Results 81 to 90 of about 6,313,615 (343)
A labeled dataset for AI-based cryo-EM map enhancement
Computational and Structural Biotechnology JournalCryogenic 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-EM data processing and analysis of the RcsF-LolCDE.
, 2022 (A) Representative cryo-EM micrograph of RcsF-LolCDE in nanodisc. (B) Selected 2D class averages of cryo-EM particle images. (C) Scheme of 3D classification and refinement of cryo-EM particle images. (D) Gold-standard FSC curves calculated with different
Yihua Huang (245089) +6 more
core +1 more source
Molecular Oncology, EarlyView.Extracellular vesicle (EV) lipidomic profiling of plasma and ascites from patients with high‐grade serous ovarian cancer and of ovarian cancer cell lines reveals enrichment of triglycerides (TGs), diacylglycerols (DGs), phosphatidylcholine (PCs), sphingomyelins (SMs), reflecting tumor metabolic reprogramming.
Shikha Rani +9 more
wiley +1 more source
Cryo-EM advances in RNA structure determination
Signal Transduction and Targeted Therapy, 2022 Cryo-electron microscopy (cryo-EM) has emerged as an unprecedented tool to resolve protein structures at atomic resolution. Structural insights of biological samples not accessible by conventional X-ray crystallography and NMR can be explored with cryo ...
Haiyun Ma +3 more
doaj +1 more source
Fast multiscale reconstruction for Cryo-EM
Journal of Structural Biology, 2018 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
Atomic cryo-EM structures of viruses [PDF]
Current Opinion in Structural Biology, 2017 During the development of single particle cryo-EM in past five decades, icosahedral viruses have led the resolution progress owing to their large mass and high symmetry. Many technical advances in cryo-EM were first established with viruses. Since reaching ∼4Å resolution in 2008, it has become a relatively routine task to solve the atomic structure of ...
Wen, Jiang, Liang, Tang
openaire +2 more sources
Cryo-EM structure of GALR2 complex with galanin.
, 2022 (A) The molecular structure of GALR2 complex is shown both as cryo-EM map and ribbon diagram. GALR2, mGαqiN, Gβ1, Gγ2, and scFv16 are colored in blue, red, yellow-orange, marine, and lemon, respectively.
Hideo Fukuhara (494318) +15 more
core +1 more source
Mutant p53R273H disrupts PDPK1 homodimerization and contributes to PDPK1 activation
Molecular Oncology, EarlyView.How mutant p53R273H drives AKT signaling is unclear. We show that p53R273H, but not wild‐type, directly binds PDPK1 via a mutation‐dependent conformational change. This interaction disrupts inhibitory PDPK1 homodimerization and enhances AKT phosphorylation.
Mei Chee Lim +11 more
wiley +1 more source
Cryo-EM data collection, refinement and validation statistics.
Cryo-EM data collection, refinement and validation statistics.
Baobin Li (2173471) +6 more
core +3 more sources
Nature Communications, 2023 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