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index medicus (6) 6
proteins (5) 5
chaperonins (4) 4
adenosine triphosphatase (3) 3
binding sites (3) 3
biological sciences (3) 3
molecular machines (3) 3
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adenosine triphosphate - metabolism (2) 2
allosteric properties (2) 2
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chaperonin 60 - chemistry (1) 1
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Chemical Reviews, ISSN 0009-2665, 06/2016, Volume 116, Issue 11, pp. 6588 - 6588
Chaperonins are nanomachines that facilitate protein folding by undergoing energy (ATP)-dependent movements that are coordinated in time and space owing to... 
Proteins | Control | Movements | Escherichia coli | Holes | Coupling | Substrates | Folding
Journal Article
Chemical Reviews, ISSN 0009-2665, 06/2016, Volume 116, Issue 11, p. 6588
  Chaperonins are nanomachines that facilitate protein folding by undergoing energy (ATP)-dependent movements that are coordinated in time and space owing to... 
Eukaryotes | E coli | Protein folding | Potassium | Adenosine triphosphatase | Substrates
Journal Article
Philosophical Transactions of the Royal Society B: Biological Sciences, ISSN 0962-8436, 06/2018, Volume 373, Issue 1749, pp. 20170176 - 20170176
Journal Article
Biophysical Journal, ISSN 0006-3495, 11/2019, Volume 117, Issue 10, pp. 1915 - 1921
A fundamental problem that has hindered the use of the classic Monod-Wyman-Changuex (MWC) allosteric model since its introduction is that it has been difficult... 
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 4/2013, Volume 110, Issue 18, pp. 7235 - 7239
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 05/2017, Volume 114, Issue 20, p. 5189
Knowing the mechanism of allosteric switching is important for understanding how molecular machines work. The CCT/TRiC chaperonin nanomachine undergoes... 
Hydrolysis | Molecular machines | Molecules | Allosteric properties | Nanostructure | Waves | ATP | Folding | Switching
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 05/2017, Volume 114, Issue 20, pp. 5189 - 5194
Knowing the mechanism of allosteric switching is important for understanding how molecular machines work. The CCT/TRiC chaperonin nanomachine undergoes... 
Molecular machines | Allostery | Conformational changes | Chaperonins | ASYMMETRY | COMPLEX | molecular machines | CCT | RING | MULTIDISCIPLINARY SCIENCES | chaperonins | conformational changes | SUBUNITS | RELEASE | MASS-SPECTROMETRY | allostery | Physiological aspects | Amino acid sequence | Molecular chaperones | Adenosine triphosphate | Methods | Biological Sciences
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2012, Volume 109, Issue 46, pp. 18833 - 18838
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 04/2013, Volume 110, Issue 18, p. 7235
  The activity of many proteins, including metabolic enzymes, molecular machines, and ion channels, is often regulated by conformational changes that are... 
Proteins | E coli | Adenosine triphosphatase | Binding sites
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2012, Volume 109, Issue 46, p. 18833
  The eukaryotic chaperonin containing t-complex polypeptide 1 (CCT/TRiC) is an ATP-fueled machine that assists protein folding. It consists of two... 
Proteins | Polypeptides | Yeast | Mutation | Cytoplasm | Adenosine triphosphatase | Binding sites
Journal Article
Biochimie, ISSN 0300-9084, 1972, Volume 54, Issue 2, pp. 257 - 260
Plasma contains a prophospholipase which may be activated a factor presents in crude trypsin. Rat platelets contain an activator having the same role as crude... 
Journal Article
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