“Native-like aggregation” of the acylphosphatase from Sulfolobus solfataricus and its biological implications
- Published in:
- FEBS Letters, 2009, v. 583, n. 16, p. 2630, doi. 10.1016/j.febslet.2009.07.013
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- Publication type:
- Article
Works matching IS 00145793 AND DT 2009 AND VI 583 AND IP 16
Results: 17
1
2
Serum amyloid A and protein AA: Molecular mechanisms of a transmissible amyloidosis
- Published in:
- FEBS Letters, 2009, v. 583, n. 16, p. 2685, doi. 10.1016/j.febslet.2009.04.026
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- Publication type:
- Article
3
Physiological responses to protein aggregates: Fibrinolysis, coagulation and inflammation (new roles for old factors)
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- FEBS Letters, 2009, v. 583, n. 16, p. 2691, doi. 10.1016/j.febslet.2009.06.013
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- Publication type:
- Article
4
Cells and prions: A license to replicate
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- FEBS Letters, 2009, v. 583, n. 16, p. 2674, doi. 10.1016/j.febslet.2009.06.014
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- Publication type:
- Article
5
Animal models of human amyloidoses: Are transgenic mice worth the time and trouble?
- Published in:
- FEBS Letters, 2009, v. 583, n. 16, p. 2663, doi. 10.1016/j.febslet.2009.07.031
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- Publication type:
- Article
6
The GroEL/GroES cis cavity as a passive anti-aggregation device
- Published in:
- FEBS Letters, 2009, v. 583, n. 16, p. 2654, doi. 10.1016/j.febslet.2009.06.049
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- Publication type:
- Article
7
The proteostasis boundary in misfolding diseases of membrane traffic
- Published in:
- FEBS Letters, 2009, v. 583, n. 16, p. 2639, doi. 10.1016/j.febslet.2009.07.014
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- Publication type:
- Article
8
The role of molecular chaperones in human misfolding diseases
- Published in:
- FEBS Letters, 2009, v. 583, n. 16, p. 2647, doi. 10.1016/j.febslet.2009.04.029
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- Publication type:
- Article
9
Glimpses of the molecular mechanisms of β<sub>2</sub>-microglobulin fibril formation in vitro: Aggregation on a complex energy landscape
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- FEBS Letters, 2009, v. 583, n. 16, p. 2623, doi. 10.1016/j.febslet.2009.05.005
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- Publication type:
- Article
10
Structure–activity relationship of amyloid fibrils
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- FEBS Letters, 2009, v. 583, n. 16, p. 2610, doi. 10.1016/j.febslet.2009.07.003
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- Publication type:
- Article
11
Switching in amyloid structure within individual fibrils: Implication for strain adaptation, species barrier and strain classification
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- FEBS Letters, 2009, v. 583, n. 16, p. 2618, doi. 10.1016/j.febslet.2009.05.044
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- Publication type:
- Article
12
Methods for structural characterization of prefibrillar intermediates and amyloid fibrils
- Published in:
- FEBS Letters, 2009, v. 583, n. 16, p. 2600, doi. 10.1016/j.febslet.2009.05.040
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- Publication type:
- Article
13
Small organic probes as amyloid specific ligands – Past and recent molecular scaffolds
- Published in:
- FEBS Letters, 2009, v. 583, n. 16, p. 2593, doi. 10.1016/j.febslet.2009.04.016
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- Publication type:
- Article
14
Protein folding, misfolding and disease
- Published in:
- 2009
- By:
- Publication type:
- Editorial
15
Biosensor-based label-free assays of amyloid growth
- Published in:
- FEBS Letters, 2009, v. 583, n. 16, p. 2587, doi. 10.1016/j.febslet.2009.06.008
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- Publication type:
- Article
16
Bridging the gap: From protein misfolding to protein misfolding diseases
- Published in:
- FEBS Letters, 2009, v. 583, n. 16, p. 2581, doi. 10.1016/j.febslet.2009.06.030
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- Publication type:
- Article
17
Editorial Board
- Published in:
- FEBS Letters, 2009, v. 583, n. 16, p. i, doi. 10.1016/S0014-5793(09)00580-8
- Publication type:
- Article