Results 81 to 90 of about 634,315 (303)

cPEPmatch Webserver: A comprehensive tool and database to aid rational design of cyclic peptides for drug discovery

open access: yesComputational and Structural Biotechnology Journal
Cyclic peptides have emerged as versatile scaffolds in drug discovery due to their stability and specificity. Here, we present the cPEPmatch webserver (accessible at https://t38webservices.nat.tum.de/cpepmatch/), an easy-to-use interface for the rational
Brianda L. Santini   +4 more
doaj   +1 more source

Self-Templated Nucleation in Peptide and Protein aggregation

open access: yes, 2008
Peptides and proteins exhibit a common tendency to assemble into highly ordered fibrillar aggregates, whose formation proceeds in a nucleation-dependent manner that is often preceded by the formation of disordered oligomeric assemblies.
Amos Maritan   +5 more
core   +1 more source

Anisotropic Assembly of Colloidal Nanoparticles: Exploiting Substrate Crystallinity [PDF]

open access: yes, 2007
We show that the crystal structure of a substrate can be exploited to drive the anisotropic assembly of colloidal nanoparticles. Pentanethiol-passivated Au particles of approximately 2 nm diameter deposited from toluene onto hydrogen-passivated Si(111 ...
Brust M.   +5 more
core   +2 more sources

Diversity and complexity in neural organoids

open access: yesFEBS Letters, EarlyView.
Neural organoid research aims to expand genetic diversity on one side and increase tissue complexity on the other. Chimeroids integrate multiple donor genomes within single organoids. Self‐organising multi‐identity organoids, exogenous cell seeding, or enforced assembly of region‐specific organoids contribute to tissue complexity.
Ilaria Chiaradia, Madeline A. Lancaster
wiley   +1 more source

Hyperosmotic stress induces PARP1‐mediated HPF1‐dependent mono(ADP‐ribosyl)ation

open access: yesFEBS Letters, EarlyView.
Sorbitol‐induced hyperosmotic stress rapidly induces reversible mono(ADP‐ribosyl)ation (MARylation) on PARP1 without the signs of genotoxic signaling. We show that PARP1 autoMARylation is HPF1 dependent and forms hydroxylamine‐resistant O‐glycosidic linkages.
Anna Georgina Kopasz   +11 more
wiley   +1 more source

Linking neurogenesis, oligodendrogenesis, and myelination defects to neurodevelopmental disruption in primary mitochondrial disorders

open access: yesFEBS Letters, EarlyView.
Mitochondrial remodeling shapes neural and glial lineage progression by matching metabolic supply with demand. Elevated OXPHOS supports differentiation and myelin formation, while myelin compaction lowers mitochondrial dependence, revealing mitochondria as key drivers of developmental energy adaptation.
Sahitya Ranjan Biswas   +3 more
wiley   +1 more source

Organizing the interface—Plasma membrane architecture and receptor dynamics in virus‐cell interactions

open access: yesFEBS Letters, EarlyView.
Plasma membranes contain dynamic nanoscale domains that organize lipids and receptors. Because viruses operate at similar scales, this architecture shapes early infection steps, including attachment, receptor engagement, and entry. Using influenza A virus and HIV‐1 as examples, we highlight how receptor nanoclusters, multivalent glycan interactions ...
Jan Schlegel, Christian Sieben
wiley   +1 more source

Second Set of Spaces [PDF]

open access: yes, 2010
This document describes the Gloss infrastructure supporting implementation of location-aware services. The document is in two parts. The first part describes software architecture for the smart space.
Allen, Ben   +10 more
core   +1 more source

Cartwheel assembly [PDF]

open access: yesPhilosophical Transactions of the Royal Society B: Biological Sciences, 2014
The cartwheel is a subcentriolar structure consisting of a central hub and nine radially arranged spokes, located at the proximal end of the centriole. It appears at the initial stage of the centriole assembly process as the first ninefold symmetrical structure.
openaire   +2 more sources

AAA+ protein unfoldases—the Moirai of the proteome

open access: yesFEBS Letters, EarlyView.
AAA+ unfoldases are essential molecular motors that power protein degradation and disaggregation. This review integrates recent cryo‐electron microscopy (cryo‐EM) structures and single‐molecule biophysical data to reconcile competing models of substrate translocation.
Stavros Azinas, Marta Carroni
wiley   +1 more source

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