Control of p97 function by cofactor binding.
- Published in:
- FEBS Letters, 2015, v. 589, n. 19PartA, p. 2578, doi. 10.1016/j.febslet.2015.08.028
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- Publication type:
- Article
Works matching IS 00145793 AND DT 2015 AND VI 589 AND IP 19PartA
Results: 25
1
2
In various protein complexes, disordered protomers have large per-residue surface areas and area of protein-, DNA- and RNA-binding interfaces.
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- FEBS Letters, 2015, v. 589, n. 19PartA, p. 2561, doi. 10.1016/j.febslet.2015.08.014
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3
Retromer-mediated endosomal protein sorting: The role of unstructured domains.
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- FEBS Letters, 2015, v. 589, n. 19PartA, p. 2620, doi. 10.1016/j.febslet.2015.05.052
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- Publication type:
- Article
4
Order and disorder in intermediate filament proteins.
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- FEBS Letters, 2015, v. 589, n. 19PartA, p. 2464, doi. 10.1016/j.febslet.2015.07.024
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- Article
5
Structural stability and functional remodeling of high-density lipoproteins.
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- FEBS Letters, 2015, v. 589, n. 19PartA, p. 2627, doi. 10.1016/j.febslet.2015.02.028
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- Publication type:
- Article
6
LINC’ing form and function at the nuclear envelope.
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- FEBS Letters, 2015, v. 589, n. 19PartA, p. 2514, doi. 10.1016/j.febslet.2015.06.011
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- Publication type:
- Article
7
Methods for protein complex prediction and their contributions towards understanding the organisation, function and dynamics of complexes.
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- FEBS Letters, 2015, v. 589, n. 19PartA, p. 2590, doi. 10.1016/j.febslet.2015.04.026
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- Publication type:
- Article
8
Multivalent IDP assemblies: Unique properties of LC8-associated, IDP duplex scaffolds.
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- FEBS Letters, 2015, v. 589, n. 19PartA, p. 2543, doi. 10.1016/j.febslet.2015.07.032
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- Publication type:
- Article
9
Functional homologies in vesicle tethering.
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- FEBS Letters, 2015, v. 589, n. 19PartA, p. 2487, doi. 10.1016/j.febslet.2015.06.001
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- Publication type:
- Article
10
Pliability of protein complexes and complexity of protein pliability.
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- FEBS Letters, 2015, v. 589, n. 19PartA, p. 2431, doi. 10.1016/j.febslet.2015.08.035
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- Publication type:
- Article
11
Dynamics, flexibility, and allostery in molecular chaperonins.
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- FEBS Letters, 2015, v. 589, n. 19PartA, p. 2522, doi. 10.1016/j.febslet.2015.06.019
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- Publication type:
- Article
12
Diversity of COP9 signalosome structures and functional consequences.
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- FEBS Letters, 2015, v. 589, n. 19PartA, p. 2507, doi. 10.1016/j.febslet.2015.06.007
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- Publication type:
- Article
13
Functional advantages of dynamic protein disorder.
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- FEBS Letters, 2015, v. 589, n. 19PartA, p. 2433, doi. 10.1016/j.febslet.2015.06.003
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- Publication type:
- Article
14
The route to protein aggregate superstructures: Particulates and amyloid-like spherulites.
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- FEBS Letters, 2015, v. 589, n. 19PartA, p. 2448, doi. 10.1016/j.febslet.2015.07.006
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- Article
15
Editorial Board.
- Published in:
- FEBS Letters, 2015, v. 589, n. 19PartA, p. i, doi. 10.1016/S0014-5793(15)00739-5
- Publication type:
- Article
16
TAPO: A combined method for the identification of tandem repeats in protein structures.
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- FEBS Letters, 2015, v. 589, n. 19PartA, p. 2611, doi. 10.1016/j.febslet.2015.08.025
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- Publication type:
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17
Structural, morphological, and functional diversity of amyloid oligomers.
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- FEBS Letters, 2015, v. 589, n. 19PartA, p. 2640, doi. 10.1016/j.febslet.2015.07.013
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- Publication type:
- Article
18
A practical guide to small angle X-ray scattering (SAXS) of flexible and intrinsically disordered proteins.
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- FEBS Letters, 2015, v. 589, n. 19PartA, p. 2570, doi. 10.1016/j.febslet.2015.08.027
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19
The multifaceted roles of intrinsic disorder in protein complexes.
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- FEBS Letters, 2015, v. 589, n. 19PartA, p. 2498, doi. 10.1016/j.febslet.2015.06.004
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- Publication type:
- Article
20
Elastin-like polypeptides as models of intrinsically disordered proteins.
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- FEBS Letters, 2015, v. 589, n. 19PartA, p. 2477, doi. 10.1016/j.febslet.2015.08.029
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- Publication type:
- Article
21
Entropic clocks in the service of electrical signaling: ‘Ball and chain’ mechanisms for ion channel inactivation and clustering.
- Published in:
- FEBS Letters, 2015, v. 589, n. 19PartA, p. 2441, doi. 10.1016/j.febslet.2015.06.010
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22
Structural disorder and its role in proteasomal degradation.
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- FEBS Letters, 2015, v. 589, n. 19PartA, p. 2552, doi. 10.1016/j.febslet.2015.07.034
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- Publication type:
- Article
23
Structure and intrinsic disorder of the proteins of the Trypanosoma brucei editosome.
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- FEBS Letters, 2015, v. 589, n. 19PartA, p. 2603, doi. 10.1016/j.febslet.2015.07.026
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- Publication type:
- Article
24
Fuzzy complexes: Specific binding without complete folding.
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- FEBS Letters, 2015, v. 589, n. 19PartA, p. 2533, doi. 10.1016/j.febslet.2015.07.022
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- Publication type:
- Article
25
Structural disorder within paramyxoviral nucleoproteins.
- Published in:
- FEBS Letters, 2015, v. 589, n. 19PartA, p. 2649, doi. 10.1016/j.febslet.2015.05.055
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- Publication type:
- Article