K Yamano, AI Fogel, C Wang, AM van der Bliek… - Elife, 2014 - elifesciences.org
Damaged mitochondria can be selectively eliminated by mitophagy. Although two gene products mutated in Parkinson's disease, PINK1, and Parkin have been found to play a …
AI Duarte, E Candeias, IN Alves, D Mena… - International journal of …, 2020 - mdpi.com
Alzheimer's disease (AD) is the most common form of dementia worldwide, being characterized by the deposition of senile plaques, neurofibrillary tangles (enriched in the …
KA Nolden, MC Harwig, RB Hill - Journal of Biological Chemistry, 2023 - ASBMB
Mitochondrial fission protein 1 (Fis1) and dynamin-related protein 1 (Drp1) are the only two proteins evolutionarily conserved for mitochondrial fission, and directly interact in …
JM Egner, KA Nolden, MC Harwig, RP Bonate… - Journal of Biological …, 2022 - ASBMB
Fission protein 1 (FIS1) and dynamin-related protein 1 (DRP1) were initially described as being evolutionarily conserved for mitochondrial fission, yet in humans the role of FIS1 in …
UK Ihenacho, R Toro, RH Mansour, RB Hill - Journal of Biological …, 2023 - ASBMB
Mitochondrial fission protein 1 (FIS1) is conserved in all eukaryotes, yet its function in metazoans is thought divergent. Structure-based sequence alignments of FIS1 revealed a …
Motivation The remodeling of short fragment (s) of the protein backbone to accommodate new function (s), fine-tune binding specificities or change/create novel protein interactions is …
M Koppenol-Raab, MC Harwig, AE Posey… - Journal of Biological …, 2016 - ASBMB
The tail-anchored protein Fis1 is implicated as a passive tether in yeast mitochondrial fission. We probed the functional role of Fis1 Glu-78, whose elevated side chain pK a …
H Ghasriani, JKC Kwok, AR Sherratt, ACY Foo… - Biochemistry, 2014 - ACS Publications
Three-dimensional domain swapping is a mode of self-interaction that can give rise to altered functional states and has been identified as the trigger event in some protein …
AL Bakkum, RB Hill - Protein Science, 2017 - Wiley Online Library
Tetratricopeptide repeat (TPR) domains are ubiquitous protein interaction domains that adopt a modular antiparallel array of α‐helices. The TPR fold typically adopts a monomeric …