Evidence map›Paper›PMID 33514045›Full record

ArticleViruses2021

Protein Binder (ProBi) as a New Class of Structurally Robust Non-Antibody Protein Scaffold for Directed Evolution.

Phuong Ngoc Pham, Maroš Huličiak, Lada Biedermannová, Jiří Černý, Tatsiana Charnavets, Gustavo Fuertes, Štěpán Herynek, Lucie Kolářová, Petr Kolenko, Jiří Pavlíček and 3 more

Open access · goldAbstract read
In one paragraph

Article in Viruses, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. 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

13 authors at 1 institution in 1 country.

Phuong Ngoc PhamInstitute of Biotechnology of the Czech Academy of Sciences, BIOCEV, CZ-25250 Vestec, Czech Republic.
Maroš HuličiakInstitute of Biotechnology of the Czech Academy of Sciences, BIOCEV, CZ-25250 Vestec, Czech Republic.
Lada BiedermannováInstitute of Biotechnology of the Czech Academy of Sciences, BIOCEV, CZ-25250 Vestec, Czech Republic.
Jiří ČernýInstitute of Biotechnology of the Czech Academy of Sciences, BIOCEV, CZ-25250 Vestec, Czech Republic.ORCID 0000-0002-1969-9304
Tatsiana CharnavetsInstitute of Biotechnology of the Czech Academy of Sciences, BIOCEV, CZ-25250 Vestec, Czech Republic.
Gustavo FuertesInstitute of Biotechnology of the Czech Academy of Sciences, BIOCEV, CZ-25250 Vestec, Czech Republic.ORCID 0000-0002-8564-8644
Štěpán HerynekInstitute of Biotechnology of the Czech Academy of Sciences, BIOCEV, CZ-25250 Vestec, Czech Republic.
Lucie KolářováInstitute of Biotechnology of the Czech Academy of Sciences, BIOCEV, CZ-25250 Vestec, Czech Republic.
Petr KolenkoInstitute of Biotechnology of the Czech Academy of Sciences, BIOCEV, CZ-25250 Vestec, Czech Republic.ORCID 0000-0002-4619-9276
Jiří PavlíčekInstitute of Biotechnology of the Czech Academy of Sciences, BIOCEV, CZ-25250 Vestec, Czech Republic.
Jiří ZahradníkInstitute of Biotechnology of the Czech Academy of Sciences, BIOCEV, CZ-25250 Vestec, Czech Republic.
Pavel MikuleckyInstitute of Biotechnology of the Czech Academy of Sciences, BIOCEV, CZ-25250 Vestec, Czech Republic.ORCID 0000-0003-2838-0335
Bohdan SchneiderInstitute of Biotechnology of the Czech Academy of Sciences, BIOCEV, CZ-25250 Vestec, Czech Republic.ORCID 0000-0001-7855-3690
Czech Academy of Sciences, Institute of Biotechnology · CZ

Funding

Czech Academy of Sciences RVO 86652036Czech Science Foundation 19-17398SMinistry of Education, Youth, and Sports of the Czech Republic LM2015043, LM2018127
6 · The paper itself

Abstract

Engineered small non-antibody protein scaffolds are a promising alternative to antibodies and are especially attractive for use in protein therapeutics and diagnostics. The advantages include smaller size and a more robust, single-domain structural framework with a defined binding surface amenable to mutation. This calls for a more systematic approach in designing new scaffolds suitable for use in one or more methods of directed evolution. We hereby describe a process based on an analysis of protein structures from the Protein Data Bank and their experimental examination. The candidate protein scaffolds were subjected to a thorough screening including computational evaluation of the mutability, and experimental determination of their expression yield in

Indexed as

Amino Acid SequenceComputer SimulationDatabases, ProteinDirected Molecular EvolutionInterleukin-10Protein BindingProtein ConformationProtein EngineeringProteinsProtein StabilityRecombinant ProteinsRibosomesInterleukin-10ProteinsRecombinant Proteinscomputational saturationdirected evolutioninterleukin-10protein engineeringprotein scaffoldribosome display

Identifiers

PMID33514045
PMCPMC7911045
OpenAlexW3124189666

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.