Results 51 to 60 of about 6,313,615 (343)
Biophysical approaches for studying viral entry
FEBS 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
Evolving data standards for cryo-EM structures
Structural Dynamics, 2020 Electron cryo-microscopy (cryo-EM) is increasingly being used to determine 3D structures of a broad spectrum of biological specimens from molecules to cells. Anticipating this progress in the early 2000s, an international collaboration of scientists with
Catherine L. Lawson +2 more
doaj +1 more source
Frontiers in Molecular Biosciences, 2021 Single-particle cryogenic electron microscopy (cryo-EM) has revolutionized the field of the structural biology, providing an access to the atomic resolution structures of large biomolecular complexes in their near-native environment. Today’s cryo-EM maps
Łukasz Nierzwicki +2 more
doaj +1 more source
Structure‐forward targeting of claudins with synthetic binders
FEBS Letters, EarlyView.Claudins form the paracellular barriers between epithelial and endothelial tissues at tight junctions and are targets for molecular binders with the goal of modulating barrier permeability. Claudin‐binding molecules are relevant in drug delivery or in altering claudin interactions with disease‐causing proteins.
Alex J. Vecchio
wiley +1 more source
Nature CommunicationsUropathogenic Escherichia coli strains use filamentous type 1 pili to adhere to and invade uroepithelial cells. The pilus consists of a flexible tip fibrillum, formed by the adhesin FimH and the subunits FimG and FimF. The pilus rod is a helical assembly
Paul Bachmann +3 more
doaj +1 more source
Using cryo-electron microscopy maps for X-ray structure determination
IUCrJ, 2018 X-ray crystallography and cryo-electron microscopy (cryo-EM) are complementary techniques for structure determination. Crystallography usually reveals more detailed information, while cryo-EM is an extremely useful technique for studying large-sized ...
Lingxiao Zeng, Wei Ding, Quan Hao
doaj +1 more source
Cryo-EM structure of the SEA complex
Nature, 2022 AbstractThe SEA complex (SEAC) is a growth regulator that acts as a GTPase-activating protein (GAP) towards Gtr1, a Rag GTPase that relays nutrient status to the Target of Rapamycin Complex 1 (TORC1) in yeast1. Functionally, the SEAC has been divided into two subcomplexes: SEACIT, which has GAP activity and inhibits TORC1, and SEACAT, which regulates ...
Tafur Petrozzi, Lucas +9 more
openaire +4 more sources
Cryo-EM Statistics for Data Collection and Model Quality.
, 2023 Cryo-EM Statistics for Data Collection and Model Quality.
Asma Hatoum-Aslan (4451431) +7 more
core +1 more source
Engineering peptides into antibodies—opportunities and strategies for therapeutic innovation
FEBS Letters, EarlyView.Peptides and antibodies occupy complementary therapeutic niches. Peptides recognize difficult targets in a compact format, while antibodies add specificity, long half‐life, and effector functions. This review examines strategies that merge both modalities—peptide grafting into loops, terminal and Fc fusions, and bioconjugation—highlighting how ...
Jinling Wang +2 more
wiley +1 more source
Cryo-EM data collection, refinement and validation statistics.
, 2020 Cryo-EM data collection, refinement and validation statistics.
Jörg Bürger (302968) +5 more
core +1 more source