Results 101 to 110 of about 3,579,241 (217)

Self-organization of intrinsically disordered proteins with folded N-termini [PDF]

, 2010
Thousands of human proteins lack recognizable tertiary structure in most of their chains. Here we hypothesize that some use their structured N-terminal domains (SNTDs) to organise the remaining protein chain via intramolecular interactions, generating ...
Philip C. Simister, Simon McGowan, Nicola O'Reilly, Stephan M. Feller, Fred Schaper   +4 more
core  

α‐Synuclein Aggregate‐Disassembling Compounds Prolong Survival in a Mouse Model of Parkinson's Disease

Aggregate, Volume 7, Issue 9, September 2026.
All‐D peptides that bind monomeric α‐synuclein shift the aggregation equilibrium, dismantle pathogenic fibrils, and suppress seeding activity in vitro and in cells. In a Parkinson's disease mouse model, treatment delays disease progression and extends survival, supporting direct aggregate disassembly as a disease‐modifying therapeutic strategy for ...
Sara Reithofer, Marc Sevenich, Madita Vollmer, Dila Kurtul, Laura Müller, Pelin Özdüzenciler, Laurin Gerhards, Kira Allmeroth, Mathias Wendt, Fahimeh Charbgoo, Sarah Schemmert, Marcel Naumann, Karolina Korostov, Gina Hartmann, Lothar Gremer, Gültekin Tamgüney, Dieter Willbold, Antje Willuweit   +17 more
wiley   +1 more source

Aberrant phase separation from a rare ABI3 mutation drives microglial dysfunction and Alzheimer's risk

Alzheimer's &Dementia, Volume 22, Issue 9, September 2026.
Abstract INTRODUCTION Although the ABI3 S209F variant is a recognized genetic risk for Alzheimer's disease (AD), its pathogenic mechanism remains elusive. METHODS Using AD mouse models (amyloid precursor protein/presenilin 1 [APP/PS1] transgenic mice, 5×familial Alzheimer's disease (5×FAD) transgenic mice) with microglia‐specific knockdown of Abelson ...
Shengnan Li, Jiongtong Lu, Kaixing Zeng, Xingyu Lu, Jiahao Zhang, Sifan Feng, Chunmei Liang, Yujie Cai, Shi Yao, Qing Huang, Guocong Liang, Rui Chen, Li Li, Fubin Ma, Jiawei Xing, Chaoyue Ouyang, Lv Luo, Jiaying Wang, You Li, Shengbo He, Yuanyuan Zhao, Yan Wang, Lili Cui   +22 more
wiley   +1 more source

Nuclear‐Spin Hyperpolarization of Biomolecules by Optically Enhanced NMR at Ultra‐High Field

Journal of the Chinese Chemical Society, Volume 73, Issue 9, Page 1589-1605, September 2026.
This study shows that the sensitivity of liquid‐state NMR spectroscopy can be dramatically increased, with enhancement factors up to 160‐fold on a 1.1 GHz ultra‐high‐field NMR spectrometer. This advance exploits low‐concentration photochemically induced dynamic nuclear polarization (LC‐photo‐CIDNP) and it enables facile atomic‐resolution detection of ...
Ji Ho Jeong, Anubhab Halder, Silvia Cavagnero   +2 more
wiley   +1 more source

Pincus blob elasticity in an intrinsically disordered protein

, 2023
Understanding the dynamic structure of intrinsically disordered proteins (IDPs) is important to deciphering their biological functions. Here, we exploit precision entropic elasticity measurements to infer the conformational behavior of a model IDP ...
Gil Koren, Hoang P. Truong, Ram Avinery, Ian L. Morgan, Omar A. Saleh, Roy Beck   +5 more
core   +1 more source

Sequence‐encoded determinants drive distinct early aggregation pathways and different structural outcomes in PNT1 fibrils across Henipavirus members

Protein Science, Volume 35, Issue 9, September 2026.
Abstract Protein aggregation is increasingly recognized as a biologically relevant process in viral proteins, yet the molecular determinants governing such phenomena remain poorly understood. Intrinsically disordered proteins (IDPs) are ubiquitous in viral proteomes, where conformational plasticity not only enables functional diversity but also permits
Harshita Sawdekar, Julien Mignon, Frank Gondelaud, Anuja Walimbe, Samrat Mukhopadhyay, Joseph Chamieh, Sonia Longhi   +6 more
wiley   +1 more source

Determinants for intrinsically disordered protein recruitment into phase-separated protein condensates

, 2022
Multivalent interactions between amino acid residues of intrinsically disordered proteins (IDPs) drive phase separation of these proteins into liquid condensates, forming various membrane-less organelles in cells.
Jang, Jinyoung, Jung, Yongwon, Song, Daesun, Park, Hyoin, Jo, Yongsang   +4 more
core   +1 more source

EPR in protein science : intrinsically disordered proteins

, 2011
Intrinsically disordered proteins (IDPs) form a unique protein category characterized by the absence of a well-defined structure and by remarkable conformational flexibility.
Drescher, Malte, Malte Drescher
core   +1 more source

Programming Multidomain Peptides With Molecular Frustration Into Biomolecular Condensates

Small, Volume 22, Issue 51, 11 September 2026.
De novo designed multidomain peptides (MDPs) were used to explore how molecular ordering influences peptide phase behavior. MDPs containing partially folded β‐sheets were found to form biomolecular condensates. This work introduces a new design principle for condensate formation and expand the design space beyond conventional intrinsically disordered ...
Debdatta Das, Jenny N. Nguyen, Navneet Sahoo, Chuanye Xiong, Haritha Asokan‐Sheeja, Yan Chang, Raniyah Ali, Eleanor D. Smith, Chad A. Brautigam, Yi Hong, Zui Pan, Peng Tao, He Dong   +12 more
wiley   +1 more source

Self-Assembling Micelles Based on an Intrinsically Disordered Protein Domain [PDF]

, 2018
Herein, we describe a new series of fusion proteins that have been developed to self-assemble spontaneously into stable micelles that are 27 nm in diameter after enzymatic cleavage of a solubilizing protein tag. The sequences of the proteins are based on
Matthew, Francis, Matthew J., Smith, Anthony, Omole, Kenneth, Downing, Jessica, Lee, Sarah, Klass, Tahoe, Fiala   +6 more
core   +2 more sources