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The DOI matches its Crossref record; 124 of the 124 references it cites were found in a registry or an index.

Properties of FDA-approved small molecule protein kinase inhibitors: A 2023 update

Roskoski, Robert·2023·Pharmacological Research
DOI 10.1016/j.phrs.2022.106552
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Abstract

Owing to the dysregulation of protein kinase activity in many diseases including cancer, this enzyme family has become one of the most important drug targets in the 21st century. There are 72 FDA-approved therapeutic agents that target about two dozen different protein kinases and three of these drugs were approved in 2022. Of the approved drugs, twelve target protein-serine/threonine protein kinases, four are directed against dual specificity protein kinases (MEK1/2), sixteen block nonreceptor protein-tyrosine kinases, and 40 target receptor protein-tyrosine kinases. The data indicate that 62 of these drugs are prescribed for the treatment of neoplasms (57 against solid tumors including breast, lung, and colon, ten against nonsolid tumors such as leukemia, and four against both solid and nonsolid tumors: acalabrutinib, ibrutinib, imatinib, and midostaurin). Four drugs (abrocitinib, baricitinib, tofacitinib, upadacitinib) are used for the treatment of inflammatory diseases (atopic dermatitis, psoriatic arthritis, rheumatoid arthritis, Crohn disease, and ulcerative colitis). Of the 72 approved drugs, eighteen are used in the treatment of multiple diseases. The following three drugs received FDA approval in 2022 for the treatment of these specified diseases: abrocitinib (atopic dermatitis), futibatinib (cholangiocarcinomas), pacritinib (myelofibrosis). All of the FDA-approved drugs are orally effective with the exception of netarsudil, temsirolimus, and trilaciclib. This review summarizes the physicochemical properties of all 72 FDA-approved small molecule protein kinase inhibitors including lipophilic efficiency and ligand efficiency.

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Image 1
CC-BY-NC-ND · From the PDF
Fig. 1 (A) Overview of active FGFR1 with bound AMP-PNP (adenylyl imidodiphosphate) and (B) its C-spine and R-spine residues. (C) The α Cout and DFG-Din structure of dormant Abl and (D) its C-spine, R-spine, and shell residues. (E) Overview of the DGF-Dout α Cin structure of JAK2 and (F) its C-spine and R-spine residues. AS, activation segment; CL, catalytic loop. GRL, glycine-rich loop. Figs. 1, 2, 5, and 6 were prepared using the PyMOL Molecular Graphics System Version 1.5.0.4 Schr ¨ odinger, LLC.
Fig. 1 (A) Overview of active FGFR1 with bound AMP-PNP (adenylyl imidodiphosphate) and (B) its C-spine and R-spine residues. (C) The α Cout and DFG-Din structure of dormant Abl and (D) its C-spine, R-spine, and shell residues. (E) Overview of the DGF-Dout α Cin structure of JAK2 and (F) its C-spine and R-spine residues. AS, activation segment; CL, catalytic loop. GRL, glycine-rich loop. Figs. 1, 2, 5, and 6 were prepared using the PyMOL Molecular Graphics System Version 1.5.0.4 Schr ¨ odinger, LLC.CC-BY-NC-ND · From the PDF
Image 3
CC-BY-NC-ND · From the PDF
Fig. 3 The location of the KLIFS residues within a generic protein kinase domain. Act Seg, activation segment. Residues in gray circles are found in the front cleft; blue circles, gate area; yellow circles, back cleft.
Fig. 3 The location of the KLIFS residues within a generic protein kinase domain. Act Seg, activation segment. Residues in gray circles are found in the front cleft; blue circles, gate area; yellow circles, back cleft.CC-BY-NC-ND · From the PDF
Fig. 4 (A -E). Chemical structures of selected protein kinase ligands.
Fig. 4 (A -E). Chemical structures of selected protein kinase ligands.CC-BY-NC-ND · From the PDF
Fig. 5 (A) Abrocitinib-JAK1. (B) Abrocitinib-JAK2. (C) Futibatinib-FGFR1. The respective PDB ID numbers are listed. The drug carbon atoms are colored yellow and the dashed lines represent polar bonds. CL, catalytic loop.
Fig. 5 (A) Abrocitinib-JAK1. (B) Abrocitinib-JAK2. (C) Futibatinib-FGFR1. The respective PDB ID numbers are listed. The drug carbon atoms are colored yellow and the dashed lines represent polar bonds. CL, catalytic loop.CC-BY-NC-ND · From the PDF
Fig. 6 (A) Overview of the structure of human Abl-1b illustrating the SH3-SH2 inhibitory domains including the RT loop interacting with the protein kinase domain (SH1). (B, C) Myristate bound to mouse Abl. (D, E) DPH bound to human Abl. (F, G) Asciminib bound to human Abl. AS, activation segment; GRL, glycine-rich loop; L, ligand.
Fig. 6 (A) Overview of the structure of human Abl-1b illustrating the SH3-SH2 inhibitory domains including the RT loop interacting with the protein kinase domain (SH1). (B, C) Myristate bound to mouse Abl. (D, E) DPH bound to human Abl. (F, G) Asciminib bound to human Abl. AS, activation segment; GRL, glycine-rich loop; L, ligand.CC-BY-NC-ND · From the PDF

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  1. Bechman K., Galloway G.B., Winthrop K.L. Small-molecule protein kinase inhibitors and the risk of fungal infections. Curr Fungal Infect Rep. 10.1007/s12281–019-00350-w. · DOI

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Metadata

Authors
Roskoski, R.
Venue
Pharmacological Research
Publisher
Elsevier BV
Published
2023-01
Volume
187
Pages
106552
ISSN
1043-6618
DOI
10.1016/j.phrs.2022.106552
Cited by
273
References
124
Language
en
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Roskoski, R. (2023). Properties of FDA-approved small molecule protein kinase inhibitors: A 2023 update. Pharmacological Research. https://doi.org/10.1016/j.phrs.2022.106552

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