Results 21 to 30 of about 55,954 (213)
Cryo-EM: beyond the microscope [PDF]
Current Opinion in Structural Biology, 2017 The pace at which cryo-EM is being adopted as a mainstream tool in structural biology has continued unabated over the past year. Initial successes in obtaining near-atomic resolution structures with cryo-EM were enabled to a large extent by advances in microscope and detector technology.
Lesley A, Earl +3 more
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Nature Methods, 2015 Gold supports nearly eliminate unwanted specimen motion in cryo-electron microscopy, enabling high-resolution structure determination of challenging proteins.
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FEBS 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
pH‐mediated activation of the lysosomal arginine sensor SLC38A9
FEBS 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
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
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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
Phosphoinositides and inositol phosphates as molecular glues
FEBS Letters, EarlyView.Inositol phosphates (IPs) and phosphoinositides (PIPs) regulate diverse eukaryotic processes. Beyond recruiting signaling proteins or acting as structural cofactors, recent studies suggest they mediate protein–protein interactions as natural molecular glues.
Aleshia Seaton‐Terry +9 more
wiley +1 more source
Cryo-EM structure of the exocyst complex [PDF]
Nature Structural & Molecular Biology, 2018 The exocyst is an evolutionarily conserved octameric protein complex that mediates the tethering of post-Golgi secretory vesicles to the plasma membrane during exocytosis and is implicated in many cellular processes such as cell polarization, cytokinesis, ciliogenesis and tumor invasion. Using cryo-EM and chemical cross-linking MS (CXMS), we solved the
Kunrong Mei +12 more
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Molecular Oncology, EarlyView.Loss of the miR‐214/199a cluster is associated with recurrence in ovarian cancer. Engineered small extracellular vesicles (m214‐sEVs) elevate miR‐214‐3p/miR‐199a‐5p in tumor cells, suppress β‐catenin, TLR4, and YKT6 signaling, reprogram tumor‐derived sEV cargo, reduce chemoresistance and migration, and enhance carboplatin efficacy and survival in ...
Weida Wang +12 more
wiley +1 more source
The Current Revolution in Cryo-EM [PDF]
Biophysical Journal, 2016 Structural biology is the study of the molecular architecture of proteins and nucleic acids, which are the basis for all life forms. Structural biology came into its own as a field during the 1950s when the atomic structures of DNA (1) and several globular proteins (2) were solved.
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