
Praveen kumar patnaikBoston University | BU · Department of Dermatology
Praveen kumar patnaik
Doctor of Philosophy
About
6
Publications
20,016
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18
Citations
Introduction
Additional affiliations
Education
July 2010 - June 2012
Publications
Publications (6)
Iron is an essential trace element that serves as a cofactor for enzymes involved in multiple metabolic pathways, including ribosome biogenesis, protein translation, DNA synthesis and repair, lipid metabolism, and mitochondrial oxidative phosphorylation. In eukaryotes, iron deficiency leads to coordinated changes in gene expression and protein tran...
Iron dyshomeostasis contributes to aging, but little information is available about the molecular mechanisms.
Here, we provide evidence that in Saccharomyces cerevisiae, aging is associated with altered expression of
genes involved in iron homeostasis. We further demonstrate that defects in the conserved mRNA-binding
protein Cth2, which controls st...
Iron dyshomeostasis contributes to aging, but little information is available about the molecular mechanisms. Here, we provide evidence that, in Saccharomyces cerevisiae, aging is associated with altered expression of genes involved in iron homeostasis. We further demonstrate that defects in the conserved mRNA-binding protein Cth2, which controls s...
Lung cancer is considered the deadliest type of
cancer for humans and is often diagnosed at the incurable
stage. Till now, no effective methods for early diagnosis and
treatment of lung cancer have been developed. This short
paper presents preliminary studies on millimeter-wave
(MMW) effect on yeast cells. It is well known that yeasts are
represent...
Apoptosis, a form of programmed cell death, is a highly regulated process, the deregulation of which has been associated with the tumor initiation, progression, and metastasis in various cancers including breast cancer. Induction of apoptosis is a popular target of various therapies currently being tested or used for breast cancer treatment. Thus,...
Questions
Questions (16)
Dear all RG members,
We are working on a project which deals with the functionality of one of the genes in yeast. We wanted to transform a single copy plasmid containing our gene of interest into the deletion strain of that particular gene in order to study its role. Can any one suggest me single copy or very low copy shuttle vectors (bacteria/yeast) that I can use for my work.
Thank you.
I would like to know is it possible to ligate incompatible overhangs formed at 5/ and 3/ end of plasmid.
Dear fellow scientists,
I am working with a GFP labelled protein in yeast. I would like to take movies of that particular protein for following its location throughout cell cycle by fluorescence microscopy. When I am using Olympus fluorescent microscope, after 2-3 minutes the fluorescent intensity is getting decreased. Is there any specific microscope with which I can take longer movies without losing fluorescence intensity?.
I am studying mRNA regulation using U1A-GFP labelling system. I wanted to study RNA binding proteins associated with gene of my interest. Can anyone suggest me the best method to immunoprecipitate mRNA in yeast?
I am working on kinases in budding yeast. I need Mata, snf1 kinase deletion strain for my studies. It would be grate if anyone can give me the strain.
Thanks in advance.
How can I arrest the budding yeast in a particular cellcycle stage without leading the cell to stress? I want to study mRNA at individual cell cycle stage of budding yeast. For that the cells shouldnot go under any stress, since stress leads the mRNA granules to move to P-bodies. SO please suggest me how to arrest budding yeast to a particular cell cycle stage.
Thank you for your time.
Does any one have any idea about the protocol to stain nucleus with Hoechst 33342 in yeast cells?
My protein of interest is getting functional upon the oxidation. I would like to know its status in cytosol to know its role in cytosol.
I would like to study the position of a protein in a stress condition. So with which method I can possibly know the position of that protein in a nucleus?