Evidence map›Paper›PMID 31617192›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2020

Expression, Purification, and Crystallization of HSV-1 Glycoproteins for Structure Determination.

Ellen M White, Samuel D Stampfer, Ekaterina E Heldwein

Abstract read
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Review
  2. Allosteric mechanism of membrane fusion activation in a herpesvirus.bioRxiv : the preprint server for biology · 2024
    Article
  3. Review
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

3 authors.

Ellen M WhiteDepartment of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA, USA.
Samuel D StampferDepartment of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA, USA.
Ekaterina E HeldweinDepartment of Molecular Biology and Microbiology, Tufts University School of Medicine, Boston, MA, USA. katya.heldwein@tufts.edu.

Funding

Structural and mechanistic studies of herpesvirus entry into host cellsDP2OD001996 · OD · TUFTS UNIVERSITY BOSTON · PI HELDWEIN, EKATERINA · 2007 to 2007
$2.5M
NIH HHS DP2 OD001996
6 · The paper itself

Abstract

Herpes simplex viruses utilize glycoproteins displayed on the viral envelope to perform a variety of functions in the viral infectious cycle. Structural and functional studies of these viral glycoproteins can benefit from biochemical, biophysical, and structural analysis of purified proteins. Here, we describe a general protocol for expression and purification of viral glycoproteins from insect cells based on those developed for the HSV-1 gB and HSV-2 gH/gL ectodomains as well as the protocol for crystallization of these glycoproteins. This protocol can be used for generating milligram amounts of wild-type (WT) or mutant gB and gH/gL ectodomains or can be adapted to produce purified ectodomains of glycoproteins from HSV or other herpesviruses for biochemical and structural studies.

Indexed as

Gene ExpressionGlycoproteinsHerpesvirus 1, HumanViral Envelope ProteinsAnimalsCrystallography, X-RayRecombinant ProteinsSf9 CellsSpodopteraGlycoproteinsRecombinant ProteinsViral Envelope ProteinsCrystallographyEctodomainGlycoproteinsHerpes simplex virusesProtein purificationViral entry

Identifiers

PMID31617192
PMCPMC9903252

What OpenQuestion holds

Textmetadata
LicenceTDM
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.