Results 101 to 110 of about 1,962,138 (310)

Oligomeric protein structure networks: insights into protein-protein interactions

open access: yesBMC Bioinformatics, 2005
Background Protein-protein association is essential for a variety of cellular processes and hence a large number of investigations are being carried out to understand the principles of protein-protein interactions.
Brinda KV, Vishveshwara Saraswathi
doaj   +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

Epigenetic blind spots – the role of DNA methylation dynamics in stem cell‐based models of embryogenesis

open access: yesFEBS Letters, EarlyView.
Embryo‐like structures (stembryos) are an innovative tool, but they are hindered by experimental variability and limited developmental potential. DNA methylation is crucial for mammalian development, but its status in stembryo models is poorly characterized.
Sara Canil   +4 more
wiley   +1 more source

pH‐mediated activation of the lysosomal arginine sensor SLC38A9

open access: yesFEBS Letters, EarlyView.
Cells monitor nutrient levels via the lysosomal transporter SLC38A9 to activate the mechanistic target of rapamycin complex 1 (mTORC1). This study reveals that SLC38A9 function is regulated by pH. We identified histidine 544 as a critical pH sensor that undergoes conformational changes to control amino acid efflux from lysosomes; therefore, it ...
Xuelang Mu, Ampon Sae Her, Tamir Gonen
wiley   +1 more source

Protein-protein interactions (PPIs) of Radix Scutellariae-Licorice herb pair.

open access: yes, 2023
Protein-protein interactions (PPIs) of Radix Scutellariae-Licorice herb pair.
Mengxin Yang (10684155)   +7 more
core   +1 more source

Biophysical approaches for studying viral entry

open access: yesFEBS Letters, EarlyView.
Viruses infect all living organisms and have been responsible for major epidemics and pandemics. Their ongoing evolutionary battle with host defenses creates a constant need for improved tools to study viral behavior. Advancing methods to probe viral attachment, fusion, and genome release deepen our understanding of how infections begin and support the
Inbar Yosibash, Raya Sorkin
wiley   +1 more source

Dancing with the Diva: Hsp90-Client Interactions

open access: yes, 2018
The molecular chaperone Hsp90 is involved in the folding, maturation, and degradation of a large number structurally and sequentially unrelated clients, often connected to serious diseases.
Sub Cellular Protein Chemistry   +4 more
core   +1 more source

The human gut microbiome across the life course

open access: yesFEBS Letters, EarlyView.
Despite significant individual variation and continuous change throughout life, the human gut microbiome follows some life stage‐specific trends. This article provides a brief overview of how gut microbiome composition shifts across different phases of life. Created in BioRender. Özkurt, E. (2026) https://BioRender.com/8q4nrnc.
Alise J. Ponsero   +4 more
wiley   +1 more source

Protein Docking mit weichen Volumenmodellen

open access: yes, 2003
Neumann S. Soft volume models for protein-protein docking. Bielefeld (Germany): Bielefeld University; 2003.Der Begriff "Protein Docking" beschreibt die Frage, ob und wie zwei gegebene Proteine interagieren, ausgehend von der 3D Struktur.
Neumann, Steffen
core  

Examining post-translational modification-mediated protein-protein interactions using a chemical proteomics approach

open access: yes, 2013
Post-translational modifications (PTM) of proteins can control complex and dynamic cellular processes via regulating interactions between key proteins.
Foley, E   +13 more
core   +1 more source

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