117657-37-1Relevant academic research and scientific papers
Ni complexes of an alane/tris(phosphine) ligand built around a strongly Lewis acidic tris(: N -pyrrolyl)aluminum
Lai, Qingheng,Cosio, Mario N.,Ozerov, Oleg V.
, p. 14845 - 14848 (2020)
Syntheses of a new tripodal alane/tris(phosphine) ligand (AlP3) based on 2-(diisopropylphosphino)pyrrole, and AlP3-supported Ni complexes are reported. The central tris(pyrrolyl)aluminum moiety acts as a stronger Lewis acid towards Ni than other related group 13 element-centered tripodal ligands, as demonstrated by the binding of H2 to Ni and the ease of reduction. This journal is
CONVENIENT SYNTHETIC EQUIVALENTS OF 2-LITHIOPYRROLE AND 2,5-DILITHIOPYRROLE.
Chen, Wha,Cava, Michael P.
, p. 6025 - 6026 (1987)
Bromination of pyrrole by 1,3-dibromo-5,5-dimethylhydantoin, followed by direct reaction with BOC anhydride and DMAP, affords the stable N-BOC derivatives of 2-bromopyrrole and 2,5-dibromopyrrole.Lithium-halogen exchange of the latter with n-butyllithium generates the N-BOC derivatives of 2-lithiopyrrole, 2,5-dilithiopyrrole or 5-bromo-2-lithiopyrrole,which react with various electrophiles to give substituted N-BOC pyrroles in excellent yield.
Synthesis of α-monobrominated pyrrole derivatives
Groenendaal,Van Loo,Vekemans,Meijer
, p. 1589 - 1600 (1995)
Surprisingly stable N-t-BOC-2-bromo-4-hexyl-pyrrole is prepared from N-t-BOC-2-trimethylstannyl-4-hexyl-pyrrole using N-bromosuccinimide as reagent. The bromo-stannyl exchange reaction is performed quantitatively in THF at -70°C under inert atmosphere. Si
GRP94 SELECTIVE INHIBITORS AND USES THEREOF
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Paragraph 0112, (2018/05/24)
The present technology provides compounds according to Formula I or Formula III as well as compositions including such compounds useful for the treatment of metastatic cancer and/or glaucoma.
Transformation of the non-selective aminocyclohexanol-based Hsp90 inhibitor into a Grp94-seletive scaffold
Mishra, Sanket J.,Ghosh, Suman,Stothert, Andrew R.,Dickey, Chad A.,Blagg, Brian S. J.
, p. 244 - 253 (2017/12/30)
Glucose regulated protein 94 kDa, Grp94, is the endoplasmic reticulum (ER) localized isoform of heat shock protein 90 (Hsp90) that is responsible for the trafficking and maturation of toll-like receptors, immunoglobulins, and integrins. As a result, Grp94 has emerged as a therapeutic target to disrupt cellular communication, adhesion, and tumor proliferation, potentially with fewer side effects compared to pan-inhibitors of all Hsp90 isoforms. Although, the N-terminal ATP binding site is highly conserved among all four Hsp90 isoforms, recent cocrystal structures of Grp94 have revealed subtle differences between Grp94 and other Hsp90 isoforms that has been exploited for the development of Grp94-selective inhibitors. In the current study, a structure-based approach has been applied to a Grp94 nonselective compound, SNX 2112, which led to the development of 8j (ACO1), a Grp94-selective inhibitor that manifests -440 nM affinity and ≥200-fold selectivity against cytosolic Hsp90 isoforms.
Original design of fluorescent ligands by fusing BODIPY and melatonin neurohormone
Thireau, Jeremy,Marteaux, Justine,Delagrange, Philippe,Lefoulon, Francois,Dufourny, Laurence,Guillaumet, Gerald,Suzenet, Franck
supporting information, p. 158 - 161 (2014/03/21)
An original design and synthesis of fluorescent ligands for melatonin receptor studies is presented and consists in the fusion of the endogenous ligand with the fluorescent BODIPY core. Probes I-IV show high affinities for MT1 and MT2 melatonin receptors and exhibit fluorescence properties compatible with cell observation.
