Ionic strength effects on amyloid formation by amylin are a complicated interplay among Debye screening, ion selectivity, and Hofmeister effects (Q37120817)

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scientific article published on 16 October 2012

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English	Ionic strength effects on amyloid formation by amylin are a complicated interplay among Debye screening, ion selectivity, and Hofmeister effects	scientific article published on 16 October 2012

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scholarly article

1 reference

Europe PubMed Central

18 August 2017

Ionic strength effects on amyloid formation by amylin are a complicated interplay among Debye screening, ion selectivity, and Hofmeister effects (English)

1 reference

Europe PubMed Central

18 August 2017

object named as

Vadim Patsalo

2

0 references

Daniel P Raleigh

object named as

Daniel P Raleigh

4

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author name string

Peter J Marek

1

1 reference

Europe PubMed Central

18 August 2017

David F Green

3

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Europe PubMed Central

18 August 2017

language of work or name

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publication date

16 October 2012

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Europe PubMed Central

18 August 2017

number of pages

13

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Europe PubMed Central

18 August 2017

51

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Europe PubMed Central

18 August 2017

43

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Europe PubMed Central

18 August 2017

8478-8490

1 reference

Europe PubMed Central

18 August 2017

All-atom empirical potential for molecular modeling and dynamics studies of proteins

1 reference

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Efficient microwave-assisted synthesis of human islet amyloid polypeptide designed to facilitate the specific incorporation of labeled amino acids

1 reference

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Amino acid sequence determinants and molecular chaperones in amyloid fibril formation

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1 reference

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CHARMM: the biomolecular simulation program

1 reference

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Atomic structure of the cross-β spine of islet amyloid polypeptide (amylin)

1 reference

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1 reference

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Structure of the cross-beta spine of amyloid-like fibrils

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Increased body temperature accelerates aggregation of the Leu-68-->Gln mutant cystatin C, the amyloid-forming protein in hereditary cystatin C amyloid angiopathy.

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Acid-induced folding of proteins

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Effect of different salt ions on the propensity of aggregation and on the structure of Alzheimer's abeta(1-40) amyloid fibrils.

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Effects of sequential proline substitutions on amyloid formation by human amylin20-29.

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Hydrophobic, Aromatic, and Electrostatic Interactions Play a Central Role in Amyloid Fibril Formation and Stability

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Effect of pH and insulin on fibrillogenesis of islet amyloid polypeptide in vitro

1 reference

https://pubmed.ncbi.nlm.nih.gov/23016872

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Effects of beta cell granule components on human islet amyloid polypeptide fibril formation

1 reference

https://pubmed.ncbi.nlm.nih.gov/23016872

12 December 2020

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Incorporation of Pseudoproline Derivatives Allows the Facile Synthesis of Human IAPP, a Highly Amyloidogenic and Aggregation-Prone Polypeptide

1 reference

https://pubmed.ncbi.nlm.nih.gov/23016872

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1021/BI300574R

1 reference

Europe PubMed Central

18 August 2017

1 reference

Europe PubMed Central

18 August 2017

1 reference

Europe PubMed Central

18 August 2017

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