(Q51963068)

English

Structures of a peptide fragment of beta2-microglobulin studied by replica-exchange molecular dynamics simulations - towards the understanding of the mechanism of amyloid formation.

scientific article published in October 2005

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scholarly article

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Europe PubMed Central

PubMed publication ID

19 April 2018

http://europepmc.org/abstract/MED/16198346

Structures of a peptide fragment of beta2-microglobulin studied by replica-exchange molecular dynamics simulations - towards the understanding of the mechanism of amyloid formation. (English)

1 reference

Europe PubMed Central

PubMed publication ID

19 April 2018

http://europepmc.org/abstract/MED/16198346

4

1 reference

Europe PubMed Central

PubMed publication ID

19 April 2018

http://europepmc.org/abstract/MED/16198346

author name string

Masamichi Nishino

1

1 reference

Europe PubMed Central

PubMed publication ID

19 April 2018

http://europepmc.org/abstract/MED/16198346

Yuji Sugita

2

1 reference

Europe PubMed Central

PubMed publication ID

19 April 2018

http://europepmc.org/abstract/MED/16198346

Takao Yoda

3

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Europe PubMed Central

PubMed publication ID

19 April 2018

http://europepmc.org/abstract/MED/16198346

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publication date

1 October 2005

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Europe PubMed Central

PubMed publication ID

19 April 2018

http://europepmc.org/abstract/MED/16198346

1 reference

Europe PubMed Central

PubMed publication ID

19 April 2018

http://europepmc.org/abstract/MED/16198346

579

1 reference

Europe PubMed Central

PubMed publication ID

19 April 2018

http://europepmc.org/abstract/MED/16198346

24

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Europe PubMed Central

PubMed publication ID

19 April 2018

http://europepmc.org/abstract/MED/16198346

5425-5429

1 reference

Europe PubMed Central

PubMed publication ID

19 April 2018

http://europepmc.org/abstract/MED/16198346

Common core structure of amyloid fibrils by synchrotron X-ray diffraction.

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.068

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Core and heterogeneity of beta2-microglobulin amyloid fibrils as revealed by H/D exchange

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.068

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Mapping the core of the beta(2)-microglobulin amyloid fibril by H/D exchange

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.068

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Investigation of a peptide responsible for amyloid fibril formation of beta 2-microglobulin by achromobacter protease I.

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.068

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Amyloidogenic synthetic peptides of β2-microglobulin—a role of the disulfide bond

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https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.068

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Solution conformations and thermodynamics of structured peptides: molecular dynamics simulation with an implicit solvation model.

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.068

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Molecular dynamics simulations of unfolding and refolding of a beta-hairpin fragment of protein G

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.068

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Understanding beta-hairpin formation

1 reference

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Dynamics and thermodynamics of beta-hairpin assembly: insights from various simulation techniques

1 reference

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Mechanisms and kinetics of beta-hairpin formation

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.068

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The free energy landscape for beta hairpin folding in explicit water

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.068

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Conformational transition states of a beta-hairpin peptide between the ordered and disordered conformations in explicit water

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.068

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Generalized-ensemble algorithms for molecular simulations of biopolymers

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.068

21 January 2018

Replica-exchange molecular dynamics method for protein folding

1 reference

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Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features

1 reference

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Comparison of simple potential functions for simulating liquid water

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.068

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A surprising simplicity to protein folding.

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.068

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Folding dynamics and mechanism of beta-hairpin formation

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.068

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Stabilities and conformations of Alzheimer's beta -amyloid peptide oligomers (Abeta 16-22, Abeta 16-35, and Abeta 10-35): Sequence effects

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.068

21 January 2018

Core structure of amyloid fibril proposed from IR-microscope linear dichroism

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.068

21 January 2018

Insights into the amyloid folding problem from solid-state NMR

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.068

21 January 2018

β-sheet formation in BPTI(16–36) by Monte Carlo simulated annealing

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.068

21 January 2018

Comparisons of force fields for proteins by generalized-ensemble simulations

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.068

21 January 2018

Secondary-structure preferences of force fields for proteins evaluated by generalized-ensemble simulations

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.068

21 January 2018

Helix-coil transitions of amino-acid homo-oligomers in aqueous solution studied by multicanonical simulations

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2005.08.068

21 January 2018

Establishment of a kinetic model of dialysis-related amyloid fibril extensionin vitro

1 reference

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21 January 2018

Identifiers

10.1016/J.FEBSLET.2005.08.068

1 reference

Europe PubMed Central

PubMed publication ID

19 April 2018

http://europepmc.org/abstract/MED/16198346

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

19 April 2018

http://europepmc.org/abstract/MED/16198346

ResearchGate publication ID

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