Results 101 to 110 of about 2,744,502 (279)

Long-Range Entropic Effects on Protein Intrinsically Disordered Regions [PDF]

open access: yes, 2019
Entropy calculations represent one of the most challenging steps in obtaining the binding free energy in proteins and their complexes, which is a grand challenge in computational biology.
Agnieszka K., Bronowska   +3 more
core   +1 more source

Heterotropic regulation and negative homotropic cooperativity

open access: yesFEBS Open Bio, EarlyView.
We identified a structural module common to some proteins that couple negative cooperativity with heterotropic regulation, two features that rarely coexist. These proteins are ring‐like and present an ordered asymmetry whereby noncontacting subunits are symmetric, and their tertiary structure differs from that of contacting subunits.
Veronica Morea   +5 more
wiley   +1 more source

Protein order and disorder: A quantitative in silico analysis [PDF]

open access: yesEPJ Web of Conferences
Proteins are fundamental biological macromolecules responsible for a wide range of cellular functions. Traditionally, a central paradigm linked the amino acid sequence to a unique, ordered three-dimensional structure that underlies biological activity ...
de Brevern Alexandre G.
doaj   +1 more source

Cell surface CD11c as a neutrophil aging marker molecule

open access: yesFEBS Open Bio, EarlyView.
Cell surface CD11chi neutrophils were more aged and had better phagocytic function than CD11c−/lo neutrophils. Transcriptomic analysis of CD11chi neutrophils and CD11c−/lo neutrophils in pediatric population showed that the most difference was seen in infants.
Sophia Koutsogiannaki   +5 more
wiley   +1 more source

Sequence complexity of amyloidogenic regions in intrinsically disordered human proteins.

open access: yesPLoS ONE, 2014
An amyloidogenic region (AR) in a protein sequence plays a significant role in protein aggregation and amyloid formation. We have investigated the sequence complexity of AR that is present in intrinsically disordered human proteins.
Swagata Das   +6 more
doaj   +1 more source

The C‐terminal domain of yeast Arginyltransferase1 is essential for its catalytic activity

open access: yesFEBS Open Bio, EarlyView.
Arginyltransferase 1 (Ate1), a eukaryotic enzyme, catalyses arginylation, transferring arginine from tRNA‐Arg to the amino terminus of the target protein. Overexpression of Ate1 in yeast is lethal and is dependent on arginylation. This study elucidates how mutations in the cofactor‐binding and active site of Ate1 and truncation of its structural ...
Vikas Kumar Yadav   +4 more
wiley   +1 more source

Rapid evolution of virus sequences in intrinsically disordered protein regions.

open access: yesPLoS Pathogens, 2014
Nodamura Virus (NoV) is a nodavirus originally isolated from insects that can replicate in a wide variety of hosts, including mammals. Because of their simplicity and ability to replicate in many diverse hosts, NoV, and the Nodaviridae in general ...
Leonid Gitlin   +4 more
doaj   +1 more source

MARK4 enhances stress granule formation under oxidative stress and increases tau accumulation

open access: yesFEBS Open Bio, EarlyView.
MARK4 (red dots) localizes to stress granules (orange dots) and promotes their formation under oxidative stress by modulating TIA1 (blue dots). MARK4 and TIA1 synergistically increase tau (purple) accumulation, and the reduction of the TIA1 ortholog suppresses neurodegeneration in a fly model.
Sho Nakajima   +8 more
wiley   +1 more source

Discovery of short linear motif-mediated interactions through phage display of intrinsically disordered regions of the human proteome.

open access: yes, 2016
The intrinsically disordered regions of eukaryotic proteomes are enriched in short linear motifs (SLiMs), which are of crucial relevance for cellular signaling and protein regulation; many mediate interactions by providing binding sites for peptide ...
Yadav, V.
core   +1 more source

The hinge region of type VII collagen is intrinsically disordered

open access: yesMatrix Biology, 2014
Type VII collagen (Col7) is important for skin integrity. As a major component of the anchoring fibrils, Col7 is essential for linking different skin layers together. The central collagenous domain of Col7 contains several interruptions of the collagen triple helix.
Richer, Barbara Christine   +1 more
openaire   +2 more sources

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