Giri Raj Dahal

ORCID: 0000-0003-1255-2761
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About
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Research Areas
  • Neurobiology and Insect Physiology Research
  • Cell death mechanisms and regulation
  • Developmental Biology and Gene Regulation
  • Protein purification and stability
  • Neuropeptides and Animal Physiology
  • DNA Repair Mechanisms
  • Viral Infectious Diseases and Gene Expression in Insects
  • Receptor Mechanisms and Signaling
  • CRISPR and Genetic Engineering
  • Wnt/β-catenin signaling in development and cancer
  • Endoplasmic Reticulum Stress and Disease
  • RNA and protein synthesis mechanisms
  • Inflammasome and immune disorders
  • Marine Biology and Environmental Chemistry
  • dental development and anomalies
  • Protein Kinase Regulation and GTPase Signaling
  • Bacterial Genetics and Biotechnology
  • Invertebrate Immune Response Mechanisms
  • Erythrocyte Function and Pathophysiology
  • Ion channel regulation and function
  • Monoclonal and Polyclonal Antibodies Research
  • Animal Behavior and Reproduction

University of Colorado Denver
2017-2019

The Medical Center of Aurora
2019

Duke Medical Center
2017

Brigham Young University
2012

Chosun University
2007-2008

Mutations that disrupt function of the human inwardly rectifying potassium channel KIR2.1 are associated with craniofacial and digital defects Andersen-Tawil Syndrome, but contribution Kir channels to development is undefined. Deletion mouse Kir2.1 also causes cleft palate defects. These strikingly similar phenotypes result from disrupted TGFβ/BMP signaling. We use Drosophila melanogaster show a homolog, Irk2, affects by disrupting BMP Phenotypes irk2 deficient lines, mutant allele, siRNA...

10.1242/dev.078592 article EN Development 2012-09-04

Abstract The β 1 adrenergic receptor (β AR) is recognized as a classical Gα s -coupled receptor. Agonist binding not only initiates G protein-mediated signaling but also through the multifunctional adapter protein β-arrestin. Some βAR ligands, such carvedilol, stimulate preferentially β-arrestin, concept known β-arrestin-biased agonism. Here, we identify mechanism, unlike that previously for any receptor, whereby carvedilol induces transition of AR from to i stabilizing distinct conformation...

10.1038/s41467-017-01855-z article EN cc-by Nature Communications 2017-11-16

Loss of embryonic ion channel function leads to morphological defects, but the underlying reason for these defects remains elusive. Here, we show that inwardly rectifying potassium (Irk) channels regulate release Drosophila bone morphogenetic protein Dpp in developing fly wing and this is necessary developmental signaling. Inhibition Irk decreases incidence distinct Dpp-GFP events above baseline fluorescence while leading a broader distribution Dpp-GFP. Work by others different cell types...

10.1242/dev.146647 article EN Development 2017-07-07

During morphogenesis, cells communicate with each other to shape tissues and organs. Several lines of recent evidence indicate that ion channels play a key role in cellular signaling tissue morphogenesis. However, little is known about the scope specific ion-channel types impinge upon developmental pathways. The Drosophila melanogaster wing an excellent model which address this problem as vein patterning acutely sensitive changes We conducted screen 180 expressed using loss-of-function...

10.1534/g3.119.400028 article EN cc-by G3 Genes Genomes Genetics 2019-02-08

Proteins and peptides expressed in the prokaryotic system often form inclusion bodies. Solubilization refolding procedures can be used for their recovery, but this process remains difficult. One strategy improving solubility of a protein interest is to fuse it highly soluble protein. To select suitable fusion partner capable solubilizing aggregation-prone (inclusion body–forming) proteins peptides, Escherichia coli thermostable were identified tested. Among them, trigger factor (TF) was...

10.2144/000112728 article EN BioTechniques 2008-05-01

10.1016/j.bbrc.2007.03.102 article EN Biochemical and Biophysical Research Communications 2007-03-27

The activity of caspase-2 was examined under varying biochemical conditions with the synthetic and protein substrates, Bid procaspase-7. results indicate that it largely influenced by pH which might be one reason behind inconsistency for cleavage its established substrates during caspase-2-induced apoptosis.

10.2174/092986608786071193 article EN Protein and Peptide Letters 2008-10-01
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