Structure–Activity Relationships and Identification of Optmized CC-Chemokine Receptor CCR1, 5, and 8 Metal-Ion Chelators

2013 ◽  
Vol 53 (11) ◽  
pp. 2863-2873 ◽  
Author(s):  
Alexander Chalikiopoulos ◽  
Stefanie Thiele ◽  
Mikkel Malmgaard-Clausen ◽  
Patrik Rydberg ◽  
Vignir Isberg ◽  
...  
Keyword(s):  
Chemokine Receptor ◽  
Metal Ion ◽  
Cc Chemokine ◽  
Structure Activity Relationships ◽  
Structure Activity ◽  
Metal Ion Chelators

scholarly journals Lead identification and structure–activity relationships of heteroarylpyrazole arylsulfonamides as allosteric CC-chemokine receptor 4 (CCR4) antagonists

2014 ◽  
Vol 12 (11) ◽  
pp. 1779 ◽  
Author(s):  
Afjal H. Miah ◽  
Royston C. B. Copley ◽  
Daniel O'Flynn ◽  
Jonathan M. Percy ◽  
Panayiotis A. Procopiou
Keyword(s):  
Chemokine Receptor ◽  
Cc Chemokine ◽  
Structure Activity Relationships ◽  
Structure Activity ◽  
Lead Identification ◽  
Chemokine Receptor 4

Synthesis and Structure–Activity Relationships of Indazole Arylsulfonamides as Allosteric CC-Chemokine Receptor 4 (CCR4) Antagonists

2013 ◽  
Vol 56 (5) ◽  
pp. 1946-1960 ◽  
Author(s):  
Panayiotis A. Procopiou ◽  
John W. Barrett ◽  
Nicholas P. Barton ◽  
Malcolm Begg ◽  
David Clapham ◽  
...  
Keyword(s):  
Chemokine Receptor ◽  
Cc Chemokine ◽  
Structure Activity Relationships ◽  
Structure Activity ◽  
Chemokine Receptor 4

Structure–Activity Relationships and Biological Characterization of a Novel, Potent, and Serum Stable C-X-C Chemokine Receptor Type 4 (CXCR4) Antagonist

2017 ◽  
Vol 60 (23) ◽  
pp. 9641-9652 ◽  
Author(s):  
Salvatore Di Maro ◽  
Francesco Saverio Di Leva ◽  
Anna Maria Trotta ◽  
Diego Brancaccio ◽  
Luigi Portella ◽  
...  
Keyword(s):  
Chemokine Receptor ◽  
Receptor Type ◽  
Biological Characterization ◽  
Cxcr4 Antagonist ◽  
Structure Activity Relationships ◽  
Structure Activity

Synthesis and Structure−Activity Relationships of Azamacrocyclic C-X-C Chemokine Receptor 4 Antagonists: Analogues Containing a Single Azamacrocyclic Ring are Potent Inhibitors of T-Cell Tropic (X4) HIV-1 Replication

2010 ◽  
Vol 53 (3) ◽  
pp. 1250-1260 ◽  
Author(s):  
Gary J. Bridger ◽  
Renato T. Skerlj ◽  
Pedro E. Hernandez-Abad ◽  
David E. Bogucki ◽  
Zhongren Wang ◽  
...  
Keyword(s):  
T Cell ◽  
Chemokine Receptor ◽  
Structure Activity Relationships ◽  
Structure Activity ◽  
Chemokine Receptor 4 ◽  
Hiv 1

Synthesis and Structure−Activity Relationships of Phenylenebis(methylene)- Linked Bis-azamacrocycles That Inhibit HIV-1 and HIV-2 Replication by Antagonism of the Chemokine Receptor CXCR4

1999 ◽  
Vol 42 (19) ◽  
pp. 3971-3981 ◽  
Author(s):  
Gary J. Bridger ◽  
Renato T. Skerlj ◽  
Sreenivasan Padmanabhan ◽  
Stephen A. Martellucci ◽  
Geoffrey W. Henson ◽  
...  
Keyword(s):  
Chemokine Receptor ◽  
Structure Activity Relationships ◽  
Chemokine Receptor Cxcr4 ◽  
Structure Activity ◽  
Hiv 1

Discovery and Structure−Activity Relationship of N-(Ureidoalkyl)-Benzyl-Piperidines As Potent Small Molecule CC Chemokine Receptor-3 (CCR3) Antagonists

2002 ◽  
Vol 45 (17) ◽  
pp. 3794-3804 ◽  
Author(s):  
George V. De Lucca ◽  
Ui T. Kim ◽  
Curt Johnson ◽  
Brian J. Vargo ◽  
Patricia K. Welch ◽  
...  
Keyword(s):  
Small Molecule ◽  
Chemokine Receptor ◽  
Structure Activity Relationship ◽  
Activity Relationship ◽  
Cc Chemokine ◽  
Structure Activity ◽  
Relationship Of

Bacterial glyoxalase I enzymes: structural and biochemical investigations

2014 ◽  
Vol 42 (2) ◽  
pp. 479-484 ◽  
Author(s):  
John F. Honek
Keyword(s):  
Metal Ion ◽  
Molecular Structures ◽  
Glyoxalase I ◽  
Structure Activity Relationships ◽  
Structure Activity

A number of bacterial glyoxalase I enzymes are maximally activated by Ni2+ and Co2+ ions, but are inactive in the presence of Zn2+, yet these enzymes will also bind this metal ion. The structure–activity relationships between these two classes of glyoxalase I serve as important clues as to how the molecular structures of these proteins control metal-activation profiles.

Structure−Activity Relationships of Cyclic Peptide-Based Chemokine Receptor CXCR4 Antagonists:  Disclosing the Importance of Side-Chain and Backbone Functionalities

2007 ◽  
Vol 50 (2) ◽  
pp. 192-198 ◽  
Author(s):  
Satoshi Ueda ◽  
Shinya Oishi ◽  
Zi-xuan Wang ◽  
Takanobu Araki ◽  
Hirokazu Tamamura ◽  
...  
Keyword(s):  
Chemokine Receptor ◽  
Cyclic Peptide ◽  
Side Chain ◽  
Structure Activity Relationships ◽  
Chemokine Receptor Cxcr4 ◽  
Structure Activity ◽  
Cxcr4 Antagonists

scholarly journals The Ribosome-Binding Mode of Trichothecene Mycotoxins Rationalizes Their Structure—Activity Relationships

2021 ◽  
Vol 22 (4) ◽  
pp. 1604
Author(s):  
Weijun Wang ◽  
Yan Zhu ◽  
Nadine Abraham ◽  
Xiu-Zhen Li ◽  
Matthew Kimber ◽  
...  
Keyword(s):  
Metal Ion ◽  
Large Family ◽  
Binding Pocket ◽  
Binding Mode ◽  
Epoxide Ring ◽  
Head Blight ◽  
Structure Activity Relationships ◽  
Existing Structures ◽  
Structure Activity ◽  
Food And Feed

Trichothecenes are the most prevalent mycotoxins contaminating cereal grains. Some of them are also considered as the virulence factors of Fusarium head blight disease. However, the mechanism behind the structure-activity relationship for trichothecenes remains unexplained. Filling this information gap is a crucial step for developing strategies to manage this large family of mycotoxins in food and feed. Here, we perform an in-depth re-examination of the existing structures of Saccharomyces cerevisiae ribosome complexed with three different trichothecenes. Multiple binding interactions between trichothecenes and 25S rRNA, including hydrogen bonds, nonpolar pi stacking interactions and metal ion coordination interactions, are identified as important binding determinants. These interactions are mainly contributed by the key structural elements to the toxicity of trichothecenes, including the oxygen in the 12,13-epoxide ring and a double bond between C9 and C10. In addition, the C3-OH group also participates in binding. The comparison of three trichothecenes binding to the ribosome, along with their binding pocket architecture, suggests that the substitutions at different positions impact trichothecenes binding in two different patterns. Moreover, the binding of trichothecenes induced conformation changes of several nucleotide bases in 25S rRNA. This then provides a structural framework for understanding the structure-activity relationships apparent in trichothecenes. This study will facilitate the development of strategies aimed at detoxifying mycotoxins in food and feed and at improving the resistance of cereal crops to Fusarium fungal diseases.

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