Folding and misfolding of human membrane proteins in health and disease: from single molecules to cellular proteostasis

JT Marinko, H Huang, WD Penn, JA Capra… - Chemical …, 2019 - ACS Publications
Advances over the past 25 years have revealed much about how the structural properties of
membranes and associated proteins are linked to the thermodynamics and kinetics of …

[HTML][HTML] Limitations and challenges in protein stability prediction upon genome variations: towards future applications in precision medicine

T Sanavia, G Birolo, L Montanucci, P Turina… - Computational and …, 2020 - Elsevier
Protein stability predictions are becoming essential in medicine to develop novel
immunotherapeutic agents and for drug discovery. Despite the large number of …

Loss-of-function, gain-of-function and dominant-negative mutations have profoundly different effects on protein structure

L Gerasimavicius, BJ Livesey, JA Marsh - Nature communications, 2022 - nature.com
Most known pathogenic mutations occur in protein-coding regions of DNA and change the
way proteins are made. Taking protein structure into account has therefore provided great …

PremPS: Predicting the impact of missense mutations on protein stability

Y Chen, H Lu, N Zhang, Z Zhu, S Wang… - PLoS computational …, 2020 - journals.plos.org
Computational methods that predict protein stability changes induced by missense
mutations have made a lot of progress over the past decades. Most of the available methods …

ProThermDB: thermodynamic database for proteins and mutants revisited after 15 years

R Nikam, A Kulandaisamy, K Harini… - Nucleic acids …, 2021 - academic.oup.com
ProThermDB is an updated version of the thermodynamic database for proteins and mutants
(ProTherm), which has∼ 31 500 data on protein stability, an increase of 84% from the …

Rapid protein stability prediction using deep learning representations

LM Blaabjerg, MM Kassem, LL Good, N Jonsson… - Elife, 2023 - elifesciences.org
Predicting the thermodynamic stability of proteins is a common and widely used step in
protein engineering, and when elucidating the molecular mechanisms behind evolution and …

DUET: a server for predicting effects of mutations on protein stability using an integrated computational approach

DEV Pires, DB Ascher, TL Blundell - Nucleic acids research, 2014 - academic.oup.com
Cancer genome and other sequencing initiatives are generating extensive data on non-
synonymous single nucleotide polymorphisms (nsSNPs) in human and other genomes. In …

Predicting and interpreting large-scale mutagenesis data using analyses of protein stability and conservation

MH Høie, M Cagiada, AHB Frederiksen, A Stein… - Cell reports, 2022 - cell.com
Understanding and predicting the functional consequences of single amino acid changes is
central in many areas of protein science. Here, we collect and analyze experimental …

WS-SNPs&GO: a web server for predicting the deleterious effect of human protein variants using functional annotation

E Capriotti, R Calabrese, P Fariselli, PL Martelli… - BMC genomics, 2013 - Springer
Background SNPs&GO is a method for the prediction of deleterious Single Amino acid
Polymorphisms (SAPs) using protein functional annotation. In this work, we present the web …

Solvent accessibility of residues undergoing pathogenic variations in humans: from protein structures to protein sequences

C Savojardo, M Manfredi, PL Martelli… - Frontiers in molecular …, 2021 - frontiersin.org
Solvent accessibility (SASA) is a key feature of proteins for determining their folding and
stability. SASA is computed from protein structures with different algorithms, and from protein …