Cryo‐EM of ABC transporters: an ice‐cold solution to everything?
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[1] Yong Zi Tan,et al. Through-grid wicking enables high-speed cryoEM specimen preparation , 2020, bioRxiv.
[2] J. Frank,et al. Three‐dimensional reconstruction from a single‐exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli , 1987, Journal of microscopy.
[4] Martin Grininger,et al. Protein denaturation at the air-water interface and how to prevent it , 2019, eLife.
[5] Microscale Fluid Behavior during Cryo-EM Sample Blotting. , 2019, Biophysical journal.
[7] Jue Chen,et al. Structural Basis of Substrate Recognition by the Multidrug Resistance Protein MRP1 , 2017, Cell.
[8] Alex J. Noble,et al. Eliminating effects of particle adsorption to the air/water interface in single-particle cryo-electron microscopy: Bacterial RNA polymerase and CHAPSO , 2019, Journal of structural biology: X.
[9] S. Sligar,et al. Applications of phospholipid bilayer nanodiscs in the study of membranes and membrane proteins. , 2007, Biochemistry.
[10] Jue Chen,et al. ATP Binding Enables Substrate Release from Multidrug Resistance Protein 1 , 2018, Cell.
[11] Lei Chen,et al. Ligand binding and conformational changes of SUR1 subunit in pancreatic ATP-sensitive potassium channels , 2018, Protein & Cell.
[12] S H W Scheres,et al. Processing of Structurally Heterogeneous Cryo-EM Data in RELION. , 2016, Methods in enzymology.
[13] X. Gong,et al. Structure of the Human Lipid Exporter ABCA1 , 2017, Cell.
[14] R. Tampé,et al. Structure of the human MHC-I peptide-loading complex , 2017, Nature.
[15] Xing Zhang,et al. Bioactive Functionalized Monolayer Graphene for High-Resolution Cryo-Electron Microscopy. , 2019, Journal of the American Chemical Society.
[16] Jose-Maria Carazo,et al. Faculty Opinions recommendation of 3D Variability Analysis: Directly resolving continuous flexibility and discrete heterogeneity from single particle cryo-EM images. , 2020 .
[17] Nikolaus Grigorieff,et al. Structure of the transporter associated with antigen processing trapped by herpes simplex virus , 2016, eLife.
[18] James M. Bell,et al. In situ structure and assembly of the multidrug efflux pump AcrAB-TolC , 2019, Nature Communications.
[19] J. Kowal,et al. Structure of the human multidrug transporter ABCG2 , 2017, Nature.
[20] J. Riordan,et al. Cryo-EM visualization of an active high open probability CFTR anion channel , 2018 .
[21] B. Shoichet,et al. Structural identification of a hotspot on CFTR for potentiation , 2019, Science.
[22] Hongjin Zheng,et al. Pathogenic siderophore ABC importer YbtPQ adopts a surprising fold of exporter , 2020, Science Advances.
[23] Ashwin Chari,et al. Atomic-resolution protein structure determination by cryo-EM , 2020, Nature.
[24] Joseph H. Davis,et al. Addressing preferred specimen orientation in single-particle cryo-EM through tilting , 2017, Nature Methods.
[25] Jue Chen,et al. Molecular structure of human P-glycoprotein in the ATP-bound, outward-facing conformation , 2018, Science.
[26] T. Walz,et al. Structural basis of MsbA-mediated lipopolysaccharide transport , 2017, Nature.
[27] Terrence Frey,et al. Faculty Opinions recommendation of TRPV1 structures in distinct conformations reveal activation mechanisms. , 2014 .
[28] N. Gao,et al. Structure of a Pancreatic ATP-Sensitive Potassium Channel , 2017, Cell.
[29] W. Kühlbrandt. The Resolution Revolution , 2014, Science.
[30] M. Liao,et al. ABCG2 transports anticancer drugs via a closed-to-open switch , 2020, Nature Communications.
[31] Microfluidic protein isolation and sample preparation for high-resolution cryo-EM , 2019, bioRxiv.
[32] John P. Moore,et al. Cryo-EM Structure of a Fully Glycosylated Soluble Cleaved HIV-1 Envelope Trimer , 2013, Science.
[33] R. Stroud,et al. Subnanometre-resolution electron cryomicroscopy structure of a heterodimeric ABC exporter , 2014, Nature.
[34] Sjors H.W. Scheres,et al. Faculty Opinions recommendation of Real-time cryo-electron microscopy data preprocessing with Warp. , 2019, Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature.
[35] R. Ravelli,et al. Cryo-EM structures from sub-nl volumes using pin-printing and jet vitrification , 2020, Nature Communications.
[36] Daniel Picot,et al. Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins , 2010, Nature Methods.
[37] A. Cheng,et al. Movies of ice-embedded particles enhance resolution in electron cryo-microscopy. , 2012, Structure.
[38] C. Gati,et al. A mycobacterial ABC transporter mediates the uptake of hydrophilic compounds , 2020, Nature.
[39] A. Rothnie,et al. Structure and function of membrane proteins encapsulated in a polymer-bound lipid bilayer. , 2017, Biochimica et biophysica acta. Biomembranes.
[40] E. Pardon,et al. Megabodies expand the nanobody toolkit for protein structure determination by single-particle cryo-EM , 2019, Nature Methods.
[41] P. Penczek,et al. A Primer to Single-Particle Cryo-Electron Microscopy , 2015, Cell.
[42] C. Tribet,et al. Amphipols: polymers that keep membrane proteins soluble in aqueous solutions. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[43] R. Glaeser,et al. Opinion: hazards faced by macromolecules when confined to thin aqueous films , 2016, Biophysics reports.
[44] Henning Urlaub,et al. GraFix: sample preparation for single-particle electron cryomicroscopy , 2008, Nature Methods.
[45] D. Tegunov,et al. Multi-particle cryo-EM refinement with M visualizes ribosome-antibiotic complex at 3.5 Å in cells , 2020, Nature Methods.
[46] Joachim Frank,et al. Time-Resolved Cryo-electron Microscopy Using a Microfluidic Chip. , 2018, Methods in molecular biology.
[47] David J. Fleet,et al. Non-uniform refinement: adaptive regularization improves single-particle cryo-EM reconstruction , 2019, Nature Methods.
[48] J. Kowal,et al. Structure of a zosuquidar and UIC2-bound human-mouse chimeric ABCB1 , 2018, Proceedings of the National Academy of Sciences.
[49] Jitendra Malik,et al. Automated multi-model reconstruction from single-particle electron microscopy data. , 2010, Journal of structural biology.
[50] Q. Luo,et al. Cryo-EM structures of lipopolysaccharide transporter LptB2FGC in lipopolysaccharide or AMP-PNP-bound states reveal its transport mechanism , 2019, Nature Communications.
[51] Claudio Ciferri,et al. Cryo-EM in drug discovery: achievements, limitations and prospects , 2018, Nature Reviews Drug Discovery.
[52] Jun Yu Li,et al. The Peptidisc, a simple method for stabilizing membrane proteins in detergent-free solution , 2018, eLife.
[53] D. Elmlund,et al. AgarFix: Simple and accessible stabilization of challenging single-particle cryo-EM specimens through crosslinking in a matrix of agar. , 2019, Journal of structural biology.
[54] B. Carragher,et al. Distinct conformational spectrum of homologous multidrug ABC transporters. , 2015, Structure.
[55] C. Russo,et al. Multifunctional graphene supports for electron cryomicroscopy , 2019, Proceedings of the National Academy of Sciences.
[56] D. Julius,et al. Structure of the TRPV1 ion channel determined by electron cryo-microscopy , 2013, Nature.
[57] J. Kowal,et al. Structural basis of small-molecule inhibition of human multidrug transporter ABCG2 , 2018, Nature Structural & Molecular Biology.
[58] Jue Chen,et al. Conformational Changes of CFTR upon Phosphorylation and ATP Binding , 2017, Cell.
[59] Michael R. Wasserman,et al. Characterization of the kinetic cycle of an ABC transporter by single-molecule and cryo-EM analyses , 2020, eLife.
[60] William J. Rice,et al. A new method for vitrifying samples for cryo-EM , 2017 .
[61] B. Chait,et al. Structural basis of substrate recognition by a polypeptide processing and secretion transporter , 2020, eLife.
[62] Erik Lindahl,et al. New tools for automated high-resolution cryo-EM structure determination in RELION-3 , 2018, eLife.
[63] Jue Chen,et al. Atomic Structure of the Cystic Fibrosis Transmembrane Conductance Regulator , 2016, Cell.
[64] E. Lindahl,et al. Characterisation of molecular motions in cryo-EM single-particle data by multi-body refinement in RELION , 2018, bioRxiv.
[65] M. Gottesman,et al. Overview: ABC Transporters and Human Disease , 2001, Journal of bioenergetics and biomembranes.
[66] Bonnie Berger,et al. Positive-unlabeled convolutional neural networks for particle picking in cryo-electron micrographs , 2018, Nature Methods.
[67] J. Dubochet,et al. Cryo-electron microscopy of vitrified specimens , 1988, Quarterly Reviews of Biophysics.
[68] Cong-Zhao Zhou,et al. Cryo-EM structure of human lysosomal cobalamin exporter ABCD4 , 2019, Cell Research.
[69] R. Stevens,et al. Engineered Nanostructured β-Sheet Peptides Protect Membrane Proteins , 2013, Nature Methods.
[70] J. Briggs,et al. An atomic model of HIV-1 capsid-SP1 reveals structures regulating assembly and maturation , 2016, Science.
[71] M. Sung,et al. Mechanism of pharmacochaperoning in a mammalian KATP channel revealed by cryo-EM , 2019, eLife.
[72] D. Gadsby,et al. Molecular Structure of the Human CFTR Ion Channel , 2017, Cell.
[73] M. Liao,et al. Structural basis of lipopolysaccharide extraction by the LptB2FGC complex , 2019, Nature.
[74] David J. Fleet,et al. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination , 2017, Nature Methods.
[75] A. Goldman,et al. A method for detergent-free isolation of membrane proteins in their local lipid environment , 2016, Nature Protocols.
[76] Yong Zi Tan,et al. Structure and Drug Resistance of the Plasmodium falciparum Transporter PfCRT , 2019, Nature.
[77] N. Unwin,et al. Analysis of transient structures by cryo-microscopy combined with rapid mixing of spray droplets. , 1994, Ultramicroscopy.
[78] Xueming Li,et al. Fabs enable single particle cryoEM studies of small proteins. , 2012, Structure.
[79] Rebecca F Thompson,et al. Approaches to altering particle distributions in cryo-electron microscopy sample preparation , 2018, Acta crystallographica. Section D, Structural biology.
[80] Jing Kong,et al. High-yield monolayer graphene grids for near-atomic resolution cryoelectron microscopy , 2019, Proceedings of the National Academy of Sciences.
[81] Jue Chen,et al. Molecular structure of the ATP-bound, phosphorylated human CFTR , 2018, Proceedings of the National Academy of Sciences.
[82] R. Henderson,et al. Comparison of optimal performance at 300 keV of three direct electron detectors for use in low dose electron microscopy , 2014, Ultramicroscopy.
[83] J. Kowal,et al. Cryo-EM structures of a human ABCG2 mutant trapped in ATP-bound and substrate-bound states , 2018, Nature.
[84] William J. Rice,et al. High Resolution Single Particle Cryo-Electron Microscopy using Beam-Image Shift , 2018, bioRxiv.
[85] Cong-Zhao Zhou,et al. Cryo-electron Microscopy Structure and Transport Mechanism of a Wall Teichoic Acid ABC Transporter , 2020, mBio.
[86] Takanori Nakane,et al. Single-particle cryo-EM at atomic resolution , 2020, Nature.
[87] C. Yoshioka,et al. Anti-diabetic drug binding site in a mammalian KATP channel revealed by Cryo-EM , 2017, eLife.
[88] A. Meister,et al. Solubilization of Membrane Proteins into Functional Lipid‐Bilayer Nanodiscs Using a Diisobutylene/Maleic Acid Copolymer , 2017, Angewandte Chemie.
[89] Thorsten Wagner,et al. SPHIRE-crYOLO is a fast and accurate fully automated particle picker for cryo-EM , 2019, Communications Biology.
[90] J. Kowal,et al. Structural insight into substrate and inhibitor discrimination by human P-glycoprotein , 2019, Science.
[91] D. Agard,et al. Electron counting and beam-induced motion correction enable near atomic resolution single particle cryoEM , 2013, Nature Methods.
[92] Yong Zi Tan,et al. Reducing effects of particle adsorption to the air-water interface in cryoEM , 2018, Nature Methods.
[93] Alexis Rohou,et al. cisTEM: User-friendly software for single-particle image processing , 2017, bioRxiv.
[94] Andreas Plückthun,et al. Covalently circularized nanodiscs for studying membrane proteins and viral entry , 2016, Nature Methods.
[95] Cong-Zhao Zhou,et al. Cryo-EM structure of human bile salts exporter ABCB11 , 2020, Cell Research.
[96] A. Ramamoorthy,et al. Styrene maleic acid derivates to enhance the applications of bio-inspired polymer based lipid-nanodiscs. , 2018, European polymer journal.
[97] J. Lyons,et al. Expression strategies for structural studies of eukaryotic membrane proteins. , 2016, Current opinion in structural biology.
[98] G. Hummer,et al. Conformation space of a heterodimeric ABC exporter under turnover conditions , 2019, Nature.
[99] Tristan Bepler,et al. Topaz-Denoise: general deep denoising models for cryoEM and cryoET , 2019, Nature Communications.
[100] D. Vasishtan,et al. Extracellular Vesicles: A Platform for the Structure Determination of Membrane Proteins by Cryo-EM , 2014, Structure.
[101] R. MacKinnon,et al. Molecular structure of human KATP in complex with ATP and ADP , 2017, bioRxiv.
[102] Lei Chen,et al. The Structural Basis for the Binding of Repaglinide to the Pancreatic KATP Channel. , 2019, Cell reports.
[103] J. Kowal,et al. Structure of the human lipid exporter ABCB4 in a lipid environment , 2019, Nature Structural & Molecular Biology.
[104] J. Riordan,et al. Cryo-EM Visualization of an Active High Open Probability CFTR Anion Channel. , 2018, Biochemistry.
[105] Robert M Glaeser,et al. Laser phase plate for transmission electron microscopy , 2019, Nature Methods.
[106] Andrej Bieri,et al. Blotting-free and lossless cryo-electron microscopy grid preparation from nanoliter-sized protein samples and single-cell extracts. , 2017, Journal of structural biology.
[107] J. Rubinstein,et al. Shake-it-off: a simple ultrasonic cryo-EM specimen-preparation device , 2019, bioRxiv.
[108] Y. Lacasse,et al. From the authors , 2005, European Respiratory Journal.
[109] Stephen G. Sligar,et al. Self-Assembly of Discoidal Phospholipid Bilayer Nanoparticles with Membrane Scaffold Proteins , 2002 .