Results 71 to 80 of about 95,914 (208)

Protein Misfolding and Aggregation as a Therapeutic Target for Polyglutamine Diseases

Brain Sciences, 2017
The polyglutamine (polyQ) diseases, such as Huntington’s disease and several types of spinocerebellar ataxias, are a group of inherited neurodegenerative diseases that are caused by an abnormal expansion of the polyQ tract in disease-causative proteins ...
Toshihide Takeuchi, Yoshitaka Nagai
doaj   +1 more source

Folding and Misfolding of Designed Heteropolymer Chains with Mutations

, 1997
We study the impact of mutations (changes in amino acid sequence) on the thermodynamics of simple protein-like heteropolymers consisting of N monomers, representing the amino acid sequence. The sequence is designed to fold into its native conformation on
Broglia, R. A., Roman, H. E., Shakhnovich, E., Tiana, G., Vigezzi, E.   +4 more
core   +2 more sources

Protein Misfolding and Neurodegenerative Diseases [PDF]

International Journal of Cell Biology, 2014
This special issue includes fifteen reviews and two original research articles by leading scientists in the fields of neuropathology, biochemistry, and cell biology, dealing with the role of protein aggregation and prion-like propagation of protein misfolding in neurodegenerative diseases.
Alessio Cardinale, Roberto Chiesa, Michael Sierks   +2 more
openaire   +3 more sources

Molecular Lysine Tweezers Counteract Aberrant Protein Aggregation. [PDF]

, 2019
Molecular tweezers (MTs) are supramolecular host molecules equipped with two aromatic pincers linked together by a spacer (Gakh, 2018). They are endowed with fascinating properties originating from their ability to hold guests between their aromatic ...
Bitan, Gal, Hadrovic, Inesa, Klärner, Frank-Gerrit, Rebmann, Philipp, Schrader, Thomas   +4 more
core  

Aggregation of the amyloid-β peptide (Aβ40) within condensates generated through liquid–liquid phase separation

Scientific Reports
The deposition of the amyloid-β (Aβ) peptide into amyloid fibrils is a hallmark of Alzheimer’s disease. Recently, it has been reported that some proteins can aggregate and form amyloids through an intermediate pathway involving a liquid-like condensed ...
Owen M. Morris, Zenon Toprakcioglu, Alexander Röntgen, Mariana Cali, Tuomas P. J. Knowles, Michele Vendruscolo   +5 more
doaj   +1 more source

TOM40 Mediates Mitochondrial Dysfunction Induced by α-Synuclein Accumulation in Parkinson's Disease. [PDF]

, 2013
Alpha-synuclein (α-Syn) accumulation/aggregation and mitochondrial dysfunction play prominent roles in the pathology of Parkinson's disease. We have previously shown that postmortem human dopaminergic neurons from PD brains accumulate high levels of ...
A Bender, A Iwai, AB Singleton, AD Roses, AH Schapira, AH Schapira, AK Reeve, Andreas Bender, Andrew O. Koob, Anthony Adame, B Spencer, Brian Spencer, C Meisinger, Christoph Laub, D Bruno, DA Clayton, DD Song, E Masliah, Edward Rockenstein, Eliezer Masliah, Emily Pham, F Fornai, H Yamamoto, IG Zigoneanu, JQ Trojanowski, K Pennington, KJ Krishnan, L Devi, L Devi, L He, L Mucke, L Naldini, LA Bindoff, LJ Martin, M Hashimoto, M Manczak, MA McFarland, Matthias Elstner, MF Beal, MG Spillantini, MH Polymeropoulos, Michael Mante, MS Chong, MS Parihar, P Klivenyi, Paula Desplats, Philipp J. Kahle, R Banerjee, R Kruger, R Scherz-Shouval, RA Marr, S Totterdell, Sarina Mueller, SM Toggas, Thomas Klopstock, U Shirendeb, V Choubey, VM Mann, W Dauer, WW Li, Y Kraytsberg   +60 more
core   +3 more sources

AlphaFold prediction of structural ensembles of disordered proteins

Nature Communications
Deep learning methods of predicting protein structures have reached an accuracy comparable to that of high-resolution experimental methods. It is thus possible to generate accurate models of the native states of hundreds of millions of proteins.
Z. Faidon Brotzakis, Shengyu Zhang, Mhd Hussein Murtada, Michele Vendruscolo   +3 more
doaj   +1 more source

Proteostasis collapse is a driver of cell aging and death. [PDF]

, 2019
What molecular processes drive cell aging and death? Here, we model how proteostasis-i.e., the folding, chaperoning, and maintenance of protein function-collapses with age from slowed translation and cumulative oxidative damage.
de Graff, Adam MR, Dill, Ken A, Santra, Mantu   +2 more
core  

RNA misfolding and the action of chaperones [PDF]

Frontiers in Bioscience, 2008
RNA folds to a myriad of three-dimensional structures and performs an equally diverse set of functions. The ability of RNA to fold and function in vivo is all the more remarkable because, in vitro, RNA has been shown to have a strong propensity to adopt misfolded, non-functional conformations.
openaire   +2 more sources

Prediction of protein biophysical traits from limited data: a case study on nanobody thermostability through NanoMelt

mAbs
In-silico prediction of protein biophysical traits is often hindered by the limited availability of experimental data and their heterogeneity. Training on limited data can lead to overfitting and poor generalizability to sequences distant from those in ...
Aubin Ramon, Mingyang Ni, Olga Predeina, Rebecca Gaffey, Patrick Kunz, Shimobi Onuoha, Pietro Sormanni   +6 more
doaj   +1 more source