Institution
Manipal University
Education•Manipal, Karnataka, India•
About: Manipal University is a education organization based out in Manipal, Karnataka, India. It is known for research contribution in the topics: Population & Medicine. The organization has 9525 authors who have published 11207 publications receiving 110687 citations.
Topics: Population, Medicine, Computer science, Health care, Cancer
Papers published on a yearly basis
Papers
More filters
••
TL;DR: The antibacterial, antiviral, and antifungal activities of different types of tea and their polyphenols are reported, highlighting their mechanisms of action and structure–activity relationship.
121 citations
••
TL;DR: There is a significant decrease in growth rate and increased doubling time of cases because of the lockdown, and social distancing is a critical means to break the cycle of infection.
120 citations
••
TL;DR: It is demonstrated that PTEN attenuates epidermal growth factor receptor (EGFR) signalling by promoting late endosome maturation by virtue of its protein phosphatase activity.
Abstract: Tumour suppressor phosphatase and tensin homologue deleted on chromosome 10 (PTEN) is a lipid phosphatase that negatively regulates growth factor-induced survival signalling. Here, we demonstrate that PTEN attenuates epidermal growth factor receptor (EGFR) signalling by promoting late endosome maturation by virtue of its protein phosphatase activity. Loss of PTEN impairs the transition of ligand-bound EGFR from early to late endosomes. We unveil Rab7, a critical GTPase for endosome maturation, as a functional PTEN interacting partner. PTEN dephosphorylates Rab7 on two conserved residues S72 and Y183, which are necessary for GDP dissociation inhibitor (GDI)-dependent recruitment of Rab7 on to late endosomes and subsequent maturation. Thus, our findings reveal PTEN-dependent endosome maturation through phosphoregulation of Rab7 as an important route of controlling EGFR signalling.
120 citations
••
TL;DR: It is shown that synapses contain LLPs that may underlie stabile long-lasting changes in synaptic structure and function, which support a potential role for them in synaptic plasticity and learning and memory.
Abstract: Memory formation is believed to result from changes in synapse strength and structure. While memories may persist for the lifetime of an organism, the proteins and lipids that make up synapses undergo constant turnover with lifetimes from minutes to days. The molecular basis for memory maintenance may rely on a subset of long-lived proteins (LLPs). While it is known that LLPs exist, whether such proteins are present at synapses is unknown. We performed an unbiased screen using metabolic pulse-chase labeling in vivo in mice and in vitro in cultured neurons combined with quantitative proteomics. We identified synaptic LLPs with half-lives of several months or longer. Proteins in synaptic fractions generally exhibited longer lifetimes than proteins in cytosolic fractions. Protein turnover was sensitive to pharmacological manipulations of activity in neuronal cultures or in mice exposed to an enriched environment. We show that synapses contain LLPs that may underlie stabile long-lasting changes in synaptic structure and function.
119 citations
••
TL;DR: It is shown that Rv1988, a secreted mycobacterial protein, is a functional methyltransferase that localizes to the host nucleus and interacts with chromatin that methylates histone H3 at H3R42 and represses the genes involved in the first line of defence againstMycobacteria.
Abstract: Mycobacteria are successful pathogens that modulate the host immune response through unclear mechanisms. Here we show that Rv1988, a secreted mycobacterial protein, is a functional methyltransferase that localizes to the host nucleus and interacts with chromatin. Rv1988 methylates histone H3 at H3R42 and represses the genes involved in the first line of defence against mycobacteria. H3R42me2, a non-tail histone modification, is present at the entry and exit point of DNA in the nucleosome and not within the regulatory sites in the N-terminal tail. Rv1988 deletion in Mycobacterium tuberculosis reduces bacterial survival in the host, and experimental expression of M. tuberculosis Rv1988 in non-pathogenic Mycobacterium smegmatis negatively affects the health of infected mice. Thus, Rv1988 is an important mycobacterial virulence factor, which uses a non-canonical epigenetic mechanism to control host cell transcription.
118 citations
Authors
Showing all 9740 results
Name | H-index | Papers | Citations |
---|---|---|---|
John J.V. McMurray | 178 | 1389 | 184502 |
Ashok Kumar | 151 | 5654 | 164086 |
Zhanhu Guo | 128 | 886 | 53378 |
Vijay P. Singh | 106 | 1699 | 55831 |
Michael Walsh | 102 | 963 | 42231 |
Akhilesh Pandey | 100 | 529 | 53741 |
Vivekanand Jha | 94 | 958 | 85734 |
Manuel Hidalgo | 92 | 538 | 41330 |
Madhukar Pai | 89 | 522 | 33349 |
Ravi Kumar | 82 | 571 | 37722 |
Vijay V. Kakkar | 60 | 470 | 17731 |
G. Münzenberg | 58 | 336 | 9837 |
Abhishek Sharma | 52 | 426 | 9715 |
Ramesh R. Bhonde | 49 | 223 | 8397 |
Chandra P. Sharma | 48 | 325 | 12100 |