Huntingtin: A Protein with a Peculiar Solvent Accessible Surface.

Giulia Babbi, Castrense Savojardo, Pier Luigi Martelli, Rita Casadio

Open access · goldAbstract read

In one paragraph

Article in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it

0cells of the map it votes in

0citing papers in PubMed

0.3field-weighted citation impact, top 52% 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

0 citing papers in PubMed, 4 citations in OpenAlex.

No citing paper in PubMed yet.

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

4 authors at 2 institutions in 1 country.

Giulia BabbiBiocomputing Group, University of Bologna, Via San Giacomo 9/2, 40126 Bologna, Italy.ORCID 0000-0002-9816-4737

Castrense SavojardoBiocomputing Group, University of Bologna, Via San Giacomo 9/2, 40126 Bologna, Italy.ORCID 0000-0002-7359-0633

Pier Luigi MartelliBiocomputing Group, University of Bologna, Via San Giacomo 9/2, 40126 Bologna, Italy.ORCID 0000-0002-0274-5669

Rita CasadioBiocomputing Group, University of Bologna, Via San Giacomo 9/2, 40126 Bologna, Italy.ORCID 0000-0002-7462-7039

University of Bologna · ITInstitute of Biomembranes, Bioenergetics and Molecular Biotechnologies · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Taking advantage of the last cryogenic electron microscopy structure of human huntingtin, we explored with computational methods its physicochemical properties, focusing on the solvent accessible surface of the protein and highlighting a quite interesting mix of hydrophobic and hydrophilic patterns, with the prevalence of the latter ones. We then evaluated the probability of exposed residues to be in contact with other proteins, discovering that they tend to cluster in specific regions of the protein. We then found that the remaining portions of the protein surface can contain calcium-binding sites that we propose here as putative mediators for the protein to interact with membranes. Our findings are justified in relation to the present knowledge of huntingtin functional annotation.

Indexed as

Computational BiologyBinding SitesCalciumHumansHuntingtin ProteinHydrophobic and Hydrophilic InteractionsModels, MolecularProtein BindingProteinsSolventsSurface PropertiesCalciumHTT protein, humanHuntingtin ProteinProteinsSolventscalcium ion–binding sitehuntingtinprotein–membrane interactionsprotein–protein interactionprotein surface annotation

Identifiers

PMID33809039

DOI10.3390/ijms22062878

PMCPMC8001614

OpenAlexW3136853032

What OpenQuestion holds

Textmetadata

LicenceCC BY

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.