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Science, ISSN 0036-8075, 11/2018, Volume 362, Issue 6416, pp. 829 - 834
Membrane proteins reside in lipid bilayers and are typically extracted from this environment for study, which often compromises their integrity. In this work,... 
OUTER-MEMBRANE | NMR | OXIDASE | STRUCTURAL BASIS | MULTIDISCIPLINARY SCIENCES | LIPIDS | SUBUNIT | Molecular Chaperones - metabolism | Bacterial Proteins - chemistry | Porins - metabolism | Molecular Chaperones - chemistry | Proteome - chemistry | Adenine Nucleotide Translocator 1 - chemistry | Cattle | Mass Spectrometry | Mitochondrial Membranes - chemistry | Porins - chemistry | Membrane Proteins - metabolism | SEC Translocation Channels - chemistry | SEC Translocation Channels - metabolism | Bacterial Outer Membrane Proteins - chemistry | Escherichia coli Proteins - metabolism | Adenine Nucleotide Translocator 1 - metabolism | Mitochondrial Proton-Translocating ATPases - chemistry | Mitochondrial Proton-Translocating ATPases - metabolism | Mitochondrial Membranes - metabolism | Animals | Bacterial Outer Membrane Proteins - metabolism | Membrane Proteins - chemistry | Protein Conformation, beta-Strand | Bacterial Proteins - metabolism | Lipid Bilayers - chemistry | Lipid Bilayers - metabolism | Escherichia coli Proteins - chemistry | Proteome - metabolism | Physiological aspects | Mass spectrometry | Methods | Membrane proteins | Escherichia coli | Muscle proteins | Fatty acids | Porins | Adenosine triphosphate | Adenosine triphosphatase | Stoichiometry | Membranes | Outer membranes | Lipids | Translocase | Chaperones | ADP | Lipid bilayers | Proteins | Mitochondria | E coli | Bacteria | Assemblies | Efflux | Inner membranes | Adenosine | Adenosine diphosphate | Membrane vesicles | Mass spectroscopy | Electron microscopy | Organic chemistry | Scientific imaging | Dimers | Disruption | ATP | Ejection
Journal Article
Journal Article
BBA - Bioenergetics, ISSN 0005-2728, 09/2018, Volume 1859, pp. e30 - e30
Journal Article
BBA - Bioenergetics, ISSN 0005-2728, 09/2018, Volume 1859, pp. e84 - e84
Journal Article
Structure, ISSN 0969-2126, 10/2018, Volume 26, Issue 10, pp. 1393 - 1398.e2
In the nucleus, RanGTP binding to importin dissociates the cargo. On the other hand, RanGTP enables exportin to bind export cargo and form the export complex... 
pre-microRNA | RanGTP | heat repeats | cargo selection mechanism | exportin 5 | RANGTP | COMPLEX | BIOPHYSICS | MECHANISM | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | NUCLEAR EXPORT | CRM1 | PROTEINS | REVEALS | CELL BIOLOGY | Exports | MicroRNA | Resveratrol
Journal Article
Current Opinion in Structural Biology, ISSN 0959-440X, 2011, Volume 21, Issue 1, pp. 101 - 108
Journal Article
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