Evidence map›Paper›PMID 26517897›Full record

ReviewBiochemical Society transactions2015

A designed repeat protein as an affinity capture reagent.

Elizabeth B Speltz, Rebecca S H Brown, Holly S Hajare, Christian Schlieker, Lynne Regan

Abstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in Biochemical Society transactions, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Intrinsic Disorder in Tetratricopeptide Repeat Proteins.International journal of molecular sciences · 2020
    Article
  2. Protein-Engineered Functional Materials.Advanced healthcare materials · 2019
    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

5 authors.

Elizabeth B SpeltzDepartment of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06511, U.S.A.
Rebecca S H BrownDepartment of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06511, U.S.A.
Holly S HajareDepartment of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06511, U.S.A.
Christian SchliekerDepartment of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06511, U.S.A.
Lynne ReganDepartment of Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06511, U.S.A. Integrated Graduate Program in Physical and Engineering Biology, Yale University, 266 Whitney Avenue, New Haven, CT 06511, U.S.A. Department of Chemistry, Yale University, 266 Whitney Avenue, New Haven, CT 06511, U.S.A. lynne.regan@yale.edu.

Funding

Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
NIGMS NIH HHS T32 GM007223
6 · The paper itself

Abstract

Repeat proteins are an attractive target for protein engineering and design. We have focused our attention on the design and engineering of one particular class: tetratricopeptide repeat (TPR) proteins. In previous work, we have shown that the structure and stability of TPR proteins can be manipulated in a rational fashion [Cortajarena (2011) Prot. Sci. 20: , 1042-1047; Main (2003) Structure 11: , 497-508]. Building on those studies, we have designed and characterized a number of different peptide-binding TPR modules and we have also assembled these modules into supramolecular arrays [Cortajarena (2009) ACS Chem. Biol. 5: , 545-552; Cortajarena (2008) ACS Chem. Biol. 3: , 161-166; Jackrel (2009) Prot. Sci. 18: , 762-774; Kajander (2007) Acta Crystallogr. D Biol. Crystallogr. 63: , 800-811]. Here we focus on the development of one such TPR-peptide interaction for a practical application, affinity purification. We illustrate the general utility of our designed protein interaction. Furthermore, this example highlights how basic research on protein-peptide interactions can lead to the development of novel reagents with important practical applications.

Indexed as

Protein EngineeringRepetitive Sequences, Amino AcidAnimalsCell LineChromatography, AffinityHumansImmobilized ProteinsIndicators and ReagentsLigandsPeptide FragmentsProtein Interaction Domains and MotifsRecombinant Fusion ProteinsImmobilized ProteinsIndicators and ReagentsLigandsPeptide FragmentsRecombinant Fusion Proteinsaffinity reagentantibodyprotein designprotein–protein interactionsprotein purificationrepeat protein

Identifiers

PMID26517897
PMCPMC5683849

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.