✦ LIBER ✦

New thiol inhibitor of Achromobacter iophagus collagenase : Specificity of the enzyme's S3′ subsite

✍ Scribed by Athanasios YIOTAKIS; Vincent DIVE

Book ID: 115124739
Publisher: John Wiley and Sons
Year: 1986
Tongue: English
Weight: 653 KB
Volume: 160
Category: Article
ISSN: 1432-1327
DOI: 10.1111/j.1432-1033.1986.tb09987.x

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

New thiol inhibitor of Achromobacter iop

New thiol inhibitor of Achromobacter iophagus collagenase : Specificity of the enzyme's S3′ subsite

✍ Athanasios YIOTAKIS; Vincent DIVE 📂 Article 📅 1986 🏛 John Wiley and Sons 🌐 English ⚖ 424 KB

Specificity of the collagenolytic enzyme

Specificity of the collagenolytic enzyme from the fungus Entomophthora coronata: Comparison with the bacterial collagenase from Achromobacter iophagus

✍ Nicole Hurion; Huguette Fromentin; Borivoj Keil 📂 Article 📅 1979 🏛 Elsevier Science 🌐 English ⚖ 652 KB

Computational study of the catalytic dom

Computational study of the catalytic domain of human neutrophil collagenase. Specific role of the S3and S′3subsites in the interaction with a phosphonate inhibitor

✍ Massimiliano Aschi; Danilo Roccatano; Alfredo Di Nola; Carlo Gallina; Enrico Gav 📂 Article 📅 2002 🏛 Springer Netherlands 🌐 English ⚖ 471 KB

Conformationally Restricted Hydantoin-Ba

Conformationally Restricted Hydantoin-Based Peptidomimetics as Inhibitors of Caspase-3 with Basic Groups Allowed at the S3 Enzyme Subsite

✍ Jesús Vázquez; Alicia García-Jareño; Laura Mondragón; Jaime Rubio-Martinez; Enri 📂 Article 📅 2008 🏛 John Wiley and Sons 🌐 English ⚖ 288 KB

Studies on the structural feature of S'1

Studies on the structural feature of S'1 subsite of neprilysin (EC.3.4.24.11): Stereochemical requirement for the enzyme-inhibitor docking process

✍ Denis Danvy; Thierry Monteil; Jean-Christophe Plaquevent; Lucette Duhamel; Pierr 📂 Article 📅 1996 🏛 Elsevier Science 🌐 English ⚖ 187 KB

The preferred conformation of thiorphan during the inhibitor-neprilysin docking process was investigated. A series of achiral inhibitors were tested. This study led to the design of a potent inhibitor, in which the ethylenic bond bears the aryl residue of P'I.

Studies of the antihypertensive effects

Studies of the antihypertensive effects of CL 242,817, a new angiotensin-I converting enzyme inhibitor [S−(R*, s*)]-1-[(3-acetylthio)-3-benzoyl-2-methyl propionyl-L-proline]

✍ Dr. F. M. Lai; P. Cervoni; P. S. Chan; C. A. Shepherd; M. A. Ronsberg; G. J. Qui 📂 Article 📅 1985 🏛 John Wiley and Sons 🌐 English ⚖ 703 KB