Thermodynamic and Structural Effects of Macrocyclic Constraints in Protein−Ligand Interactions-Reference-Cited by-同舟云学术

Thermodynamic and Structural Effects of Macrocyclic Constraints in Protein−Ligand Interactions

Published:2010-08-17 Issue:8 Volume:1 Page:448-452
ISSN:1948-5875
Container-title:ACS Medicinal Chemistry Letters
language:en
Short-container-title:ACS Med. Chem. Lett.

Author:

DeLorbe John E.¹,Clements John H.¹,Whiddon Benjamin B.¹,Martin Stephen F.¹

Affiliation:

1. Department of Chemistry and Biochemistry, The Institute of Cellular and Molecular Biology, and The Texas Institute of Drug and Diagnostic Development, The University of Texas, Austin, Texas 78712

Publisher

American Chemical Society (ACS)

Subject

Organic Chemistry,Drug Discovery,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/ml100142y

Reference13 articles.

1. CONFORMATIONAL RESTRICTION AND/OR STERIC HINDRANCE IN MEDICINAL CHEMISTRY

2. Lowering the Entropic Barrier for Binding Conformationally Flexible Inhibitors to Enzymes,

3. Ligand Preorganization May Be Accompanied by Entropic Penalties in Protein–Ligand Interactions

4. Thermodynamic and Structural Effects of Conformational Constraints in Protein−Ligand Interactions. Entropic Paradoxy Associated with Ligand Preorganization

5. Calorimetric and Structural Studies of 1,2,3-Trisubstituted Cyclopropanes as Conformationally Constrained Peptide Inhibitors of Src SH2 Domain Binding

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