Evidence map›Paper›PMID 34349760›Full record

ReviewFrontiers in immunology2021

Structure-Function Relationships of Covalent and Non-Covalent BTK Inhibitors.

Rula Zain, Mauno Vihinen

Abstract readReview
In one paragraph

Review in Frontiers in immunology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed.

  1. Review
  2. Article
  3. Review
  4. Article
  5. CHARMM-GUIbioRxiv : the preprint server for biology · 2026
    Article
  6. Review
  7. Review
  8. Review
  9. Review
  10. Review
  11. Current and future landscape of Bruton tyrosine kinase inhibitors in allergy.The Journal of allergy and clinical immunology · 2025
    Review
  12. Beyond relapses: How BTK inhibitors are shaping the future of progressive MS treatment.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2025
    Review
  13. Review
  14. Review
  15. Article
  16. Review
  17. Review
  18. Article
  19. New Means and Challenges in the Targeting of BTK.Clinical cancer research : an official journal of the American Association for Cancer Research · 2024
    Review
  20. 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

2 authors.

Rula ZainDepartment of Laboratory Medicine, Clinical Research Centre, Karolinska Institutet, Karolinska University Hospital, Huddinge, Sweden.
Mauno VihinenDepartment of Experimental Medical Science, Lund University, Lund, Sweden.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Low-molecular weight chemical compounds have a longstanding history as drugs. Target specificity and binding efficiency represent major obstacles for small molecules to become clinically relevant. Protein kinases are attractive cellular targets; however, they are challenging because they present one of the largest protein families and share structural similarities. Bruton tyrosine kinase (BTK), a cytoplasmic protein tyrosine kinase, has received much attention as a promising target for the treatment of B-cell malignancies and more recently autoimmune and inflammatory diseases. Here we describe the structural properties and binding modes of small-molecule BTK inhibitors, including irreversible and reversible inhibitors. Covalently binding compounds, such as ibrutinib, acalabrutinib and zanubrutinib, are discussed along with non-covalent inhibitors fenebrutinib and RN486. The focus of this review is on structure-function relationships.

Indexed as

Agammaglobulinaemia Tyrosine KinaseAnimalsAntineoplastic AgentsBinding SitesHumansModels, MolecularMolecular Targeted TherapyNeoplasmsProtein BindingProtein ConformationProtein Kinase InhibitorsStructure-Activity RelationshipAgammaglobulinaemia Tyrosine KinaseAntineoplastic AgentsBTK protein, humanProtein Kinase InhibitorsacalabrutinibBTK inhibitorscovalent and non-covalent bindingfenebrutinibibrutinibprotein-inhibitor interactionsstructure-function relationshipzanubrutinib

Identifiers

PMID34349760
PMCPMC8328433

What OpenQuestion holds

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Registered trials

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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.