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Full-Text Articles in Structural Biology

G-Quadruplex Dna-Driven Genomic Instability Under Ber Loss, Addison Belick, Claryssa Gutierrez, Joslynn Rosas, Andrea Vargas Apr 2026

G-Quadruplex Dna-Driven Genomic Instability Under Ber Loss, Addison Belick, Claryssa Gutierrez, Joslynn Rosas, Andrea Vargas

Posters - 2026

Base Excision Repair (BER) is a cellular tool that can repair damaged DNA (Hindi et al., 2022, Cellular and Molecular Life Sciences). G-quadruplexes (G4s) are unique 4-stranded structures in DNA or RNA that are rich in guanine (Gray et al., 2023, Nat. Chem. Biol). The purpose of this study is to understand whether BER contributes to the removal of G4s in DNA. This will determine if the BER-deficient yeast is more sensitive to treatment with G4-binding drugs than the BER-proficient yeast. We will replace the APN1 gene in the yeast genome with the URA3 gene, because the wild type yeast …


Investigating Rad14 Gene Nucleotide Excision Repair On G-Quadruplexes, Juan Pablo Olvera Rodriguez, Tyna Trevino, Yvette Gonzalez, Georgia Romike Apr 2026

Investigating Rad14 Gene Nucleotide Excision Repair On G-Quadruplexes, Juan Pablo Olvera Rodriguez, Tyna Trevino, Yvette Gonzalez, Georgia Romike

Posters - 2026

DNA is typically found as a double-stranded helical structure; however, it can be found in different types of structures, such as G-quadruplexes (G4s). These are structures formed when DNA sequences are rich in Guanines, which interact with each other by hydrogen bonding, forming stacked G-tetrads. These guanine-rich structures are known for interacting with DNA during important cell processes, such as recombination and replication, leading to instability and DNA damage (Grey et al., 2014). If not treated properly, these structures may contribute to mutations and cancer development. To solve these issues, cells have developed maintenance pathways such as Nucleotide Excision Repair …


D101n: A Unique And Ill-Understood Familial Als-Related Sod1 Mutant, Analisa Lott Dec 2024

D101n: A Unique And Ill-Understood Familial Als-Related Sod1 Mutant, Analisa Lott

Honors Program Theses and Research Projects

Background: Amyotrophic Lateral Sclerosis (ALS) is a fatal neurodegenerative disease, with 90% of documented cases considered sporadic and about 10% showing a hereditary link; such cases are deemed as familial ALS (fALS). Superoxide dismutase (SOD), a copper-zinc binding enzyme that protects cells from damaging free radicals, has been linked to fALS with certain toxic gain of function mutations, such as the D101N mutant. The human SOD1 D101N mutant has been shown to be associated with rapidly progressing neurodegeneration yet is less prone to aggregation than similar mutants, but its deviation from wild-type (WT) SOD1 remains misunderstood.

Objective: Although the D101N …


Expression And Purification Of Domain 1 Of The Cards Toxin, Dylan Andrews, Allison Woods, Ahmad Galaleldeen Apr 2024

Expression And Purification Of Domain 1 Of The Cards Toxin, Dylan Andrews, Allison Woods, Ahmad Galaleldeen

Posters - 2024

Mycoplasma pneumoniae (Mp) is an atypical bacterium that is linked to various respiratory diseases such as walking pneumonia and asthma. Upon infection, Mp produces a 591-aa virulence factor known as Community Acquired Respiratory Distress Syndrome Toxin (CARDS TX). The crystal structure of this 591-aa cytotoxin reveals a triangular molecule comprised of an N-terminal ADP-ribosylating domain and a Cterminal tandem β-trefoil domain that is responsible for vacuolation of the host’s cells. Based on structural and sequence homology to other ADP ribosylating toxins, the NAD+ binding site has been predicted, yet none of the published structures of the CARDS toxin contain NAD+. …


Purifying The Human Rna-Lariat Debranching Enzyme, Ammar Saigal Dec 2013

Purifying The Human Rna-Lariat Debranching Enzyme, Ammar Saigal

Honors Program Theses and Research Projects

This project is my first official research endeavor and it involved becoming acquainted with a large variety of biochemistry and molecular biology techniques. The goal is to elucidate the structure of a protein common to most if not all cells of organisms within the Domain Eukarya, which is one of the three taxonomic domains into which all life is categorized. This is the domain most relevant to human beings as it includes plants, fungi, and animals (from a strictly biologically-taxonomic perspective, the species Homo sapiens to which you and I belong is considered belonging to the Kingdom Animalia [Animal]).