoprotein

Microsecond MD Simulation and Multiple-Conformation Virtual Screening to Identify Potential Anti-COVID-19 Inhibitors Against SARS-CoV-2 Main Protease.

Antiviral Drug Targets of Single-Stranded RNA Viruses Causing Chronic Human Diseases

Structural Biology of Nuclear Auxin Action.

Iron-dependent callose deposition adjusts root meristem maintenance to phosphate availability.

Solution structure of the PsIAA4 oligomerization domain reveals interaction modes for transcription factors in early auxin response.

Arabidopsis calmodulin-binding protein IQ67-domain 1 localizes to microtubules and interacts with kinesin light chain-related protein-1.

Peer review (3 reviews for 2 publications/grants)