Design, synthesis and X-ray crystallographic studies of novel FKBP-12 ligands-Reference-Cited by-同舟云学术

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Design, synthesis and X-ray crystallographic studies of novel FKBP-12 ligands

Published:1995-08 Issue:15 Volume:5 Page:1719-1724
ISSN:0960-894X
Container-title:Bioorganic & Medicinal Chemistry Letters
language:en
Short-container-title:Bioorganic & Medicinal Chemistry Letters

Author:

Babine Robert E.,Bleckman T.M.,Kissinger C.R.,Showalter R.,Pelletier L.A.,Lewis C.,Tucker Kathleen,Moomaw Ellen,Parge H.E.,Villafranca J.Ernest

Publisher

Elsevier BV

Subject

Organic Chemistry,Clinical Biochemistry,Drug Discovery,Pharmaceutical Science,Molecular Biology,Molecular Medicine,Biochemistry

Reference30 articles.

1. Design of enzyme inhibitors using iterative protein crystallographic analysis

2. Peptidyl-Prolylcis/trans Isomerases and Their Effectors

3. A cytosolic binding protein for the immunosuppressant FK506 has peptidyl-prolyl isomerase activity but is distinct from cyclophilin

4. A receptor for the immuno-suppressant FK506 is a cis–trans peptidyl-prolyl isomerase

5. The immunophilins

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3. Targeting Protein Folding: A Novel Approach for the Treatment of Pathogenic Bacteria;Journal of Medicinal Chemistry;2020-08-13

4. FKBP Ligands—Where We Are and Where to Go?;Frontiers in Pharmacology;2018-12-05

5. De Novo Design of Ligands Using Computational Methods;Methods in Molecular Biology;2018

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