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JOURNAL OF BIOLOGICAL CHEMISTRY, ISSN 0021-9258, 03/2019, Volume 294, Issue 13, pp. 5181 - 5197
Journal Article
Science, ISSN 0036-8075, 12/2013, Volume 342, Issue 6165, pp. 1477 - 1483
Journal Article
Science, ISSN 0036-8075, 12/2013, Volume 342, Issue 6165, pp. 1484 - 1490
Journal Article
Nature, ISSN 0028-0836, 07/2017, Volume 547, Issue 7663, pp. 360 - 361
For many enveloped viruses, binding to a receptor(s) on a host cell acts as the first step in a series of events culminating in fusion with the host cell... 
SYSTEM | ANTIBODIES | LEGINON | IMAGES | MULTIDISCIPLINARY SCIENCES | VACCINE | CLASSIFICATION | GP120 | GLYCOPROTEIN | CRYO-EM STRUCTURE | NEUTRALIZATION | Immunoglobulin Fab Fragments - ultrastructure | env Gene Products, Human Immunodeficiency Virus - ultrastructure | HIV Envelope Protein gp41 - genetics | Antibodies - chemistry | HIV Envelope Protein gp41 - metabolism | env Gene Products, Human Immunodeficiency Virus - metabolism | HIV Envelope Protein gp41 - chemistry | Receptors, CCR5 - metabolism | env Gene Products, Human Immunodeficiency Virus - genetics | HIV-1 - chemistry | Antibodies - immunology | Binding Sites - drug effects | env Gene Products, Human Immunodeficiency Virus - chemistry | Allosteric Regulation - drug effects | HIV Envelope Protein gp41 - ultrastructure | Amino Acid Sequence | CD4 Antigens - ultrastructure | Receptors, HIV - chemistry | Antibodies - ultrastructure | Models, Molecular | Receptors, HIV - ultrastructure | Immunoglobulin Fab Fragments - pharmacology | Antibodies - pharmacology | Cryoelectron Microscopy | HIV-1 - ultrastructure | Receptors, HIV - metabolism | CD4 Antigens - chemistry | Immunoglobulin Fab Fragments - chemistry | Receptors, CCR5 - chemistry | Ligands | Immunoglobulin Fab Fragments - immunology | CD4 Antigens - metabolism | Physiological aspects | Genetic aspects | Glycoproteins | HIV (Viruses) | Structure | Binding | Carbohydrates | Antigens | CCR5 protein | Glycoprotein gp41 | Glycoprotein | Antibodies | Viruses | Glycosylation | Trimers | Cell fusion | Electron microscopy | Crystallography | CXCR4 protein | CD4 antigen | Proteins | Transmission electron microscopy | Neutralizing | Human immunodeficiency virus--HIV | Mutation | Coordination compounds | Binding sites
Journal Article
Journal Article
Progress in biophysics and molecular biology, ISSN 0079-6107, 01/2020, Volume 150, pp. 160 - 183
Virtually all single-particle cryo-EM experiments currently suffer from specimen adherence to the air-water interface, leading to a non-uniform distribution in... 
Journal Article
Journal Article
Structure, ISSN 0969-2126, 10/2019, Volume 27, Issue 10, pp. 1497 - 1507.e3
Filament formation by enzymes is increasingly recognized as an important phenomenon with potentially unique regulatory properties and biological roles. SgrAI... 
endonuclease | self-association | indirect readout | filament-forming enzyme | DNA sequence specificity | protein filament | enzyme mechanism | cryo-EM | DNA binding | allostery | VISUALIZATION | DNA CLEAVAGE | SPECIFICITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | VALIDATION | CRYO-EM | ACETYL-COA CARBOXYLASE | CELL BIOLOGY | LIVER PHOSPHOFRUCTOKINASE | BIOPHYSICS | REORGANIZATION | METABOLIC ENZYMES | AGGREGATION
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2014, Volume 111, Issue 45, pp. 15981 - 15986
All organisms have evolved mechanisms to manage the stalling of ribosomes upon translation of aberrant mRNA. In eukaryotes, the large ribosomal... 
Proteins | Datasets | Yeasts | Quality assurance | Messenger RNA | Ubiquitins | Ribosomes | Electron microscopy | Transfer RNA | Tunnels | Tae2/nemf | Protein quality control | Listerin/Ltn1 E3 ubiquitin ligase | Cryo-EM | Translational surveillance | SYSTEM | listerin/Ltn1 E3 ubiquitin ligase | MULTIDISCIPLINARY SCIENCES | ELECTRON-MICROSCOPY | CRYO-EM IMAGES | FREALIGN | Tae2/Nemf | LISTERIN | DISSOCIATION | SCREEN | translational surveillance | protein quality control | SIGNAL RECOGNITION PARTICLE | cryo-EM | E3 UBIQUITIN LIGASE | REVEALS | Protein Structure, Tertiary | Ribosome Subunits, Large, Eukaryotic - genetics | Saccharomyces cerevisiae - genetics | Protein Biosynthesis - physiology | Ubiquitin-Protein Ligases - metabolism | RNA, Transfer, Amino Acyl - genetics | Structure-Activity Relationship | RNA-Binding Proteins | Saccharomyces cerevisiae Proteins - genetics | Saccharomyces cerevisiae - metabolism | Ribosome Subunits, Large, Eukaryotic - metabolism | Proteolysis | RNA, Transfer, Amino Acyl - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Proteasome Endopeptidase Complex - metabolism | Ubiquitination - physiology | Ubiquitin-Protein Ligases - genetics | Genetic research | Genetic aspects | Research | Structure | Genetic translation | Biological Sciences | Nemf | listerin | Tae2 | Ltn1 E3 ubiquitin ligase
Journal Article