scholarly journals Thermal Decay of Rhodopsin: Role of Hydrogen Bonds in Thermal Isomerization of 11-cisRetinal in the Binding Site and Hydrolysis of Protonated Schiff Base

2009 ◽  
Vol 131 (25) ◽  
pp. 8750-8751 ◽  
Author(s):  
Jian Liu ◽  
Monica Yun Liu ◽  
Jennifer B. Nguyen ◽  
Aditi Bhagat ◽  
Victoria Mooney ◽  
...  
Keyword(s):  
Schiff Base ◽  
Hydrogen Bonds ◽  
Binding Site ◽  
Thermal Isomerization ◽  
Thermal Decay ◽  
Hydrolysis Of

scholarly journals Chemical Kinetic Analysis of Thermal Decay of Rhodopsin Reveals Unusual Energetics of Thermal Isomerization and Hydrolysis of Schiff Base

2011 ◽  
Vol 286 (44) ◽  
pp. 38408-38416 ◽  
Author(s):  
Jian Liu ◽  
Monica Yun Liu ◽  
Li Fu ◽  
Gefei Alex Zhu ◽  
Elsa C. Y. Yan
Keyword(s):  
Schiff Base ◽  
Kinetic Analysis ◽  
Chemical Kinetic ◽  
Thermal Isomerization ◽  
Thermal Decay ◽  
Hydrolysis Of

Studies of the role of water on some imine–acid complexes by means of Raman spectroscopy

1992 ◽  
Vol 70 (11) ◽  
pp. 2751-2757
Author(s):  
P. Turcotte ◽  
S. Alex ◽  
D. Vocelle
Keyword(s):  
Raman Spectroscopy ◽  
Schiff Base ◽  
Strong Acid ◽  
Time Span ◽  
Dichloroacetic Acid ◽  
Water Molecules ◽  
Tert Butylamine ◽  
Hydrolysis Of ◽  
Dioxane Mixture

The percentages of protonation were determined for a conjugated Schiff base trans, trans-2,4-heptadienylidene tert-butylamine in the presence of 3-chloropropionic acid (CPR) and dichloroacetic acid (DCA) in three solvents of different polarities. In dioxane, a solvent of low polarity, protonation is only important for the strong acid DCA (50–60%). By using solvents of higher polarities, protonation is seen to increase and is almost complete for DCA in ethanol. When water molecules are added to these systems, hydrolysis of the Schiff base, measured inside the time span of the experiments (10 min), occurs readily in dioxane, is very slow in a chloroform–dioxane mixture (9:1), and is totally absent in a mixture of ethanol–dioxane (1:9). Results indicate that water does not mediate protonation in all three sets of solvent combinations. The results are also discussed in terms of the possible role that water molecules could have in the visual and bacterial pigments.

Cell-specific regulation of IRS-1 gene expression: role of E box and C/EBP binding site in HepG2 cells and CHO cells

Diabetes ◽  
1997 ◽  
Vol 46 (3) ◽  
pp. 354-362 ◽  
Author(s):  
K. Matsuda ◽  
E. Araki ◽  
R. Yoshimura ◽  
K. Tsuruzoe ◽  
N. Furukawa ◽  
...  
Keyword(s):  
Gene Expression ◽  
Binding Site ◽  
Cho Cells ◽  
Hepg2 Cells ◽  
E Box ◽  
Specific Regulation

scholarly journals Superinduction of CYP1A1 transcription by cycloheximide. Role of the DNA binding site for the liganded Ah receptor.

1992 ◽  
Vol 267 (21) ◽  
pp. 15146-15151
Author(s):  
A Lusska ◽  
L Wu ◽  
J P Whitlock
Keyword(s):  
Dna Binding ◽  
Binding Site ◽  
Ah Receptor ◽  
Dna Binding Site

scholarly journals Steroid Sulphatase and Its Inhibitors: Past, Present and Future

Molecules ◽  
2021 ◽  
Vol 26 (10) ◽  
pp. 2852
Author(s):  
Paul A. Foster
Keyword(s):  
Good Evidence ◽  
The Past ◽  
Steroid Sulphatase ◽  
University Of Oxford ◽  
Therapeutic Value ◽  
Breast And Prostate Cancer ◽  
The University ◽  
Further Development ◽  
Hydrolysis Of

Steroid sulphatase (STS), involved in the hydrolysis of steroid sulphates, plays an important role in the formation of both active oestrogens and androgens. Since these steroids significantly impact the proliferation of both oestrogen- and androgen-dependent cancers, many research groups over the past 30 years have designed and developed STS inhibitors. One of the main contributors to this field has been Prof. Barry Potter, previously at the University of Bath and now at the University of Oxford. Upon Prof. Potter’s imminent retirement, this review takes a look back at the work on STS inhibitors and their contribution to our understanding of sulphate biology and as potential therapeutic agents in hormone-dependent disease. A number of potent STS inhibitors have now been developed, one of which, Irosustat (STX64, 667Coumate, BN83495), remains the only one to have completed phase I/II clinical trials against numerous indications (breast, prostate, endometrial). These studies have provided new insights into the origins of androgens and oestrogens in women and men. In addition to the therapeutic role of STS inhibition in breast and prostate cancer, there is now good evidence to suggest they may also provide benefits in patients with colorectal and ovarian cancer, and in treating endometriosis. To explore the potential of STS inhibitors further, a number of second- and third-generation inhibitors have been developed, together with single molecules that possess aromatase–STS inhibitory properties. The further development of potent STS inhibitors will allow their potential therapeutic value to be explored in a variety of hormone-dependent cancers and possibly other non-oncological conditions.

scholarly journals Excision and transposition of Tn5 as an SOS activity in Escherichia coli.

Genetics ◽  
1991 ◽  
Vol 128 (1) ◽  
pp. 45-57 ◽  
Author(s):  
C T Kuan ◽  
S K Liu ◽  
I Tessman
Keyword(s):  
Escherichia Coli ◽  
Binding Site ◽  
Reca Protein ◽  
Precursor Molecule ◽  
Functional Integrity ◽  
Lexa Protein ◽  
Lexa Binding ◽  
Additional Role ◽  
Stimulation Of

Abstract Excision and transposition of the Tn5 element in Escherichia coli ordinarily appear to occur by recA-independent mechanisms. However, recA(Prtc) genes, which encode RecA proteins that are constitutively activated to the protease state, greatly enhanced excision and transposition; both events appeared to occur concomitantly and without destruction of the donor DNA. The recombinase function of the RecA protein was not required. Transposition was accompanied by partial, and occasionally full, restoration of the functional integrity of the gene vacated by the excised Tn5. The stimulation of transposition was inhibited by an uncleavable LexA protein and was strongly enhanced by an additional role of the RecA(Prtc) protein besides its mediation of LexA cleavage. To account for the enhanced transposition, we suggest that (i) there may be a LexA binding site within the promoter for the IS50 transposase, (ii) activated RecA may cleave the IS50 transposition inhibitor, and (iii) the transposase may be formed by RecA cleavage of a precursor molecule.

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