Effect of the Nature of the Counterion on the Properties of Anionic Surfactants. 3. Self-Association Behavior of Tetrabutylammonium Dodecyl Sulfate and Tetradecyl Sulfate:  Clouding and Micellar Growth

2004 ◽  
Vol 108 (47) ◽  
pp. 18195-18203 ◽  
Author(s):  
Raoul Zana ◽  
Mohamed Benrraou ◽  
Barney L. Bales
Keyword(s):  
Anionic Surfactants ◽  
Micellar Growth ◽  
Dodecyl Sulfate ◽  
Association Behavior ◽  
Self Association

Ultramicroelectrode Voltammetric Investigation of Intermicellar Interaction and Micellar Growth of Sodium Dodecyl Sulfate in Aqueous NaCl Solutions

2004 ◽  
Vol 108 (22) ◽  
pp. 7523-7527 ◽  
Author(s):  
Zhenyu Yang ◽  
Yao Lu ◽  
Jinsheng Zhao ◽  
Qingtao Gong ◽  
Xiuli Yin ◽  
...  
Keyword(s):  
Sodium Dodecyl Sulfate ◽  
Sodium Dodecyl ◽  
Micellar Growth ◽  
Dodecyl Sulfate

Spectroscopic and self-association behavior of a porphyrin-β-cyclodextrin conjugate

2007 ◽  
Vol 31 (8) ◽  
pp. 1499 ◽  
Author(s):  
Antonino Puglisi ◽  
Roberto Purrello ◽  
Enrico Rizzarelli ◽  
Salvatore Sortino ◽  
Graziella Vecchio
Keyword(s):  
Association Behavior ◽  
Self Association

scholarly journals Structure and inhibitor binding characterization of oncogenic MLLT1 mutants

2021 ◽  
Author(s):  
Xiaomin Ni ◽  
Allyn T. Londregan ◽  
Dafydd R. Owen ◽  
Stefan Knapp ◽  
Apirat Chaikuad
Keyword(s):  
Conformational Changes ◽  
Structural Basis ◽  
Wild Type ◽  
Structural Comparison ◽  
Inhibitor Binding ◽  
Binding Interface ◽  
Association Behavior ◽  
Self Association ◽  
Potential Strategy

AbstractDysfunction of YEATS-domain-containing MLLT1, an acetyl/acyl-lysine dependent epigenetic reader domain, has been implicated in the development of aggressive cancers. Mutations in the YEATS domain have been recently reported as a cause of MLLT1 aberrant reader function. However, structural basis for the reported alterations in affinity for acetyled/acylated histone has remained elusive. Here, we report the crystal structures of both insertion and substitution present in cancer, revealing significant conformational changes of the YEATS-domain loop 8. Structural comparison demonstrates that such alteration not only altered the binding interface for acetylated/acylated histones, but the sequence alterations in the T1 loop may enable dimeric assembly consistent inducing self-association behavior. Nevertheless, we show that also the MLLT1 mutants can be targeted by developed acetyllysine mimetic inhibitors with affinities similarly to wild type. Our report provides a structural basis for the altered behaviors and potential strategy for targeting oncogenic MLLT1 mutants.

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