Results 21 to 30 of about 707,163 (239)

A Bibliometric Analysis of Publications in Uremic Toxins From 1991 to 2024

open access: yesTherapeutic Apheresis and Dialysis, EarlyView.
ABSTRACT Background Uremic toxins are a growing area of research in nephrology, with significant implications in the progression and treatment of chronic kidney disease (CKD) and the management of end‐stage kidney disease (ESKD). This bibliometric analysis aims to evaluate the global research trends, key contributors, and the impact of publications in ...
Yuh‐Shan Ho   +7 more
wiley   +1 more source

p97 Disease Mutations Modulate Nucleotide-Induced Conformation to Alter Protein-Protein Interactions. [PDF]

open access: yes, 2016
The AAA+ ATPase p97/VCP adopts at least three conformations that depend on the binding of ADP and ATP and alter the orientation of the N-terminal protein-protein interaction (PPI) domain into up and down conformations.
Arkin, Michelle   +2 more
core  

Designability of lattice model heteropolymers

open access: yes, 2001
Protein folds are highly designable, in the sense that many sequences fold to the same conformation. In the present work we derive an expression for the designability in a 20 letter lattice model of proteins which, relying only on the Central Limit ...
A. Sali   +28 more
core   +1 more source

Enteropathogenic E. coli shows delayed attachment and host response in human jejunum organoid‐derived monolayers compared to HeLa cells

open access: yesFEBS Letters, EarlyView.
Enteropathogenic E. coli (EPEC) infects the human intestinal epithelium, resulting in severe illness and diarrhoea. In this study, we compared the infection of cancer‐derived cell lines with human organoid‐derived models of the small intestine. We observed a delayed in attachment, inflammation and cell death on primary cells, indicating that host ...
Mastura Neyazi   +5 more
wiley   +1 more source

Is protein folding problem really a NP-complete one ? First investigations

open access: yes, 2013
To determine the 3D conformation of proteins is a necessity to understand their functions or interactions with other molecules. It is commonly admitted that, when proteins fold from their primary linear structures to their final 3D conformations, they ...
Bahi, Jacques M.   +3 more
core   +3 more sources

Exploring the Levinthal limit in protein folding [PDF]

open access: yes, 2017
According to the thermodynamic hypothesis, the native state of proteins is uniquely defined by their amino acid sequence. On the other hand, according to Levinthal, the native state is just a local minimum of the free energy and a given amino acid ...
B Fazi   +23 more
core   +1 more source

Hidden conformations in protein structures [PDF]

open access: yesBioinformatics, 2011
Abstract Motivation: Prediction of interactions between protein residues (contact map prediction) can facilitate various aspects of 3D structure modeling. However, the accuracy of ab initio contact prediction is still limited. As structural genomics initiatives move ahead, solved structures of homologous proteins can be used as multiple ...
Haim Ashkenazy, Ron Unger, Yossef Kliger
openaire   +2 more sources

Organoids in pediatric cancer research

open access: yesFEBS Letters, EarlyView.
Organoid technology has revolutionized cancer research, yet its application in pediatric oncology remains limited. Recent advances have enabled the development of pediatric tumor organoids, offering new insights into disease biology, treatment response, and interactions with the tumor microenvironment.
Carla Ríos Arceo, Jarno Drost
wiley   +1 more source

Folding and Misfolding of Designed Heteropolymer Chains with Mutations

open access: yes, 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.   +4 more
core   +2 more sources

Reciprocal control of viral infection and phosphoinositide dynamics

open access: yesFEBS Letters, EarlyView.
Phosphoinositides, although scarce, regulate key cellular processes, including membrane dynamics and signaling. Viruses exploit these lipids to support their entry, replication, assembly, and egress. The central role of phosphoinositides in infection highlights phosphoinositide metabolism as a promising antiviral target.
Marie Déborah Bancilhon, Bruno Mesmin
wiley   +1 more source

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