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2-Amino-5-nitro-1-naphthalenesulfonic acid is an organic compound with the chemical formula C10H9N2O4S. It is a yellow crystalline solid that is soluble in water and has a molecular weight of 260.25 g/mol. 2-Amino-5-nitro-1-naphthalenesulfonic acid is a derivative of naphthalene, featuring an amino group at the 2-position, a nitro group at the 5-position, and a sulfonic acid group at the 1-position. It is used in various applications, including as an intermediate in the synthesis of dyes and pigments, as well as in the production of certain pharmaceuticals. Due to its chemical structure, it may exhibit properties such as acidity from the sulfonic acid group and basicity from the amino group, making it a versatile building block in organic chemistry.

6025-92-9

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6025-92-9 Usage

Check Digit Verification of cas no

The CAS Registry Mumber 6025-92-9 includes 7 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 4 digits, 6,0,2 and 5 respectively; the second part has 2 digits, 9 and 2 respectively.
Calculate Digit Verification of CAS Registry Number 6025-92:
(6*6)+(5*0)+(4*2)+(3*5)+(2*9)+(1*2)=79
79 % 10 = 9
So 6025-92-9 is a valid CAS Registry Number.

6025-92-9Relevant academic research and scientific papers

Aminothiazoles as Potent and Selective Sirt2 Inhibitors: A Structure-Activity Relationship Study

Schiedel, Matthias,Rumpf, Tobias,Karaman, Berin,Lehotzky, Attila,Oláh, Judit,Gerhardt, Stefan,Ovádi, Judit,Sippl, Wolfgang,Einsle, Oliver,Jung, Manfred

, p. 1599 - 1612 (2016/03/05)

Sirtuins are NAD+-dependent protein deacylases that cleave off acetyl but also other acyl groups from the ε-amino group of lysines in histones and other substrate proteins. Dysregulation of human Sirt2 (hSirt2) activity has been associated with the pathogenesis of cancer, inflammation, and neurodegeneration, which makes the modulation of hSirt2 activity a promising strategy for pharmaceutical intervention. The sirtuin rearranging ligands (SirReals) have recently been discovered by us as highly potent and isotype-selective hSirt2 inhibitors. Here, we present a well-defined structure-activity relationship study, which rationalizes the unique features of the SirReals and probes the limits of modifications on this scaffold regarding inhibitor potency. Moreover, we present a crystal structure of hSirt2 in complex with an optimized SirReal derivative that exhibits an improved in vitro activity. Lastly, we show cellular hyperacetylation of the hSirt2 targeted tubulin caused by our improved lead structure.

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