Buchumschlag

Concentration‐dependent mutational scanning probes the cellular folding landscape of α‐synuclein in yeast

Fuente: Wiley Open Access

Gespeichert in:

Bibliographische Detailangaben
Hauptverfasser:	Daeun Noh, Robert W. Newberry
Format:	Artículo Open Access
Veröffentlicht:	Wiley 2026
Schlagworte:	Protein Science
Online-Zugang:	Acceder al recurso
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Ähnliche Einträge

Backbone double‐mutant cycle analysis quantifies hydrogen‐bond energies in proteins
von: Haoliang Zheng, et al.
Veröffentlicht: (2026)

Copper ion incorporation in α‐synuclein amyloids
von: Gulshan Walke, et al.
Veröffentlicht: (2024)

Amyloid formation of alternatively spliced variants of α‐synuclein
von: Daniel Q. SanGiovanni, et al.
Veröffentlicht: (2025)

In silico peptide self‐assembly reveals the importance of N‐terminal motifs and the inhibition mechanism of the mutation L38M in α ‐synuclein fibrillation
von: Van T. T. Nguyen, et al.
Veröffentlicht: (2026)

Competing chaperone pathways in α‐synuclein disaggregation and aggregation dynamics
von: Nicola K. Auld, et al.
Veröffentlicht: (2025)

Structural insights into the unique recognition module between α‐synuclein peptide and nanobody
von: Zeyaul Islam, et al.
Veröffentlicht: (2024)

The effects of biological crowders on fibrillization, structure, diffusion, and conformational dynamics of α‐synuclein
von: Sina Heravi, et al.
Veröffentlicht: (2024)

Specific inhibition of α‐synuclein oligomer generation and toxicity by the chaperone domain Bri2 BRICHOS
von: Laurène Adam, et al.
Veröffentlicht: (2024)

The role of phospholipid saturation and composition in α‐synuclein aggregation and toxicity: A dual in vitro and in vivo approach
von: Aidan P. Holman, et al.
Veröffentlicht: (2025)

The structural landscape of the immunoglobulin fold by large‐scale de novo design
von: Jorge Roel‐Touris, et al.
Veröffentlicht: (2024)

Mapping the energy landscape of a fold‐switching protein MAD2
von: Ander F. Pereira, et al.
Veröffentlicht: (2025)

Understanding the stability landscape of LbCas12a by deep analysis of stabilizing mutations and mutation combinations
von: Jiajun Dong, et al.
Veröffentlicht: (2025)

Heterogeneous folding landscapes and predetermined breaking points within a protein family
von: Sebastian Pechmann
Veröffentlicht: (2024)

Correction to “The structural landscape of the immunoglobulin fold by large‐scale de novo design”
Veröffentlicht: (2025)

Complete combinatorial mutational enumeration of a protein functional site enables sequence‐landscape mapping and identifies highly‐mutated variants that retain activity
von: Mireia Solà Colom, et al.
Veröffentlicht: (2024)

Defining short linear motif binding determinants by phage display‐based deep mutational scanning
von: Caroline Benz, et al.
Veröffentlicht: (2025)

Synonymous and non‐synonymous codon substitutions can alleviate dependence on GroEL for folding
von: Tali Haviv Reingewertz, et al.
Veröffentlicht: (2024)

Multivalent interaction induces phase separation and formation of more toxic aggregates of α‐syn in a yeast model of Parkinson's disease
von: Rajeev Jain, et al.
Veröffentlicht: (2025)

NumSimEX: A method using EXX hydrogen exchange mass spectrometry to map the energetics of protein folding landscapes
von: Jasper A. G. Flint, et al.
Veröffentlicht: (2025)

The role of the nucleus in the control of mitochondrial precursor proteins in yeast
von: Kira Ritzenhofen, et al.
Veröffentlicht: (2026)

An ALS ‐associated mutation in the C‐terminal α‐helix of TDP ‐43 uncouples condensate formation and amyloid assembly
von: Emily J. Byrd, et al.
Veröffentlicht: (2026)

Design of a yeast SUMO tag to eliminate internal translation initiation
von: Jamison D. Law, et al.
Veröffentlicht: (2024)

AlphaFold2's training set powers its predictions of some fold‐switched conformations
von: Joseph W. Schafer, et al.
Veröffentlicht: (2025)

Selection of nanobodies against liponanoparticle‐embedded membrane proteins by yeast‐surface display
von: Greg J. Dodge, et al.
Veröffentlicht: (2025)

Predicting absolute protein folding stability using generative models
von: Matteo Cagiada, et al.
Veröffentlicht: (2024)

Novel insights into the assembly of the yeast translation initiation multifactor complex: The critical role of eIF5
von: Borja Sáez de la Fuente, et al.
Veröffentlicht: (2026)

Structural and functional specialization of Bordetella pertussis DsbA for pertussis toxin folding
von: Stephanie Penning, et al.
Veröffentlicht: (2025)

Glycopolymers stabilize protein folding and protein–protein interactions via enthalpic interactions
von: Sabrina M. Richter, et al.
Veröffentlicht: (2025)

Molecular mechanisms of chaperone‐directed protein folding: Insights from atomistic simulations
von: Matteo Castelli, et al.
Veröffentlicht: (2024)

Expanding the biocatalytic and oxidative landscape of the old yellow enzyme family
von: David W. White, et al.
Veröffentlicht: (2025)

Investigating operational stability and causes of cofactor release in fold type I amine transaminase
von: Xuebin Feng, et al.
Veröffentlicht: (2026)

Direct comparison of the structural dynamics between spontaneous and ligand‐induced folding of staphylococcal nuclease
von: Yujiro Mori, et al.
Veröffentlicht: (2025)

In vitro, cellular and in vivo studies of amyloid oligomers structure and toxicity: Challenges and advances
von: Magdalena I. Ivanova, et al.
Veröffentlicht: (2026)

Weak, specific chemical interactions dictate barnase stability in diverse cellular environments
von: Ume Tahir, et al.
Veröffentlicht: (2025)

A functional and structural comparative analysis of large tumor antigens reveals evolution of different importin α‐dependent nuclear localization signals
von: Emily M. Cross, et al.
Veröffentlicht: (2024)

Computational studies on the functional and structural impact of pathogenic mutations in enzymes
von: Upeksha C. Dissanayake, et al.
Veröffentlicht: (2025)

Viral envelope proteins fused to multiple distinct fluorescent reporters to probe receptor binding
von: Ilhan Tomris, et al.
Veröffentlicht: (2024)

Intermediate heterogeneity modulates coupling between chain compaction and structure formation during protein folding
von: Anushka Kaushik, et al.
Veröffentlicht: (2026)

The double histone fold: Structure, functional implications across the tree of life and relevance to protein design
von: Anna Ranaudo, et al.
Veröffentlicht: (2026)

Proline variants in the BRCA1 coiled‐coil domain disrupt folding and binding to PALB2
von: Chrissy N. S. Baker, et al.
Veröffentlicht: (2024)