Kisun Pokharel

Contact Information:

Kisun Pokharel

Natural Resources Institute Finland (Luke)

Tietotie 4, FI-31600

Jokioinen, Finland

kisun.pokharel@luke.fi

Hello and Namaste! Welcome to my personal website.

I am Kisun Pokharel, originally from Nepal, and I’ve been living, studying, and working in Finland since 2009 when I came here to pursue a Master’s in Bioinformatics. I received my PhD in Genetics from the University of Helsinki in 2020. I am currently working as a Senior Scientist at the Resources Institute Finland (Luke) in Jokioinen, my expertise spans bioinformatics, genomics, and biodiversity. I have made significant contributions to livestock genomics especially focusing on the native breeds/populations of Sheep, Cattle, and Reindeer. I strongly believe that locally adapted populations are valuable genetic resources in the context of population growth and climate change. Therefore, we need to conserve, characterize and sustainably utilize these to safeguard future food security. I have worked with diverse Next-Generation Sequencing (NGS) data across various species, from microbes to livestock and fish, handling both short read and long read sequencing technologies. My recent interests include integrating different omics datasets and exploring the use of AI in genomics.

news

Mar 01, 2024	Rodney Okwasiimire started his PhD project
Jan 22, 2024	Personal Webpage of Kisun Pokharel Launched.
Nov 20, 2020	I defended my PhD

latest posts

Dec 27, 2023	New research on reindeer genomics published
Jul 10, 2023	ISAG Conference in Cape Town, South Africa
Jun 05, 2020	Genomics of Finnish reindeer

selected publications

Whole-genome sequencing provides novel insights into the evolutionary history and genetic adaptation of reindeer populations in northern Eurasia

Kisun Pokharel^*, Melak Weldenegodguad^*, Stephan Dudeck, and 8 more authors

Scientific Reports, 2023

DOI Bib

@article{pokharel_whole-genome_2023,
  dimensions = {true},
  author = {Pokharel, Kisun and Weldenegodguad, Melak and Dudeck, Stephan and Honkatukia, Mervi and Lindeberg, Heli and Mazzullo, Nuccio and Paasivaara, Antti and Peippo, Jaana and Soppela, Päivi and Stammler, Florian and Kantanen, Juha},
  journal = {Scientific Reports},
  number = {1},
  title = {Whole-genome sequencing provides novel insights into the evolutionary history and genetic adaptation of reindeer populations in northern {Eurasia}},
  volume = {13},
  year = {2023},
  doi = {10.1038/s41598-023-50253-7},
}

Integrated ovarian mRNA and miRNA transcriptome profiling characterizes the genetic basis of prolificacy traits in sheep (Ovis aries)

Kisun Pokharel, Jaana Peippo, Mervi Honkatukia, and 8 more authors

BMC Genomics, Jan 2018

Abs DOI

The highly prolific breeds of domestic sheep (Ovis aries) are globally valuable genetic resources for sheep industry. Genetic, nutritional and other environmental factors affect prolificacy traits in sheep. To improve our knowledge of the sheep prolificacy traits, we conducted mRNA-miRNA integrated profiling of ovarian tissues from two pure breeds with large (Finnsheep) vs. small (Texel) litter sizes and their F1 crosses, half of which were fed a flushing diet.
The structure and catalytic cycle of a sodium-pumping pyrophosphatase

Juho Kellosalo, Tommi Kajander, Konstantin Kogan, and 2 more authors

Science (New York, N.Y.), Jul 2012

Abs DOI

Membrane-integral pyrophosphatases (M-PPases) are crucial for the survival of plants, bacteria, and protozoan parasites. They couple pyrophosphate hydrolysis or synthesis to Na(+) or H(+) pumping. The 2.6-angstrom structure of Thermotoga maritima M-PPase in the resting state reveals a previously unknown solution for ion pumping. The hydrolytic center, 20 angstroms above the membrane, is coupled to the gate formed by the conserved Asp(243), Glu(246), and Lys(707) by an unusual "coupling funnel" of six α helices. Comparison with our 4.0-angstrom resolution structure of the product complex suggests that helix 12 slides down upon substrate binding to open the gate by a simple binding-change mechanism. Below the gate, four helices form the exit channel. Superimposing helices 3 to 6, 9 to 12, and 13 to 16 suggests that M-PPases arose through gene triplication.