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Ramamoorthy Siva

Researcher at VIT University

Publications -  108
Citations -  2795

Ramamoorthy Siva is an academic researcher from VIT University. The author has contributed to research in topics: Gene & Mutant. The author has an hindex of 25, co-authored 102 publications receiving 2040 citations. Previous affiliations of Ramamoorthy Siva include Ben-Gurion University of the Negev.

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The amazing potential of fungi: 50 ways we can exploit fungi industrially

Kevin D. Hyde, +69 more
- 03 Jul 2019 - 
TL;DR: This manuscript reviews fifty ways in which fungi can potentially be utilized as biotechnology and provides a flow chart that can be used to convince funding bodies of the importance of fungi for biotechnological research and as potential products.
Journal Article

Status of natural dyes and dye-yielding plants in India

Ramamoorthy Siva
- 01 Jan 2007 - 
TL;DR: The availability of natural dyes, their extraction, applications, mordant types, advantages and disadvantages, and their extraction and dyeing technique in India are reviewed.
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Integrative Bioinformatics Approaches to Map Potential Novel Genes and Pathways Involved in Ovarian Cancer.

TL;DR: This study identified the most relevant biological networks involving DEGs that were mainly enriched in the cell cycle (in metaphase checkpoints) and revealed the role of APC in cell cycle regulation pathways.
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Dysregulation of Signaling Pathways Due to Differentially Expressed Genes From the B-Cell Transcriptomes of Systemic Lupus Erythematosus Patients - A Bioinformatics Approach.

TL;DR: Four genes (EGR1, CD38, CAV1, and AKT1) were identified to be strongly associated with SLE and might serve as potential biomarkers in early diagnosis and as therapeutic targets for SLE.
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Influence of V54M mutation in giant muscle protein titin: a computational screening and molecular dynamics approach

TL;DR: The deleterious mutant V54M was mapped, modeled the mutant protein complex, and deciphered the impact of mutation on binding with its partner telethonin in the titin crystal structure of PDB ID: 1YA5 with the aid of docking analysis to understand the mechanistic action of V 54M mutation in altering the protein structure, dynamics, and stability.