Evidence map›Paper›PMID 22238299›Full record

ArticleJournal of virology2012

Residues in the hendra virus fusion protein transmembrane domain are critical for endocytic recycling.

Andreea Popa, James R Carter, Stacy E Smith, Lance Hellman, Michael G Fried, Rebecca Ellis Dutch

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

19 citing papers in PubMed, 24 citations in OpenAlex.

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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

6 authors at 1 institution in 1 country.

Andreea PopaDepartment of Molecular and Cellular Biochemistrya and Center for Structural Biology,b University of Kentucky, Lexington, Kentucky, USA.
James R Carter
Stacy E Smith
Lance Hellman
Michael G Fried
Rebecca Ellis Dutch
University of Kentucky · US

Funding

Yessinia autotransporters (Yaps): Structure, function, and host responseU54AI057157 · NIAID · UNIV OF NORTH CAROLINA CHAPEL HILL · PI CROWE, JAMES E · 2003 to 2013
$91.4M
UNDERSTANDING THE MOLECULAR BASIS OF EPIGENETIC TRANSCRIPTIONAL SILENCINGP20RR020171 · NCRR · UNIVERSITY OF KENTUCKY · PI LOUIS HERSH, LOUIS HERSH LOUIS HERSH · 2004 to 2011
$16.5M
SV5 and Hendra virus F protein promoted membrane fusionR01AI051517 · NIAID · UNIVERSITY OF KENTUCKY · PI DUTCH, REBECCA E. · 2002 to 2019
$4.4M
COOPERATIVE INTERACTIONS IN DNA REPAIRR01GM070662 · NIGMS · UNIVERSITY OF KENTUCKY · PI FRIED, MICHAEL G. · 2004 to 2010
$1.4M
NCRR NIH HHS 2P20 RR020171NCRR NIH HHS P20 RR020171NIAID NIH HHS R01 AI051517NIAID NIH HHS R01AI051517NIAID NIH HHS U54 AI057157NIAID NIH HHS U54AI057157NIGMS NIH HHS R01 GM070662NIGMS NIH HHS R01GM070662
6 · The paper itself

Abstract

Hendra virus is a highly pathogenic paramyxovirus classified as a biosafety level four agent. The fusion (F) protein of Hendra virus is critical for promoting viral entry and cell-to-cell fusion. To be fusogenically active, Hendra virus F must undergo endocytic recycling and cleavage by the endosomal/lysosomal protease cathepsin L, but the route of Hendra virus F following internalization and the recycling signals involved are poorly understood. We examined the intracellular distribution of Hendra virus F following endocytosis and showed that it is primarily present in Rab5- and Rab4-positive endosomal compartments, suggesting that cathepsin L cleavage occurs in early endosomes. Hendra virus F transmembrane domain (TMD) residues S490 and Y498 were found to be important for correct Hendra virus F recycling, with the hydroxyl group of S490 and the aromatic ring of Y498 important for this process. In addition, changes in association of isolated Hendra virus F TMDs correlated with alterations to Hendra virus F recycling, suggesting that appropriate TMD interactions play an important role in endocytic trafficking.

Indexed as

EndocytosisAmino Acid MotifsAmino Acid SequenceAnimalsCell LineEndosomesHendra VirusHenipavirus InfectionsHumansMolecular Sequence DataProtein Structure, TertiaryProtein TransportSequence AlignmentViral Fusion ProteinsViral Fusion Proteins

Identifiers

PMID22238299
PMCPMC3302302
OpenAlexW2067051545

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.