Sadhana A Samant
Overview
Explore the profile of Sadhana A Samant including associated specialties, affiliations and a list of published articles.
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13
Citations
730
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Recent Articles
1.
Samant S, Pillai V, Gupta M
JCSM Rapid Commun
. 2021 Jul;
4(1):40-56.
PMID: 34212132
Background: During cancer cachexia, cytokines released from tumour cells can alter body's metabolism, which can lead to onset of this disease process. Biological basis of cachexia is multifactorial; hence, it...
2.
Samant S, Pillai V, Gupta M
Can J Physiol Pharmacol
. 2018 Nov;
97(4):235-245.
PMID: 30407871
Many chronic diseases are associated with unintentional loss of body weight, which is termed "cachexia". Cachexia is a complex multifactorial syndrome associated with the underlying primary disease, and characterized by...
3.
Samant S, Kanwal A, Pillai V, Bao R, Gupta M
Sci Rep
. 2017 Sep;
7(1):11877.
PMID: 28928419
Muscle wasting, also known as cachexia, is associated with many chronic diseases, which worsens prognosis of primary illness leading to enhanced mortality. Molecular basis of this metabolic syndrome is not...
4.
Samant S, Pillai V, Sundaresan N, Shroff S, Gupta M
J Biol Chem
. 2015 Apr;
290(25):15559-15569.
PMID: 25911107
Reversible lysine acetylation is a widespread post-translational modification controlling the activity of proteins in different subcellular compartments. We previously demonstrated that a class II histone deacetylase (HDAC), HDAC4, and a...
5.
Samant S, Zhang H, Hong Z, Pillai V, Sundaresan N, Wolfgeher D, et al.
Mol Cell Biol
. 2013 Dec;
34(5):807-19.
PMID: 24344202
Mitochondrial morphology is regulated by the balance between two counteracting mitochondrial processes of fusion and fission. There is significant evidence suggesting a stringent association between morphology and bioenergetics of mitochondria....
6.
Pillai V, Sundaresan N, Samant S, Wolfgeher D, Trivedi C, Gupta M
Mol Cell Biol
. 2011 Mar;
31(11):2349-63.
PMID: 21444723
Like phosphorylation, acetylation of lysine residues within a protein is considered a biologically relevant modification that controls the activity of target proteins. During stress of cells, massive protein acetylation takes...
7.
Samant S, Courson D, Sundaresan N, Pillai V, Tan M, Zhao Y, et al.
J Biol Chem
. 2010 Dec;
286(7):5567-77.
PMID: 21177250
Reversible lysine acetylation is a widespread post-translational modification controlling the activity of proteins in different subcellular compartments. We previously demonstrated that a class II histone deacetylase (HDAC), HDAC4, and a...
8.
Kim G, Samant S, Earley J, Svensson E
PLoS One
. 2009 Jul;
4(7):e6161.
PMID: 19582148
MicroRNAs are increasingly being recognized as regulators of embryonic development; however, relatively few microRNAs have been identified to regulate cardiac development. FOG-2 (also known as zfpm2) is a transcriptional co-factor...
9.
Sundaresan N, Samant S, Pillai V, Rajamohan S, Gupta M
Mol Cell Biol
. 2008 Aug;
28(20):6384-401.
PMID: 18710944
There are seven SIRT isoforms in mammals, with diverse biological functions including gene regulation, metabolism, and apoptosis. Among them, SIRT3 is the only sirtuin whose increased expression has been shown...
10.
Gupta M, Samant S, Smith S, Shroff S
J Biol Chem
. 2008 Feb;
283(15):10135-46.
PMID: 18250163
Reversible acetylation of lysine residues within a protein is considered a biologically relevant modification that rivals phosphorylation ( Kouzarides, T. (2000) EMBO J. 19, 1176-1179 ). The enzymes responsible for...