Results 81 to 90 of about 6,845,089 (390)

Nanopore Sensing of Protein Folding.

ACS Nano, 2017
Single-molecule studies of protein folding hold keys to unveiling protein folding pathways and elusive intermediate folding states-attractive pharmaceutical targets.
Wei Si, A. Aksimentiev
semanticscholar   +1 more source

Learning inverse folding from millions of predicted structures

bioRxiv, 2022
We consider the problem of predicting a protein sequence from its backbone atom coordinates. Machine learning approaches to this problem to date have been limited by the number of available experimentally determined protein structures.
Chloe Hsu, Robert Verkuil, Jason Liu, Zeming Lin, B. Hie, Tom Sercu, Adam Lerer, Alexander Rives   +7 more
semanticscholar   +1 more source

Mycobacterium tuberculosis sulfurtransferase SseA is activated by its neighboring gene product Rv3284

FEBS Letters, EarlyView.
Tuberculosis remains a global health challenge and new therapeutic targets are required. Here, we characterized SseA, a sulfurtransferase from Mycobacterium tuberculosis involved in macrophage infection, and its interaction with the newly identified protein SufEMtb that activates SseA enzymatic activity.
Giulia Di Napoli, Alex Fissore, Edoardo Salladini, Eleonora Raccuia, Simonetta Oliaro‐Bosso, Alessia Ruggiero, Rita Berisio, Milagros Medina, Adrian Velazquez‐Campoy, Salvatore Adinolfi, Mauro Marengo   +10 more
wiley   +1 more source

Rational design of structure‐based vaccines targeting misfolded alpha‐synuclein conformers of Parkinson's disease and related disorders

Bioengineering & Translational Medicine
Synucleinopathies, including Parkinson's disease (PD), multiple system atrophy (MSA), and dementia with Lewy bodies (DLB), are neurodegenerative disorders caused by the accumulation of misfolded alpha‐synuclein protein.
Jose Miguel Flores‐Fernandez, Verena Pesch, Aishwarya Sriraman, Enrique Chimal‐Juarez, Sara Amidian, Xiongyao Wang, Caleb Duckering, Andrew Fang, Sara Reithofer, Liang Ma, Leonardo M. Cortez, Valerie L. Sim, Gültekin Tamgüney, Holger Wille   +13 more
doaj   +1 more source

Study on the Influence of mRNA, the Genetic Language, on Protein Folding Rates

Frontiers in Genetics, 2021
Many works have reported that protein folding rates are influenced by the characteristics of amino acid sequences and protein structures. However, few reports on the problem of whether the corresponding mRNA sequences are related to the protein folding ...
Ruifang Li, Hong Li, Xue Feng, Ruifeng Zhao, Yongxia Cheng   +4 more
doaj   +1 more source

Reading the three-dimensional structure of a protein from its amino acid sequence

, 2000
While all the information required for the folding of a protein is contained in its amino acid sequence, one has not yet learnt how to extract this information so as to predict the detailed, biological active, three-dimensional structure of a protein ...
Broglia, R. A., Tiana, G.
core   +1 more source

Rubredoxin Variant Folds without Iron [PDF]

, 1999
Pyroccocus furiosus rubredoxin (PFRD), like most studied hyperthermophilic proteins, does not undergo reversible folding. The irreversibility of folding is thought to involve PFRD’s iron-binding site.
Mayo, Stephen L., Strop, Pavel
core   +1 more source

Aβ42 promotes the aggregation of α‐synuclein splice isoforms via heterogeneous nucleation

FEBS Letters, EarlyView.
The aggregation of amyloid‐β (Aβ) and α‐synuclein (αSyn) is associated with Alzheimer's and Parkinson's diseases. This study reveals that Aβ aggregates serve as potent nucleation sites for the aggregation of αSyn and its splice isoforms, shedding light on the intricate interplay between these two pathogenic proteins.
Alexander Röntgen, Zenon Toprakcioglu, Michele Vendruscolo   +2 more
wiley   +1 more source

Flexible protein folding by ant colony optimization [PDF]

, 2008
Protein structure prediction is one of the most challenging topics in bioinformatics. As the protein structure is found to be closely related to its functions, predicting the folding structure of a protein to judge its functions is meaningful to the ...
Hu, X., Li, Y., Zhang, J.
core   +1 more source

Managing the protein folding demands in the endoplasmic reticulum of plants.

New Phytologist, 2016
Endoplasmic reticulum (ER) stress occurs in plants during certain developmental stages or under adverse environmental conditions, as a result of the accumulation of unfolded or misfolded proteins in the ER.
Jian-Xiang Liu, S. Howell
semanticscholar   +1 more source