✦ LIBER ✦

Interaction of reversible inhibitors with catalytic centers and allosteric sites of cholinesterases

✍ Scribed by V. D. Tonkopii; V. B. Prozorovskii; I. M. Suslova

Publisher: Springer US
Year: 1976
Tongue: English
Weight: 334 KB
Volume: 82
Category: Article
ISSN: 0007-4888
DOI: 10.1007/bf00785549

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

A simple method of assessing competitive

A simple method of assessing competitive interaction of reversible inhibitors with cholinesterases

✍ V. D. Tonkopii; V. B. Prozorovskii; M. G. Konstorum 📂 Article 📅 1975 🏛 Springer US 🌐 English ⚖ 205 KB

Granzyme M: characterization with sites

Granzyme M: characterization with sites of post-translational modification and specific sites of interaction with substrates and inhibitors

✍ Rukhshan Khurshid; Mahjabeen Saleem; Muhammad Saleem Akhtar; Asmat Salim 📂 Article 📅 2010 🏛 Springer 🌐 English ⚖ 315 KB

ChemInform Abstract: Docking of Noncompe

ChemInform Abstract: Docking of Noncompetitive Inhibitors into Dengue Virus Type 2 Protease: Understanding the Interactions with Allosteric Binding Sites.

✍ Rozana Othman; Tan Siew Kiat; Norzulaani Khalid; Rohana Yusof; E. Irene Newhouse 📂 Article 📅 2008 🏛 John Wiley and Sons ⚖ 15 KB 👁 1 views

ChemInform Abstract: Cholinesterases: St

ChemInform Abstract: Cholinesterases: Structure of the Active Site and Mechanism of the Effect of Cholinergic Receptor Blockers on the Rate of Interaction with Ligands

✍ A. M. Antokhin; E. T. Gainullina; V. F. Taranchenko; S. B. Ryzhikov; D. K. Yavae 📂 Article 📅 2011 🏛 John Wiley and Sons ⚖ 20 KB 👁 2 views

Interaction of the active site of the Ni

Interaction of the active site of the Ni–Fe–Se hydrogenase fromDesulfovibrio vulgarisHildenborough with carbon monoxide and oxygen inhibitors

✍ Cristina Gutiérrez-Sánchez; Olaf Rüdiger; Víctor M. Fernández; Antonio L. De Lac 📂 Article 📅 2010 🏛 John Wiley and Sons 🌐 English ⚖ 275 KB

Structure-Based Synthetic Mimicry of Dis

Structure-Based Synthetic Mimicry of Discontinuous Protein Binding Sites: Inhibitors of the Interaction of Mena EVH1 Domain with Proline-Rich Ligands

✍ Cornelia Hunke; Tatjana Hirsch; Jutta Eichler 📂 Article 📅 2006 🏛 John Wiley and Sons 🌐 English ⚖ 393 KB 👁 1 views

## Abstract The Mena EVH1 domain, a protein‐interaction module involved in actin‐based cell motility, recognizes proline‐rich ligand motifs, which are also present in the sequence of the surface protein ActA of __Listeria monocytogenes__. The interaction of ActA with host Mena EVH1 enables the bact