49573-30-0Relevant articles and documents
Syntheses of aromatic aldehydes by laccase of pleurotus ostreatus MTCC-1801
Chaurasia, Pankaj Kumar,Yadava, Sudha,Bharati, Shashi Lata,Singh, Sunil Kumar
, p. 2535 - 2544 (2014)
GRAPHICAL ABSTRACT Selective bioconversion of the aromatic methyl group to its aldehyde group is one of the best applications of the laccases. In the present communication, crude laccase, obtained from the liquid culture medium of the fungal strain Pleurotus ostreatus MTCC-1801, has been used for the selective bioconversion of toluene, 3-nitrotoluene, 4-nitrotoluene, 2-fluorotoluene, 4-fluorotoluene, 2-chlorotoluene, 3-chlorotoluene, 4-chlorotoluene, and 3,4-dimethoxytoluene to benzaldehyde, 3-nitrobenzaldehyde, 4-nitrobenzaldehyde, 2-fluorobenzaldehyde, 4-fluorobenzaldehyde, 2-chlorobenzaldehyde, 3-chlorobenzaldehyde, 4-chlorobenzaldehyde, and 3,4-dimethoxybenzaldehyde, respectively, in the presence of 2,2′-azino-bis (3-ethylbenzthiazoline-6-sulfonic acid) diammonium salt (ABTS) as a mediator molecule. Time taken by these conversions was 1-2 h, and average yield of products was more than 93%.
Targeted degradation of the enhancer lysine acetyltransferases CBP and p300
Vannam, Raghu,Sayilgan, Jan,Ojeda, Samuel,Karakyriakou, Barbara,Hu, Eileen,Kreuzer, Johannes,Morris, Robert,Herrera Lopez, Xcanda Ixchel,Rai, Sumit,Haas, Wilhelm,Lawrence, Michael,Ott, Christopher J.
, p. 503 - 12,514 (2021)
The enhancer factors CREB-binding protein (CBP) and p300 (also known as KAT3A and KAT3B) maintain gene expression programs through lysine acetylation of chromatin and transcriptional regulators and by scaffolding functions mediated by several protein-protein interaction domains. Small molecule inhibitors that target some of these domains have been developed; however, they cannot completely ablate p300/CBP function in cells. Here we describe a chemical degrader of p300/CBP, dCBP-1. Leveraging structures of ligand-bound p300/CBP domains, we use in silico modeling of ternary complex formation with the E3 ubiquitin ligase cereblon to enable degrader design. dCBP-1 is exceptionally potent at killing multiple myeloma cells and can abolish the enhancer that drives MYC oncogene expression. As an efficient degrader of this unique class of acetyltransferases, dCBP-1 is a useful tool alongside domain inhibitors for dissecting the mechanism by which these factors coordinate enhancer activity in normal and diseased cells.
MODIFIED PROTEINS AND PROTEIN DEGRADERS
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Paragraph 001195-001197, (2021/12/08)
Provided herein are compounds, pharmaceutical compositions, and methods for binding or degrading target proteins. Further provided herein are compounds having a DNA damage-binding protein 1 (DDB1) binding moiety. Some such embodiments include a linker. Some such embodiments include a target protein binding moiety. Further provided herein are ligand-DDB1 complexes. Further provided herein are in vivo modified DDB1 proteins.
IMIDAZOPIPERAZINONE INHIBITORS OF TRANSCRIPTION ACTIVATING PROTEINS
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Paragraph 0536-0538, (2019/10/20)
The present disclosure relates to heterocyclic compounds and methods which may be useful as inhibitors of transcription activating proteins such as CBP and P300 for the treatment or prevention of diseases such as proliferative diseases, inflammatory disorders, autoimmune diseases, and fibrotic diseases.
