862388-11-2Relevant academic research and scientific papers
COMPOSITION FOR TREATMENT AND/OR PREVENTION OF PERIPHERAL NERVE DISORDER
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Paragraph 0188; 0193, (2019/10/29)
The present invention provides a means for treating and/or preventing peripheral nerve disorder by facilitating regeneration of peripheral nerves. Specifically, the present invention provides a composition for treating and/or preventing peripheral nerve d
Lissencephaly therapeutic agent
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Page/Page column 35; 36, (2016/07/27)
An object of the present invention is to provide a medicament and method for treating lissencephaly patients. The present invention provides a lissencephaly therapeutic or preventive agent comprising a compound represented by the general formula (I): wher
LISSENCEPHALY THERAPEUTIC AGENT
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Page/Page column, (2013/10/22)
An object of the present invention is to provide a medicament and method for treating lissencephaly patients. The present invention provides a lissencephaly therapeutic or preventive agent comprising a compound represented by the general formula (I): wher
ALPHA-KETOAMIDE DERIVATIVE, AND PRODUCTION METHOD AND USE THEREOF
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Page/Page column 36, (2008/06/13)
The present invention provides a compound represented by the formula (I): (INSERT CHEMICAL FORMULA) (wherein R1 is a lower alkyl substituted by a lower alkoxy or a heterocyclic group, or a heterocyclic group; R2 is a lower alkyl opti
Exploration of orally available calpain inhibitors: Peptidyl α-ketoamides containing an amphiphile at P3 site
Shirasaki, Yoshihisa,Miyashita, Hiroyuki,Yamaguchi, Masazumi,Inoue, Jun,Nakamura, Masayuki
, p. 4473 - 4484 (2007/10/03)
A novel series of dipeptidyl α-ketoamide derivatives with amphiphile was designed and synthesized as water-soluble calpain inhibitors. The introduction of amphiphiles at the P3 site increased water solubility without loss of membrane permeability and prov
Significance of hydrogen bonding at the S1′ subsite of calpain I
Donkor, Isaac O.,Zheng, Xiaozhang,Han, Jie,Lacy, Calvin,Miller, Duane D.
, p. 1753 - 1755 (2007/10/03)
α-Ketohydroxamates were synthesized as bioisosteres of α-ketoamides. The α-ketohydroxamates were generally more potent than the corresponding α-ketoamides. The potency of the compounds suggests that hydrogen bonding and steric bulk of substituents on the nitrogen atom of the ketoamide moiety influence calpain inhibition.
