Fabs enable single particle cryoEM studies of small proteins - Wikidata - wikimedia - TriplyDB

Fabs enable single particle cryoEM studies of small proteins

Fabs enable single particle cryoEM studies of small proteins

http://www.wikidata.org/entity/Q34223995

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Cryo-EM studies of the structure and dynamics of vacuolar-type ATPases Dynamic Viral Glycoprotein Machines: Approaches for Probing Transient States That Drive Membrane Fusion Structural and Computational Biology in the Design of Immunogenic Vaccine Antigens Membrane protein structures without crystals, by single particle electron cryomicroscopy Fusion to a homo-oligomeric scaffold allows cryo-EM analysis of a small protein Native immunogold labeling of cell surface proteins and viral glycoproteins for cryo-electron microscopy and cryo-electron tomography applications Prefusion structure of trimeric HIV-1 envelope glycoprotein determined by cryo-electron microscopy Cryo-EM Structure of a Fully Glycosylated Soluble Cleaved HIV-1 Envelope Trimer Structure of -galactosidase at 3.2-A resolution obtained by cryo-electron microscopy The Preserved HTH-Docking Cleft of HIV-1 Integrase Is Functionally Critical Protein Crystallography in Vaccine Research and Development Structural characterization of the mechanosensitive channel candidate MCA2 from Arabidopsis thaliana Towards an integrative structural biology approach: combining Cryo-TEM, X-ray crystallography, and NMR.Single-particle electron microscopy in the study of membrane protein structure Subnanometre-resolution electron cryomicroscopy structure of a heterodimeric ABC exporter Breaking Cryo-EM Resolution Barriers to Facilitate Drug Discovery.Single particle electron cryo-microscopy of a mammalian ion channel.Averaging of viral envelope glycoprotein spikes from electron cryotomography reconstructions using Jsubtomo Development and characterization of synthetic antibodies binding to the cystic fibrosis conductance regulator.Cryo-electron microscopy and X-ray crystallography: complementary approaches to structural biology and drug discovery.A method for integrative structure determination of protein-protein complexes.High-gradient nanomagnets on cantilevers for sensitive detection of nuclear magnetic resonance.Polyclonal Antibody Production for Membrane Proteins via Genetic Immunization.An introduction to sample preparation and imaging by cryo-electron microscopy for structural biology.Structures of Ebola virus GP and sGP in complex with therapeutic antibodies.Conformational Chaperones for Structural Studies of Membrane Proteins Using Antibody Phage Display with Nanodiscs The study of vacuolar-type ATPases by single particle electron microscopy.Cryo-electron microscopy for structural biology: current status and future perspectives.Single-particle cryo-electron microscopy of macromolecular complexes.Applications of NMR to membrane proteins.[Cryo-microscopy, an alternative to the X-ray crystallography?].How good can cryo-EM become?Building a pseudo-atomic model of the anaphase-promoting complex Cryo-EM structures of the TMEM16A calcium-activated chloride channel.The Therapeutic Antibody LM609 Selectively Inhibits Ligand Binding to Human αVβ3 Integrin via Steric Hindrance.Locking the Elbow: Improved Antibody Fab Fragments as Chaperones for Structure Determination.Labeling of Membrane Complexes for Electron Microscopy.The full-length cytochrome P450 enzyme CYP102A1 dimerizes at its reductase domains and has flexible heme domains for efficient catalysis.Ensemble cryoEM elucidates the mechanism of insulin capture and degradation by human insulin degrading enzyme.Stabilization of a Membrane-Associated Amyloid-β Oligomer for Its Validation in Alzheimer's Disease.

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P2860

Fabs enable single particle cryoEM studies of small proteins

http://www.wikidata.org/entity/Q34223995

description

2012 nî lūn-bûn

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2012 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2012 թվականի ապրիլին հրատարակված գիտական հոդված

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2012年の論文

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2012年学术文章

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2012年学术文章

@zh-cn

2012年学术文章

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2012年学术文章

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2012年学术文章

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2012年學術文章

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name

Fabs enable single particle cryoEM studies of small proteins

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Fabs enable single particle cryoEM studies of small proteins

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Fabs enable single particle cryoEM studies of small proteins

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type

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Fabs enable single particle cryoEM studies of small proteins

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Fabs enable single particle cryoEM studies of small proteins

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Fabs enable single particle cryoEM studies of small proteins

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prefLabel

Fabs enable single particle cryoEM studies of small proteins

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Fabs enable single particle cryoEM studies of small proteins

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Fabs enable single particle cryoEM studies of small proteins

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J.STR.2012.02.017

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Fabs enable single particle cryoEM studies of small proteins

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P2093

Agustin Avila-Sakar

http://www.w3.org/2001/XMLSchema#string

Andrea Rossi

http://www.w3.org/2001/XMLSchema#string

Charles H Greenberg

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Charles S Craik

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Claudia M Mergel

http://www.w3.org/2001/XMLSchema#string

Javier Chaparro-Riggers

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JungMin Kim

http://www.w3.org/2001/XMLSchema#string

Maofu Liao

http://www.w3.org/2001/XMLSchema#string

Narinobu Juge

http://www.w3.org/2001/XMLSchema#string

Pavel Strop

http://www.w3.org/2001/XMLSchema#string

P2860

Binding of proprotein convertase subtilisin/kexin type 9 to epidermal growth factor-like repeat A of low density lipoprotein receptor decreases receptor recycling and increases degradation

Structure of a nanobody-stabilized active state of the β(2) adrenoceptor

3.3 A cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry.

Inhibition of PCSK9: a powerful weapon for achieving ideal LDL cholesterol levels

Negative staining and image classification — powerful tools in modern electron microscopy

Molecular biology of PCSK9: its role in LDL metabolism

Crystal structure of the HIV-1 integrase catalytic core and C-terminal domains: A model for viral DNA binding

Structure of a two-domain fragment of HIV-1 integrase: implications for domain organization in the intact protein.

Structure of the human transferrin receptor-transferrin complex

Structural and biophysical studies of PCSK9 and its mutants linked to familial hypercholesterolemia

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582-592

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scholarly article

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10.1016/J.STR.2012.02.017

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4

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22483106

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