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Cited by in F6Publishing
For: Hähle A, Geiger TM, Merz S, Meyners C, Tianqi M, Kolos J, Hausch F. FKBP51 and FKBP12.6-Novel and tight interactors of Glomulin. PLoS One 2019;14:e0221926. [PMID: 31490997 DOI: 10.1371/journal.pone.0221926] [Cited by in Crossref: 5] [Cited by in F6Publishing: 5] [Article Influence: 1.7] [Reference Citation Analysis]
Number Citing Articles
1 Queisser A, Seront E, Boon LM, Vikkula M. Genetic Basis and Therapies for Vascular Anomalies. Circ Res 2021;129:155-73. [PMID: 34166070 DOI: 10.1161/CIRCRESAHA.121.318145] [Cited by in Crossref: 22] [Cited by in F6Publishing: 25] [Article Influence: 22.0] [Reference Citation Analysis]
2 Williams E, Riesebos E, Kerr G, Bullock AN. ALK2 Receptor Kinase Association with FKBP12.6 Is Structurally Conserved with the ALK2-FKBP12 Complex. Biomedicines 2021;9:129. [PMID: 33572801 DOI: 10.3390/biomedicines9020129] [Cited by in Crossref: 1] [Cited by in F6Publishing: 1] [Article Influence: 1.0] [Reference Citation Analysis]
3 Nguyen HL, Boon LM, Vikkula M. Genetics of vascular anomalies. Semin Pediatr Surg 2020;29:150967. [PMID: 33069286 DOI: 10.1016/j.sempedsurg.2020.150967] [Cited by in Crossref: 11] [Cited by in F6Publishing: 5] [Article Influence: 5.5] [Reference Citation Analysis]
4 Rein T. Post-translational modifications and stress adaptation: the paradigm of FKBP51. Biochem Soc Trans 2020;48:441-9. [PMID: 32318709 DOI: 10.1042/BST20190332] [Cited by in Crossref: 3] [Cited by in F6Publishing: 3] [Article Influence: 1.5] [Reference Citation Analysis]
5 Rein T. Peptidylprolylisomerases, Protein Folders, or Scaffolders? The Example of FKBP51 and FKBP52. BioEssays 2020;42:1900250. [DOI: 10.1002/bies.201900250] [Cited by in Crossref: 6] [Cited by in F6Publishing: 7] [Article Influence: 3.0] [Reference Citation Analysis]