Evidence map›Paper›PMID 27553235›Full record

ArticleAdvances in experimental medicine and biology2016

Membrane Protein Crystallisation: Current Trends and Future Perspectives.

Joanne L Parker, Simon Newstead

Open access · hybridAbstract read
In one paragraph

Article in Advances in experimental medicine and biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
14.0field-weighted citation impact, top 1% 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

23 citing papers in PubMed, 51 citations in OpenAlex.

  1. Review
  2. HisScientific reports · 2023
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  4. Studying membrane proteins with MicroED.Biochemical Society transactions · 2022
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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 at 1 institution in 1 country.

Joanne L ParkerDepartment of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK.
Simon NewsteadDepartment of Biochemistry, University of Oxford, Oxford, OX1 3QU, UK. simon.newstead@bioch.ox.ac.uk.
University of Oxford · GB

Funding

Wellcome Trust 102890Wellcome Trust 102890/Z/13/Z
6 · The paper itself

Abstract

Alpha helical membrane proteins are the targets for many pharmaceutical drugs and play important roles in physiology and disease processes. In recent years, substantial progress has been made in determining their atomic structure using X-ray crystallography. However, a major bottleneck still remains; the identification of conditions that give crystals that are suitable for structure determination. Over the past 10 years we have been analysing the crystallisation conditions reported for alpha helical membrane proteins with the aim to facilitate a rational approach to the design and implementation of successful crystallisation screens. The result has been the development of MemGold, MemGold2 and the additive screen MemAdvantage. The associated analysis, summarised and updated in this chapter, has revealed a number of surprisingly successfully strategies for crystallisation and detergent selection.

Indexed as

AnimalsBacterial ProteinsBuffersChemical PrecipitationCrystallizationCrystallography, X-RayDetergentsHumansHydrogen-Ion ConcentrationMembrane ProteinsProtein Structure, SecondarySaltsBacterial ProteinsBuffersDetergentsMembrane ProteinsSaltsCrystallisationDetergent selectionMembrane proteinScreen development

Identifiers

PMID27553235
PMCPMC5033070
OpenAlexW2513984184

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.