876345-13-0Relevant articles and documents
A biocompatible condensation reaction for the labeling of terminal cysteine residues on proteins
Ren, Hongjun,Xiao, Fei,Zhan, Ke,Kim, Young-Pil,Xie, Hexin,Xia, Zuyong,Rao, Jianghong
, p. 9658 - 9662 (2009)
Going live: A protein-labeling method based on the use of a single amino acid taglan N-terminal cysteine residuel and small-molecule probes containing a cyanobenzothiazole (CBT) unit has been used for the specific fluorescence labeling of proteins in vitro and at the surface of live cells (see scheme). This simople ligation reaction proceeds with a high degree of specificity under physiological conditions. Rd: a rhodamine dye; TEV: Tobacco etch virus.
IRAK DEGRADERS AND USES THEREOF
-
Paragraph 00962; 001046; 001049-001050, (2020/06/19)
The present invention provides compounds, compositions thereof, and methods of using the same.
IRAK DEGRADERS AND USES THEREOF
-
Paragraph 2580; 2582, (2019/07/10)
The present invention provides compounds, compositions thereof, and methods of using the same.
MDM2-BASED MODULATORS OF PROTEOLYSIS AND ASSOCIATED METHODS OF USE
-
Paragraph 0376; 0384, (2017/01/31)
The description relates to MDM2 binding compounds, including bifunctional compounds comprising the same, which find utility as modulators of targeted ubiquitination, especially inhibitors of a variety of polypeptides and other proteins which are degraded and/or otherwise inhibited by bifunctional compounds according to the present invention. In particular, the description provides compounds, which contain on one end a ligand which binds to the MDM2 E3 ubiquitin ligase and on the other end a moiety which binds a target protein such that the target protein is placed in proximity to the ubiquitin ligase to effect degradation (and inhibition) of that protein. Compounds can be synthesized that exhibit a broad range of pharmacological activities consistent with the degradation/inhibition of targeted polypeptides of nearly any type.
Zinc(II)cyclen-peptide conjugates interacting with the weak effector binding state of Ras
Schmidt, Florian,Rosnizeck, Ina C.,Spoerner, Michael,Kalbitzer, Hans Robert,K?nig, Burkhard
experimental part, p. 38 - 48 (2011/03/22)
Zinc(II)cyclen-peptide hybrid compounds and bis-zinc(II)cyclen complexes are prepared as potential binders of the guanine nucleotide binding protein Ras, an important molecular switch in cellular signal transduction. The design of the compounds is based on the previous observation that zinc(II)cyclen complexes could serve as lead compounds for inhibitors of Ras-effector interaction and thus be able to interrupt Ras induced signal transduction. Zinc(II)cyclen selectively stabilizes conformational state 1 of active Ras, a conformational state with drastically decreased affinity to effector proteins like Raf-kinase. To achieve higher binding affinities of such Ras-Raf interaction inhibitors, zinc(II)cyclen conjugates with short peptides, derived from the sequence of the Ras-activator SOS, were prepared by solid phase synthesis protocols. Dinuclear bis-zinc(II)cyclen complexes were obtained from alkyne-azide cycloaddition reactions. NMR investigations of the prepared compounds revealed that the peptide conjugates do not lead to an increase in Ras binding affinity of the metal complex-peptide conjugates. The dinuclear zinc complexes lead to an immediate precipitation of the protein prohibiting spectroscopic investigations of their binding.
BisPNA targeting to DNA: Effect of neutral loop on DNA duplex strand invasion by aepPNA-N7G/aepPNA-C substituted peptide nucleic acids
Shirude, Pravin S.,Kumar, Vaijayanti A.,Ganesh, Krishna N.
, p. 5207 - 5215 (2007/10/03)
N7-Alkyl-substituted guanine (N7G) as a CH+ mimic has been introduced into aminoethylglycyl PNA (aegPNA) forming a hairpin through a neutral linker derived from bis(tetraethylene) glycol (teg-teg). These form pH-independent PNA2:DNA
