Evidence map›Paper›PMID 24688717›Full record

ReviewComputational and structural biotechnology journal2013

The albumin-binding domain as a scaffold for protein engineering.

Johan Nilvebrant, Sophia Hober

Open access · goldAbstract readReview
In one paragraph

Review in Computational and structural biotechnology journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

44 citing papers in PubMed, 111 citations in OpenAlex.

  1. Phase I Study ofJournal of nuclear medicine : official publication, Society of Nuclear Medicine · 2021
    Trial
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  6. Article
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  9. Article
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  11. Design and evolution of a synthetic small protein scaffold based on the WW domain.Protein science : a publication of the Protein Society · 2025
    Article
  12. Development and Preclinical Evaluation of [Journal of nuclear medicine : official publication, Society of Nuclear Medicine · 2025
    Article
  13. Review
  14. A functional helix shuffled variant of the B domain of Staphylococcus aureus.Protein science : a publication of the Protein Society · 2025
    Article
  15. Article
  16. Article
  17. Therapeutic Fusion Proteins.The AAPS journal · 2023
    Review
  18. Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Johan NilvebrantDivision of Protein Technology, School of Biotechnology, KTH Royal Institute of Technology, AlbaNova University Center, SE-106 91 Stockholm, Sweden.
Sophia HoberDivision of Protein Technology, School of Biotechnology, KTH Royal Institute of Technology, AlbaNova University Center, SE-106 91 Stockholm, Sweden.
AlbaNova · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The albumin-binding domain is a small, three-helical protein domain found in various surface proteins expressed by gram-positive bacteria. Albumin binding is important in bacterial pathogenesis and several homologous domains have been identified. Such albumin-binding regions have been used for protein purification or immobilization. Moreover, improvement of the pharmacokinetics, through the non-covalent association to albumin, by fusing such domains to therapeutic proteins has been shown to be successful. Domains derived from streptococcal protein G and protein PAB from Finegoldia magna, which share a common origin and therefore represent an interesting evolutionary system, have been thoroughly studied structurally and functionally. Their albumin-binding sites have been mapped and these domains form the basis for a wide range of protein engineering approaches. By substitution-mutagenesis they have been engineered to achieve a broader specificity, an increased stability or an improved binding affinity, respectively. Furthermore, novel binding sites have been incorporated either by replacing the original albumin-binding surface, or by complementing it with a novel interaction interface. Combinatorial protein libraries, where several residues have been randomized simultaneously, have generated a large number of new variants with desired binding characteristics. The albumin-binding domain has also been utilized to explore the relationship between three-dimensional structure and amino acid sequence. Proteins with latent structural information built into their sequence, where a single amino acid substitution shifts the equilibrium in favor of a different fold with a new function, have been designed. Altogether, these examples illustrate the versatility of the albumin-binding domain as a scaffold for protein engineering.

Indexed as

affinity maturationaffinity proteinalbuminbispecificprotein domainspecificity

Identifiers

PMID24688717
PMCPMC3962080
OpenAlexW2020558940

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.