(Q27690644)

Sulfolobus solfataricus

1 reference

5

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Francesco Bemporad

Francesco Bemporad

2

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Matteo de Rosa

Matteo de Rosa

1

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Stefano Ricagno

Stefano Ricagno

6

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Sara Pellegrino

Sara Pellegrino

3

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author name string

Fabrizio Chiti

Interconversion between two unrelated protein folds in the lymphotactin native state

4

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language of work or name

English

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publication date

September 2014

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published in

FEBS Journal

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volume

281

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issue

18

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page(s)

4072-84

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cites work

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Intrinsically unstructured proteins and their functions

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

The binding mechanisms of intrinsically disordered proteins.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

The Yin and Yang of protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Frequencies of amino acid strings in globular protein sequences indicate suppression of blocks of consecutive hydrophobic residues

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Nature disfavors sequences of alternating polar and non-polar amino acids: implications for amyloidogenesis

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Glycine residues appear to be evolutionarily conserved for their ability to inhibit aggregation

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Sequence conservation in Ig-like domains: the role of highly conserved proline residues in the fibronectin type III superfamily

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

How evolutionary pressure against protein aggregation shaped chaperone specificity

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Aggregation propensity of the human proteome

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Prevention of amyloid-like aggregation as a driving force of protein evolution.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Amyloid formation by globular proteins under native conditions

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Experimental free energy surfaces reveal the mechanisms of maintenance of protein solubility

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Arrangement of subunits and ordering of beta-strands in an amyloid sheet

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Delicate balance between functionally required flexibility and aggregation risk in a β-rich protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Functional interactions as a survival strategy against abnormal aggregation

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Fully metallated S134N Cu,Zn-superoxide dismutase displays abnormal mobility and intermolecular contacts in solution

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Characterizing intermolecular interactions that initiate native-like protein aggregation

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Natural beta-sheet proteins use negative design to avoid edge-to-edge aggregation

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

The degree of structural protection at the edge beta-strands determines the pathway of amyloid formation in globular proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Rationally designed mutations convert de novo amyloid-like fibrils into monomeric beta-sheet proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

"Native-like aggregation" of the acylphosphatase from Sulfolobus solfataricus and its biological implications

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Aggregation of the Acylphosphatase from Sulfolobus solfataricus: the folded and partially unfolded states can both be precursors for amyloid formation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Structural and dynamics characteristics of acylphosphatase from Sulfolobus solfataricus in the monomeric state and in the initial native-like aggregates

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Exploring the mechanism of formation of native-like and precursor amyloid oligomers for the native acylphosphatase from Sulfolobus solfataricus.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Are proteins well-packed?

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Inference of macromolecular assemblies from crystalline state

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Protein structure, neighbor effect, and a new index of amino acid dissimilarities.

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Crystal structure and anion binding in the prokaryotic hydrogenase maturation factor HypF acylphosphatase-like domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Studying the folding process of the acylphosphatase from Sulfolobus solfataricus. A comparative analysis with other proteins from the same superfamily

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Scaling and assessment of data quality

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Phasercrystallographic software

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

PHENIX: a comprehensive Python-based system for macromolecular structure solution

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

REFMAC5 dictionary: organization of prior chemical knowledge and guidelines for its use

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Features and development of Coot

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

A series of PDB related databases for everyday needs

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Metastability of Native Proteins and the Phenomenon of Amyloid Formation

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Probing Solvent Accessibility of Transthyretin Amyloid by Solution NMR Spectroscopy

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1111%2FFEBS.12861

21 January 2018

Identifiers

DOI

10.1111/FEBS.12861

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1811807

OpenCitations bibliographic resource ID

1811807

1 reference