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Monita Muralidharan

Researcher at St. John's University

Publications -  21
Citations -  927

Monita Muralidharan is an academic researcher from St. John's University. The author has contributed to research in topics: Hemoglobin & Glycation. The author has an hindex of 8, co-authored 19 publications receiving 560 citations. Previous affiliations of Monita Muralidharan include University of California, San Francisco.

Papers
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Journal ArticleDOI

The Global Phosphorylation Landscape of SARS-CoV-2 Infection.

Mehdi Bouhaddou, +77 more
- 06 Aug 2020 - 
TL;DR: A quantitative mass spectrometry-based phosphoproteomics survey of SARS-CoV-2 infection in Vero E6 cells reveals dramatic rewiring of phosphorylation on host and viral proteins, revealing potential COVID-19 therapies.
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Proteomic Approaches to Study SARS-CoV-2 Biology and COVID-19 Pathology.

TL;DR: In this article, the authors discuss how the proteomic research community can leverage technologies and expertise to address the pandemic by investigating four key areas of study in SARS-CoV-2 biology.
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Conformational heterogeneity of tau: Implication on intrinsic disorder, acid stability and fibrillation in Alzheimer's disease.

TL;DR: The observations at low pH indicate that a reorganization of the intricate network of momentary long-range contacts in tau might have implication in its aggregation pathology, and nano-electrospray mass spectrometry coupled with ion mobility provides a direct insight into the ensemble of highly heterogeneous conformational families of tau at physiological pH.
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Beneficiary effect of nanosizing ferric pyrophosphate as food fortificant in iron deficiency anemia: evaluation of bioavailability, toxicity and plasma biomarker

TL;DR: The nanoparticle ferric pyrophosphate could be a promising food fortificant in combating iron deficiency anemia, while Fetuin-B, a negative acute phase protein, might be a potential candidate for detecting biological responses to the nanoparticle exposure in vivo.
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Glutathionylation induced structural changes in oxy human hemoglobin analyzed by backbone amide hydrogen/deuterium exchange and MALDI-mass spectrometry.

TL;DR: This study investigated the effects of glutathionylation on quaternary structure of hemoglobin using hydrogen/deuterium exchange (H/DX) based mass spectrometry to understand structural perturbation on post-translational modification of proteins in solution phase.