Results 81 to 90 of about 914,048 (349)
Advances in Structure Modeling Methods for Cryo-Electron Microscopy Maps
Molecules, 2019 Cryo-electron microscopy (cryo-EM) has now become a widely used technique for structure determination of macromolecular complexes. For modeling molecular structures from density maps of different resolutions, many algorithms have been developed.
Eman Alnabati, Daisuke Kihara
doaj +1 more source
Protein–Protein Modeling Using Cryo-EM Restraints [PDF]
, 2020 The recent improvements in cryo-electron microscopy (cryo-EM) in the past few years are now allowing to observe molecular complexes at atomic resolution. As a consequence, numerous structures derived from cryo-EM are now available in the Protein Data Bank. However, if for some complexes atomic resolution is reached, this is not true for all.
Trellet, Mikael +2 more
openaire +4 more sources
Phosphatidylinositol 4‐kinase as a target of pathogens—friend or foe?
FEBS Letters, EarlyView.This graphical summary illustrates the roles of phosphatidylinositol 4‐kinases (PI4Ks). PI4Ks regulate key cellular processes and can be hijacked by pathogens, such as viruses, bacteria and parasites, to support their intracellular replication. Their dual role as essential host enzymes and pathogen cofactors makes them promising drug targets.
Ana C. Mendes +3 more
wiley +1 more source
A simple stochastic model for the evolution of protein lengths
, 2007 We analyse a simple discrete-time stochastic process for the theoretical modeling of the evolution of protein lengths. At every step of the process a new protein is produced as a modification of one of the proteins already existing and its length is ...
A. Meir +5 more
core +1 more source
Automated Protein Structure Modeling with SWISS-MODEL Workspace and the Protein Model Portal [PDF]
, 2011 Comparative protein structure modeling is a computational approach to build three-dimensional structural models for proteins using experimental structures of related protein family members as templates. Regular blind assessments of modeling accuracy have demonstrated that comparative protein structure modeling is currently the most reliable technique ...
Bordoli, Lorenza, Schwede, Torsten
openaire +3 more sources
FEBS Letters, EarlyView.Bifidobacterium bifidum establishes symbiosis with infants by metabolizing lacto‐N‐biose I (LNB) from human milk oligosaccharides (HMOs). The extracellular multidomain enzyme LnbB drives this process, releasing LNB via its catalytic glycoside hydrolase family 20 (GH20) lacto‐N‐biosidase domain.
Xinzhe Zhang +5 more
wiley +1 more source
The Caenorhabditis elegans DPF‐3 and human DPP4 have tripeptidyl peptidase activity
FEBS Letters, EarlyView.The dipeptidyl peptidase IV (DPPIV) family comprises serine proteases classically defined by their ability to remove dipeptides from the N‐termini of substrates, a feature that gave the family its name. Here, we report the discovery of a previously unrecognized tripeptidyl peptidase activity in DPPIV family members from two different species.
Aditya Trivedi, Rajani Kanth Gudipati
wiley +1 more source
Analytical Approaches to Improve Accuracy in Solving the Protein Topology Problem
Molecules, 2018 To take advantage of recent advances in genomics and proteomics it is critical that the three-dimensional physical structure of biological macromolecules be determined.
Kamal Al Nasr +3 more
doaj +1 more source
Bactericidal/Permeability-Increasing Protein Downregulates the Inflammatory Response in In Vivo Models of Arthritis [PDF]
, 2022 Anna Scanu +7 more
openalex +1 more source
The role and implications of mammalian cellular circadian entrainment
FEBS Letters, EarlyView.At their most fundamental level, mammalian circadian rhythms occur inside every individual cell. To tell the correct time, cells must align (or ‘entrain’) their circadian rhythm to the external environment. In this review, we highlight how cells entrain to the major circadian cues of light, feeding and temperature, and the implications this has for our
Priya Crosby
wiley +1 more source