<?xml version="1.0" encoding="utf-8" standalone="yes"?><rss version="2.0" xmlns:atom="http://www.w3.org/2005/Atom"><channel><title>Casian Veselin - HTBAA 2026 spring :: 2026a-casian-veselin</title><link>https://pages.htgaa.org/2026b/casian-veselin/index.html</link><description>About me ⋆✴︎˚｡⋆ 11th grade highschool student in Romania&#10;I really love biology and the sciences that make it up, be it molecular dynamics, organic chemistry, systems biology or even evolution. At the moment, neurobiology, endocrinology and bioinformatics are my focus.&#10;✦ I love art.. probably listening to music right now&#10;☣︎ Founder of BioNexTim.</description><generator>Hugo</generator><language>en</language><atom:link href="https://pages.htgaa.org/2026b/casian-veselin/index.xml" rel="self" type="application/rss+xml"/><item><title>Homework</title><link>https://pages.htgaa.org/2026b/casian-veselin/homework/index.html</link><pubDate>Mon, 01 Jan 0001 00:00:00 +0000</pubDate><guid>https://pages.htgaa.org/2026b/casian-veselin/homework/index.html</guid><description>Weekly homework submissions: Week 1 HW: project ideas</description></item><item><title>Labs</title><link>https://pages.htgaa.org/2026b/casian-veselin/labs/index.html</link><pubDate>Mon, 01 Jan 0001 00:00:00 +0000</pubDate><guid>https://pages.htgaa.org/2026b/casian-veselin/labs/index.html</guid><description>Lab writeups:</description></item><item><title>Final Project</title><link>https://pages.htgaa.org/2026b/casian-veselin/final-project/index.html</link><pubDate>Mon, 01 Jan 0001 00:00:00 +0000</pubDate><guid>https://pages.htgaa.org/2026b/casian-veselin/final-project/index.html</guid><description>I. Abstract Prions are misfolded proteins that exhibit ‘infectious’-like behaviour and are the root cause for multiple prion protein associated neurodiseases: Creutzfeldt–Jakob Disease, Kuru (not exclusively in humans) and Scrapie and Bovine spongiform encephalopathy (BSE, mad-cow disease) characteristically affecting ovines and bovines respectively.&#10;In humans, the gene PrPC encodes for the premature version of the cellular prion protein (253-a.a. long) found within neuroglia and neurons, its function and role remain ambiguous and have not been described fully (or so it is believed). After post-translational modification in the endoplasmic reticulum, the precursor protein loses its N-terminal signal peptide (1-22) and C-terminal signal peptide (232-253) and carries on as a mature, functional PrPC surface glycoprotein that is 208-209 residues long. Faulty folding or interaction with other midfolded prion proteins can lead the native cellular variant of the protein to display a different structure and, thus, behaviour: resulting isoform is called PrPSc (scrapie-associated prion protein).</description></item></channel></rss>