Evidence map›Paper›PMID 31418550›Full record

ArticleBiomacromolecules2019

Nature of Amorphous Hydrophilic Block Affects Self-Assembly of an Artificial Viral Coat Polypeptide.

Lione Willems, Larissa van Westerveld, Stefan Roberts, Isaac Weitzhandler, Carlos Calcines Cruz, Armando Hernandez-Garcia, Ashutosh Chilkoti, Enrico Mastrobattista, John van der Oost, Renko de Vries

Open access · hybridAbstract read
In one paragraph

Article in Biomacromolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.3field-weighted citation impact, top 47% of its field
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

1 citing paper in PubMed, 5 citations in OpenAlex.

  1. Article
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

10 authors at 4 institutions in 3 countries.

Lione Willems
Larissa van Westerveld
Stefan RobertsDepartment of Biomedical Engineering , Duke University , Durham , North Carolina 27708 , United States.
Isaac WeitzhandlerDepartment of Biomedical Engineering , Duke University , Durham , North Carolina 27708 , United States.
Carlos Calcines CruzInstitute of Chemistry, Department of Chemistry of Biomacromolecules , National Autonomous University of Mexico , 04510 Mexico City , Mexico.
Armando Hernandez-GarciaInstitute of Chemistry, Department of Chemistry of Biomacromolecules , National Autonomous University of Mexico , 04510 Mexico City , Mexico.
Ashutosh ChilkotiDepartment of Biomedical Engineering , Duke University , Durham , North Carolina 27708 , United States.
Enrico MastrobattistaDepartment of Pharmaceutics, Utrecht Institute of Pharmaceutical Sciences (UIPS), Faculty of Science , Utrecht University , Universiteitsweg 99 , 3584 CG Utrecht , The Netherlands.ORCID 0000-0002-6745-2015
John van der Oost
Wageningen University & Research · NLDuke University · USUniversidad Nacional Autónoma de México · MXUtrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Consensus motifs for sequences of both crystallizable and amorphous blocks in silks and natural structural analogues of silks vary widely. To design novel silklike polypeptides, an important question is therefore how the nature of either the crystallizable or the amorphous block affects the self-assembly and resulting physical properties of silklike polypeptides. We address herein the influence of the amorphous block on the self-assembly of a silklike polypeptide that was previously designed to encapsulate single DNA molecules into rod-shaped viruslike particles. The polypeptide has a triblock architecture, with a long N-terminal amorphous block, a crystallizable midblock, and a C-terminal DNA-binding block. We compare the self-assembly behavior of a triblock with a very hydrophilic collagen-like amorphous block (GXaaYaa)

Indexed as

Protein MultimerizationAmino Acid MotifsCapsidCapsid ProteinsCollagenCrystallizationDNA, ViralElastinHydrophobic and Hydrophilic InteractionsPeptidesSilkCapsid ProteinsCollagenDNA, ViralElastinPeptidesSilk

Identifiers

PMID31418550
PMCPMC6794640
OpenAlexW2968598428

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.