Evidence map›Paper›PMID 17368485›Full record

ArticleJournal of molecular biology2007

Hydrophobic cooperativity as a mechanism for amyloid nucleation.

Ronald D Hills, Charles L Brooks

Abstract read
In one paragraph

Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

33 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Ronald D HillsDepartment of Molecular Biology, Kellogg School of Science and Technology, The Scripps Research Institute, 10550 N. Torrey Pines Road TPC6, La Jolla, CA 92037, USA.
Charles L Brooks

Funding

WEB BASED DOCUMENTATION &TUTORIALS FOR YAMMPP41RR012255 · NCRR · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BROOKS, CHARLES L · 1997 to 2009
$10.4M
PROTEIN FOLDING THERMODYNAMICS AND KINETICSR01GM048807 · NIGMS · SCRIPPS RESEARCH INSTITUTE · PI BROOKS, CHARLES L · 1994 to 2005
$1.9M
NCRR NIH HHS P41 RR012255NCRR NIH HHS RR 12255NIGMS NIH HHS GM 48807NIGMS NIH HHS R01 GM048807
6 · The paper itself

Abstract

The kinetics of amyloid fibril formation are in most cases explained by classical nucleation theory, yet the mechanisms behind nucleation are not well understood. We show using molecular dynamics simulations that the hydrophobic cooperativity in the self-association of the model amyloidogenic peptide STVIYE is sufficient to allow for nucleation-dependent polymerization with a pentamer critical nucleus. The role of electrostatics was also investigated. Novel considerations of the electrostatic solvation energy using the Born-Onsager equation are put forth to rationalize the aggregation of charged peptides and provide new insight into the energetic differences between parallel and antiparallel beta-sheets. Together these results help explain the influence of molecular charge in the class of fibril-forming hexapeptides recently designed by Serrano and collaborators.

Indexed as

Models, BiologicalAmyloidComputer SimulationHydrogen BondingHydrophobic and Hydrophilic InteractionsPeptide FragmentsProtein ConformationStatic ElectricityThermodynamicsAmyloidPeptide Fragments

Identifiers

PMID17368485
PMCPMC1997311

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.