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223,739 results

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Page 1
Did you mean rotein kinase binding (3 results)?
Flavonoids as protein kinase inhibitors for cancer chemoprevention: direct binding and molecular modeling.
Hou DX, Kumamoto T. Hou DX, et al. Antioxid Redox Signal. 2010 Sep 1;13(5):691-719. doi: 10.1089/ars.2009.2816. Antioxid Redox Signal. 2010. PMID: 20070239 Review.
Deregulation of protein kinase function has been implicated in carcinogenesis. The inhibition of protein kinases has emerged as an important target for cancer chemoprevention and therapy. ...Recent studies show that flavonoids can bind directly to some …
Deregulation of protein kinase function has been implicated in carcinogenesis. The inhibition of protein kinases …
A new paradigm for protein kinase inhibition: blocking phosphorylation without directly targeting ATP binding.
Bogoyevitch MA, Fairlie DP. Bogoyevitch MA, et al. Drug Discov Today. 2007 Aug;12(15-16):622-33. doi: 10.1016/j.drudis.2007.06.008. Epub 2007 Aug 2. Drug Discov Today. 2007. PMID: 17706543 Review.
Protein kinases are now recognised as an important class of drug targets. Whilst many protein kinase inhibitors directly interact with the ATP-binding site, Gleevec is a notable example from a new class of allosteric inhibitors that alter pro …
Protein kinases are now recognised as an important class of drug targets. Whilst many protein kinase inhibitors …
Identification of FAM53C as a cytosolic-anchoring inhibitory binding protein of the kinase DYRK1A.
Miyata Y, Nishida E. Miyata Y, et al. Life Sci Alliance. 2023 Oct 6;6(12):e202302129. doi: 10.26508/lsa.202302129. Print 2023 Dec. Life Sci Alliance. 2023. PMID: 37802655 Free PMC article.
The protein kinase DYRK1A encoded in human chromosome 21 is the major contributor to the multiple symptoms observed in Down syndrome patients. ...Here, we identified FAM53C with no hitherto known biological function as a novel suppressive binding partner of D …
The protein kinase DYRK1A encoded in human chromosome 21 is the major contributor to the multiple symptoms observed in Down sy …
Renaissance of Allostery to Disrupt Protein Kinase Interactions.
Leroux AE, Biondi RM. Leroux AE, et al. Trends Biochem Sci. 2020 Jan;45(1):27-41. doi: 10.1016/j.tibs.2019.09.007. Epub 2019 Nov 2. Trends Biochem Sci. 2020. PMID: 31690482 Review.
Protein-protein interactions often regulate the activity of protein kinases by allosterically modulating the conformation of the ATP-binding site. Bidirectional allostery implies that reverse modulation (i.e., from the ATP-binding site to …
Protein-protein interactions often regulate the activity of protein kinases by allosterically modulating the con …
A Ca2+-dependent protein kinase activity associated with serotonin binding protein.
Adlersberg M, Liu KP, Hsiung SC, Ehrlich Y, Tamir H. Adlersberg M, et al. J Neurochem. 1987 Oct;49(4):1105-15. doi: 10.1111/j.1471-4159.1987.tb10000.x. J Neurochem. 1987. PMID: 3040904
A protein kinase activity that copurifies with SBP (SBP-kinase) was partially characterized and compared with calcium/calmodulin-dependent protein kinase II (CAM-PK II). SBP itself is not the enzyme since heating destroyed the protein …
A protein kinase activity that copurifies with SBP (SBP-kinase) was partially characterized and compared with calcium/c …
Structural basis for the action of the drug trametinib at KSR-bound MEK.
Khan ZM, Real AM, Marsiglia WM, Chow A, Duffy ME, Yerabolu JR, Scopton AP, Dar AC. Khan ZM, et al. Nature. 2020 Dec;588(7838):509-514. doi: 10.1038/s41586-020-2760-4. Epub 2020 Sep 14. Nature. 2020. PMID: 32927473 Free PMC article.
Here we report X-ray crystal structures of MEK bound to the scaffold KSR (kinase suppressor of RAS) with various MEK inhibitors, including the clinical drug trametinib. The structures reveal an unexpected mode of binding in which trametinib directly engages KSR at t …
Here we report X-ray crystal structures of MEK bound to the scaffold KSR (kinase suppressor of RAS) with various MEK inhibitors, incl …
Functional classification of protein kinase binding sites using Cavbase.
Kuhn D, Weskamp N, Hüllermeier E, Klebe G. Kuhn D, et al. ChemMedChem. 2007 Oct;2(10):1432-47. doi: 10.1002/cmdc.200700075. ChemMedChem. 2007. PMID: 17694525
Herein we present a method for classifying protein families on the basis of the properties of their active sites. We have developed Cavbase, a method for describing and comparing protein binding pockets, and show its application to the functional classificati …
Herein we present a method for classifying protein families on the basis of the properties of their active sites. We have developed C …
The rapamycin-binding domain of the protein kinase mammalian target of rapamycin is a destabilizing domain.
Edwards SR, Wandless TJ. Edwards SR, et al. J Biol Chem. 2007 May 4;282(18):13395-401. doi: 10.1074/jbc.M700498200. Epub 2007 Mar 9. J Biol Chem. 2007. PMID: 17350953 Free PMC article.
Rapamycin is an immunosuppressive drug that binds simultaneously to the 12-kDa FK506- and rapamycin-binding protein (FKBP12, or FKBP) and the FKBP-rapamycin binding (FRB) domain of the mammalian target of rapamycin (mTOR) kinase. The resulting t …
Rapamycin is an immunosuppressive drug that binds simultaneously to the 12-kDa FK506- and rapamycin-binding protein (FK …
Substrate diversity of the cAMP-dependent protein kinase: regulation based upon multiple binding interactions.
Walsh DA, Glass DB, Mitchell RD. Walsh DA, et al. Curr Opin Cell Biol. 1992 Apr;4(2):241-51. doi: 10.1016/0955-0674(92)90039-f. Curr Opin Cell Biol. 1992. PMID: 1599690 Review.
The proposition is forwarded that the cAMP-dependent protein kinase is one of quite a small class of enzymes wherein differential modes of binding of its multiple substrates make an important contribution to the end physiological response. It is postulated th …
The proposition is forwarded that the cAMP-dependent protein kinase is one of quite a small class of enzymes wherein different …
223,739 results
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