Evidence map›Paper›PMID 29857161›Full record

ArticleBiochimica et biophysica acta. Proteins and proteomics2018

Directed evolution and biophysical characterization of a full-length, soluble, human caveolin-1 variant.

Joshua N Smith, Joshua M Edgar, J Mark Balk, Mariam Iftikhar, Jessica C Fong, Tivoli J Olsen, Dmitry A Fishman, Sudipta Majumdar, Gregory A Weiss

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochimica et biophysica acta. Proteins and proteomics, 2018. 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
0.1field-weighted citation impact, top 55% 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, 1 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

9 authors at 1 institution in 1 country.

Joshua N SmithDepartment of Molecular Biology and Biochemistry,University of California, Irvine, CA 92697, USA.
Joshua M EdgarDepartment of Chemistry, University of California, Irvine, CA 92697, USA.
J Mark BalkDepartment of Chemistry, University of California, Irvine, CA 92697, USA.
Mariam IftikharDepartment of Chemistry, University of California, Irvine, CA 92697, USA.
Jessica C FongDepartment of Pharmaceutical Sciences, University of California, Irvine, CA 92697, USA.
Tivoli J OlsenDepartment of Chemistry, University of California, Irvine, CA 92697, USA.
Dmitry A FishmanDepartment of Chemistry, University of California, Irvine, CA 92697, USA.
Sudipta MajumdarDepartment of Chemistry, University of California, Irvine, CA 92697, USA.
Gregory A WeissDepartment of Molecular Biology and Biochemistry,University of California, Irvine, CA 92697, USA; Department of Chemistry, University of California, Irvine, CA 92697, USA. Electronic address: gweiss@uci.edu.
University of California, Irvine · US

Funding

Virus-host interactions: a multi-scale training programT32AI007319 · NIAID · UNIVERSITY OF CALIFORNIA-IRVINE · PI SEMLER, BERT L, SHI, YONGSHENG · 1988 to 2024
$2.4M
Engineering Soluble Aggregation-Prone and Membrane-Bound ProteinsR01GM078528 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI WEISS, GREGORY A. · 2006 to 2010
$1.3M
Membrane Protein Co- Crystallization with Highly Crystalline and Soluble ProteinsR01GM100700 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI WEISS, GREGORY A. · 2012 to 2015
$1.1M
NIAID NIH HHS T32 AI007319NIGMS NIH HHS R01 GM078528NIGMS NIH HHS R01 GM100700
6 · The paper itself

Abstract

Protein engineering by directed evolution can alter proteins' structures, properties, and functions. However, membrane proteins, despite their importance to living organisms, remain relatively unexplored as targets for protein engineering and directed evolution. This gap in capabilities likely results from the tendency of membrane proteins to aggregate and fail to overexpress in bacteria cells. For example, the membrane protein caveolin-1 has been implicated in many cell signaling pathways and diseases, yet the full-length protein is too aggregation-prone for detailed mutagenesis, directed evolution, and biophysical characterization. Using a phage-displayed library of full-length caveolin-1 variants, directed evolution with alternating subtractive and functional selections isolated a full-length, soluble variant, termed cav

Indexed as

Catalytic DomainCaveolin 1Cells, CulturedCyclic AMP-Dependent Protein KinasesDirected Molecular EvolutionEscherichia coliHIV Envelope Protein gp41HumansPeptide LibraryProtein DomainsProtein EngineeringProtein FoldingRNA-Binding ProteinsSignal TransductionThermodynamicsCaveolin 1CAVIN1 protein, humanCyclic AMP-Dependent Protein Kinasesgp41 protein, Human immunodeficiency virus 1HIV Envelope Protein gp41Peptide LibraryRNA-Binding ProteinsBiophysicsCaveolaeCaveolinMembrane proteinsOligomerizationPhage display

Identifiers

PMID29857161
PMCPMC6269214
OpenAlexW2805388810

What OpenQuestion holds

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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.