Kisun Pokharel

Natural Resources Institute Finland (Luke)

Tietotie 4, FI-31600

Jokioinen, Finland

kisun.pokharel@luke.fi

Welcome to my personal website.

My name is Kisun Pokharel. I work as a Senior Scientist at Natural Resources Institute Finland Luke.

latest posts

May 14, 2024	Google Gemini updates: Flash 1.5, Gemma 2 and Project Astra
Apr 23, 2022	Displaying External Posts on Your al-folio Blog

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.