221244-14-0 Usage
Description
1-NM-PP1 is a cell-permeable inhibitor specifically designed to target and inhibit kinases that have been mutated by a single base substitution to become 'analog sensitive' (as), as compared to their wild-type counterparts. It was initially developed to inhibit v-Src-as1, a rationally engineered v-Src tyrosine kinase, with high potency and specificity. The compound has a white crystalline solid appearance and has been utilized to study the functions of various kinases in mammalian and yeast systems.
Uses
Used in Pharmaceutical Research:
1-NM-PP1 is used as a potent and specific inhibitor for [application reason] studying the functions of mutated kinases in both mammalian and yeast systems. Its high potency and unique specificity make it a valuable tool in pharmaceutical research for understanding the roles of these kinases in cellular processes and potential therapeutic applications.
Used in Kinase Inhibition:
1-NM-PP1 is used as a tyrosine kinase inhibitor for [application reason] preferentially inhibiting mutated, analog-sensitive kinases over their wild-type counterparts. This selective inhibition allows for a more targeted approach in studying the effects of these mutated kinases on cellular processes and potential therapeutic interventions.
Used in Cancer Research:
1-NM-PP1 is used as a research tool for [application reason] elucidating the roles of specific mutated kinases in cancer development and progression. By inhibiting these kinases, researchers can gain insights into the molecular mechanisms underlying cancer and identify potential therapeutic targets for cancer treatment.
Used in Drug Development:
1-NM-PP1 is used as a lead compound for [application reason] developing novel inhibitors targeting mutated kinases associated with various diseases, including cancer. Its high potency and specificity make it a promising starting point for the design and synthesis of new drugs with improved efficacy and selectivity.
Used in Cellular Signaling Studies:
1-NM-PP1 is used as a research tool for [application reason] investigating the roles of mutated kinases in cellular signaling pathways. By selectively inhibiting these kinases, researchers can better understand the complex signaling networks involved in cellular processes and identify potential points of intervention for therapeutic purposes.
Used in Yeast Systems:
1-NM-PP1 is used as a specific inhibitor for [application reason] studying the functions of mutated kinases in yeast systems. This allows researchers to gain insights into the conservation of kinase functions across different organisms and identify potential targets for antifungal or other therapeutic applications.
references
[1] bishop ac1, ubersax ja, petsch dt, matheos dp, gray ns, blethrow j, shimizu e, tsien jz, schultz pg, rose md, wood jl, morgan do, shokat km. a chemical switch for inhibitor-sensitive alleles of any protein kinase. nature. 2000 sep 21; 407 (6802): 395-401.
Check Digit Verification of cas no
The CAS Registry Mumber 221244-14-0 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 2,2,1,2,4 and 4 respectively; the second part has 2 digits, 1 and 4 respectively.
Calculate Digit Verification of CAS Registry Number 221244-14:
(8*2)+(7*2)+(6*1)+(5*2)+(4*4)+(3*4)+(2*1)+(1*4)=80
80 % 10 = 0
So 221244-14-0 is a valid CAS Registry Number.
InChI:InChI=1/C20H21N5/c1-20(2,3)25-19-17(18(21)22-12-23-19)16(24-25)11-14-9-6-8-13-7-4-5-10-15(13)14/h4-10,12H,11H2,1-3H3,(H2,21,22,23)
221244-14-0Relevant articles and documents
Discovery of a potent protein kinase D inhibitor: insights in the binding mode of pyrazolo[3,4-d]pyrimidine analogues
Verschueren, Klaas,Cobbaut, Mathias,Demaerel, Joachim,Saadah, Lina,Voet, Arnout R. D.,Van Lint, Johan,De Borggraeve, Wim M.
, p. 640 - 646 (2017/03/30)
In this study, we set out to rationally optimize PKD inhibitors based on the pyrazolo[3,4-d]pyrimidine scaffold. The lead compound for this study was 1-NM-PP1, which was previously found by us and others to inhibit PKD. In our screening we identified one compound (3-IN-PP1) displaying a 10-fold increase in potency over 1-NM-PP1, opening new possibilities for specific protein kinase inhibitors for kinases that show sensitivity towards pyrazolo[3,4-d]pyrimidine derived compounds. Interestingly the observed SAR was not in complete agreement with the commonly observed binding mode where the pyrazolo[3,4-d]pyrimidine compounds are bound in a similar fashion as PKD's natural ligand ATP. Therefore we suggest an alternate binding mode where the compounds are flipped 180 degrees. This possible alternate binding mode for pyrazolo[3,4-d]pyrimidine based compounds could pave the way for a new class of specific protein kinase inhibitors for kinases sensitive towards pyrazolo[3,4-d]pyrmidines.
COMPOSITIONS AND METHODS FOR TREATING TOXOPLASMOSIS. CRYPTOSPORIDIOSIS AND OTHER APICOMPLEXAN PROTOZOAN RELATED DISEASES
-
, (2011/08/21)
Compositions and methods for the treatment of toxoplasmosis-, caused by the infectious eukaryotic parasite Toxoplasma gondii (T, gondii) and for the treatment of ciyptosporidiosis, caused by the infectious eukaryotic parasites Cryptosporidium parvum (C parvuai) and Cnγtosporidium homimus (C. hominus) are described. In particular, the present disclosure is directed to compositions and methods for inhibiting either T. gondii calcium dependent protein kinases (TgCDPKs) or C. parvum and C. hominus calcium dependent protein kinases (CpDPKS) using pyrazolopyriinidine and/or imidazo[l,5-a]pyraziαe inhibitors, of the formula.(I), wherein the variables X. Y, Z, L. R1. and R3 are defined herein.
Generation of monospecific nanomolar tyrosine kinase inhibitors via a chemical genetic approach
Bishop, Anthony C.,Kung, Chi-Yun,Shah, Kavita,Witucki, Laurie,Shokat, Kevan M.,Liu, Yi
, p. 627 - 631 (2007/10/03)
Selective protein kinase inhibitors are highly sought after as tools for studying cellular signal transduction cascades, yet few have been discovered due to the highly conserved fold of kinase catalytic domains. Through a combination of small molecule syn
