Results 91 to 100 of about 6,328,527 (298)
Guiding AlphaFold to predict how Munc13‐1 opens Syntaxin‐1
The syntaxin‐1 Habc‐domain (orange), linker (pink) and SNARE motif (yellow) form a closed conformation that binds to Munc18‐1 (violet) and is opened by the Munc13‐1 MUN domain (cyan) to form the SNARE complex that triggers neurotransmitter release.
Madhurima Chattopadhyay +2 more
wiley +1 more source
A labeled dataset for AI-based cryo-EM map enhancement
Cryogenic electron microscopy (cryo-EM) has transformed structural biology by enabling near atomic resolution imaging of macromolecular complexes. However, cryo-EM density maps suffer from intrinsic noise arising from structural sources, shot noise, and ...
Nabin Giri +3 more
doaj +1 more source
Cryo-electron microscopy (cryo-EM) enables the determination of membrane protein structures in native-like environments. Characterising how membrane proteins interact with the surrounding membrane lipid environment is assisted by resolution of lipid-like
T. Bertie Ansell +12 more
doaj +1 more source
Importin 7 mediates the nuclear import of HIV‐1 integrase via a specific interacting interface
HIV‐1 integrase enables viral DNA integration into the host genome. By binding to the core domain of the host protein Importin 7 via its C‐terminal domain, the integrase is transported across the nuclear membrane into the nucleus, where integration of the viral genome into host DNA takes place. This translocation is a critical step for subsequent viral
Juana Bana +5 more
wiley +1 more source
Fast multiscale reconstruction for Cryo-EM
We present a multiscale reconstruction framework for single-particle analysis (SPA). The representation of three-dimensional (3D) objects with scaled basis functions permits the reconstruction of volumes at any desired scale in the real-space. This multiscale approach generates interesting opportunities in SPA for the stabilization of the initial ...
Donati, Laurene +3 more
openaire +4 more sources
Cryo-EM and X-ray data collection.
(a) Cryo-EM map of ACS122 and ACS114 in complex with the AMC009 SOSIP trimer. Only the Fab variable regions are shown here. (b) Cryo-EM map of ACS122 and ACS114 in complex with AMC009 SOSIP colored by local resolution (Å). (c) Gold-standard Fourier shell
Patricia van der Woude (9323416) +25 more
core +1 more source
Biophysical characterisation shows that NanX, a membrane transport protein from the major facilitator superfamily (MFS), forms both monomers and dimers after purification. AlphaFold modelling and substrate docking provide information on residues likely involved in substrate recognition for NanX and another MFS member, NanT.
Michael C. Newton‐Vesty +13 more
wiley +1 more source
Preferred particle orientation presents a major challenge for many single particle cryo-electron microscopy (cryo-EM) samples. Orientation bias limits the angular information used to generate three-dimensional maps and thus affects the reliability and ...
James Chen +3 more
doaj +1 more source
Exploring Applications of Crowdsourcing to Cryo-EM
Abstract Extraction of particles from cryo-electron microscopy (cryo-EM) micrographs is a crucial step in processing single-particle datasets. Although algorithms have been developed for automatic particle picking, these algorithms generally rely on two-dimensional templates for particle identification, which may exhibit biases that can
Bruggemann, Jacob +2 more
openaire +2 more sources
Myogenic Fusogen‐Engineered Lipid Nanoparticles Enhance mRNA Delivery in Skeletal Muscle
This study reports a biomimetic strategy of engineering full‐length Myomaker, a muscle‐specific fusogen, into lipid nanoparticles (LNPs) to harness the native myoblast fusion capability for skeletal muscle mRNA delivery. The resulting Mymk‐LNPs enhance transfection in differentiating myocytes and enable Cre‐mediated reporter activation in injured ...
Fangyu Zhang +18 more
wiley +1 more source

