Arshdeep Sidhu

ORCID: 0000-0002-2851-1019
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About
Contact & Profiles
Research Areas
  • Parkinson's Disease Mechanisms and Treatments
  • Alzheimer's disease research and treatments
  • DNA Repair Mechanisms
  • CRISPR and Genetic Engineering
  • Supramolecular Self-Assembly in Materials
  • Prion Diseases and Protein Misfolding
  • Glycosylation and Glycoproteins Research
  • Aortic Disease and Treatment Approaches
  • Advanced Fluorescence Microscopy Techniques
  • Botulinum Toxin and Related Neurological Disorders
  • Enzyme Structure and Function
  • Bone Tissue Engineering Materials
  • Neurological diseases and metabolism
  • Aortic aneurysm repair treatments
  • Cardiac Health and Mental Health
  • RNA and protein synthesis mechanisms
  • RNA Research and Splicing
  • Signaling Pathways in Disease
  • Force Microscopy Techniques and Applications
  • Ubiquitin and proteasome pathways
  • Protein Structure and Dynamics
  • Peptidase Inhibition and Analysis
  • Quantum Dots Synthesis And Properties
  • Viral Infectious Diseases and Gene Expression in Insects
  • Advanced Electron Microscopy Techniques and Applications

University of British Columbia
2025

University of the Fraser Valley
2024

Nitte University
2022

University Health Network
2022

Erasmus MC
2018-2021

Erasmus MC Cancer Institute
2021

Oncode Institute
2021

University of Twente
2014-2018

National Institute of Immunology
2011

Thioflavin-T (ThT) is the most commonly used fluorescent dye for following amyloid formation semi-quantitatively in vitro, specifically probing fibrillar cross-β-sheet content. In recent years, structural polymorphism of fibrils has been shown to be an important aspect formation, both vitro and neurodegenerative diseases. Therefore, understanding ThT-amyloid interactions context amyloids necessary correct interpretation ThT fluorescence data. Here we study influence fibril morphology on...

10.1080/13506129.2018.1517736 article EN cc-by-nc-nd Amyloid 2018-07-03

Amyloid polymorphs have become one of the focal points molecular studies neurodegenerative diseases like Parkinson's disease. Due to their distinct biochemical properties and prion-like characteristics, insights into origin stability amyloid over time are crucial for understanding potential role polymorphism in these diseases. Here, we systematically study fibrillization recombinantly produced human α-synuclein (αSyn) an extended period unravel temporal evolution polymorphism. We follow...

10.1021/acschemneuro.6b00287 article EN publisher-specific-oa ACS Chemical Neuroscience 2016-11-16

10.1016/j.bbapap.2014.09.007 article EN Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 2014-09-16

Abstract The formation of α-synuclein (α-S) amyloid aggregates, called Lewy bodies (LBs), is a hallmark Parkinson’s disease (PD). function LBs in the process however still unclear; they have been associated with both neuroprotection and toxicity. To obtain insight into this contradiction, we induced α-S inclusions, using three different induction methods SH-SY5Y cells rat-derived primary neuronal cells. Using confocal STED microscopy observed induction-dependent differences inclusion...

10.1038/srep23116 article EN cc-by Scientific Reports 2016-03-17

Under aggregation-prone conditions, soluble amyloidogenic protein monomers can self-assemble into fibrils or they fibrillize on preformed fibrillar seeds (seeded aggregation). Seeded aggregations are known to propagate the morphology of in event cross-seeding. However, not all proteins cross-seed aggregation. Cross-seeding has been proposed be restricted either because differences sequences conformations between and monomers. Here, we examine cross-seeding efficiency three α-synuclein...

10.1021/acschemneuro.5b00322 article EN publisher-specific-oa ACS Chemical Neuroscience 2016-03-19

Breast cancer type two susceptibility protein (BRCA2) is an essential in genome maintenance, homologous recombination (HR), and replication fork protection. Its function includes multiple interaction partners requires timely localization to relevant sites the nucleus. We investigated importance of highly conserved DNA-binding domain (DBD) C-terminal (CTD) BRCA2. generated BRCA2 variants missing one or both domains mouse embryonic stem (ES) cells defined their contribution HR dynamic nucleus,...

10.7554/elife.67926 article EN cc-by eLife 2021-07-13

A new approach to sample preparation and enzymatic digestion in bottom-up proteomics has been developed using alginate-based hydrogel entrapment of enzymes. This facilitates rapid room-temperature digestions with multienzyme capabilities. Three methodologies were tested: within microcentrifuge tubes,

10.1021/acs.analchem.4c04846 article EN cc-by-nc-nd Analytical Chemistry 2024-11-11

BRCA2 is a key breast cancer associated protein that predicted to have interspersed regions of intrinsic disorder. Intrinsic disorder coupled with large size likely allows sample broad range conformational space. We expect the resulting dynamic arrangements domains are functionally important aspect its role in homologous recombination DNA repair. To determine architectural organization and landscape BRCA2, we used scanning force microscopy based single molecule analyses map flexible...

10.1093/nar/gkaa648 article EN cc-by-nc Nucleic Acids Research 2020-08-07

Abstract BRCA2 is an essential protein in genome maintenance, homologous recombination and replication fork protection. Its function includes multiple interaction partners requires timely localization to relevant sites the nucleus. We investigated importance of highly conserved DNA binding domain (DBD) C-terminal (CTD) BRCA2. generated variants missing one or both domains mouse ES cells defined their contribution HR dynamic nucleus, by single particle tracking mobility. Changes molecular...

10.1101/2021.03.02.433541 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2021-03-02
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