ChemInform Abstract: PHARMACOLOGICAL EFFECTS OF INTRODUCING A DOUBLE BOND INTO A BINDING SITE OF OXYTOCIN. ANALOGS WITH L-3,4-DEHYDROPROLINE IN POSITION 7

1977 ◽  
Vol 8 (34) ◽  
pp. no-no
Author(s):  
S. MOORE ◽  
A. M. FELIX ◽  
J. MEIENHOFER ◽  
C. W. SMITH ◽  
R. WALTER
Keyword(s):  
Double Bond ◽  
Binding Site ◽  
Pharmacological Effects

Pharmacological effects of introducing a double bond into a binding site of oxytocin. Analogs with L-3,4-dehydroproline in position 7

1977 ◽  
Vol 20 (4) ◽  
pp. 495-500 ◽  
Author(s):  
Stanley Moore ◽  
Arthur M. Felix ◽  
Johannes Meienhofer ◽  
Clark W. Smith ◽  
Roderich Walter
Keyword(s):  
Double Bond ◽  
Binding Site ◽  
Pharmacological Effects

scholarly journals H2 Formation Holds the Key to Opening the Fe Coordination Sites of Nitrogenase FeMo-cofactor for Dinitrogen Activation

2020 ◽  
Author(s):  
Yong Li ◽  
Wan-Lu Li ◽  
Jin-Cheng Liu ◽  
Jun-Bo Lu ◽  
W. H. Eugen Schwarz ◽  
...  
Keyword(s):  
Double Bond ◽  
Binding Site ◽  
Energy Release ◽  
Triple Bond ◽  
Quantum Mechanical ◽  
Essential Step ◽  
Coordination Sites ◽  
Femo Cofactor ◽  
H2 Formation ◽  
Electron Transfers

The present quantum-mechanical and molecular-mechanics study reveals the crucial roles of H<sub>2</sub> formation, of H<sub>2</sub>S shift and of N<sub>2</sub> bond expansion in the nitrogenase process of the reduction of N<sub>2</sub> to <a href="https://en.wikipedia.org/wiki/Ammonia">NH<sub>3</sub></a>. Proton and electron transfers to the Fe(C@Fe<sub>6</sub>S<sub>9</sub>)Mo unit of the FeMo-co complex weaken the Fe-S and Fe-H bonds and expose the <b>Fe</b> coordination sites, coupled with energy release due to H<sub>2</sub> generation. Thereby the two sites <b>Fe2</b> and <b>Fe6</b> become prepared for stronger N<sub>2</sub> adsorption, expanding and attenuating the ǀN≡Nǀ bond. After subsequent detachment of H<sub>2</sub>S from its Fe binding site into a holding site of the rearranged protein residue, the <b>Fe6</b> site becomes completely unfolded, and the N<sub>2</sub> triple bond becomes completely activated to an ‑<u>N</u>=<u>N</u>- double bond for easy subsequent hydrogenation to NH<sub>3</sub>. We explain in particular, why the obligatory H<sub>2</sub> formation is an essential step in N<sub>2</sub> adsorption and activation

scholarly journals H2 Formation Holds the Key to Opening the Fe Coordination Sites of Nitrogenase FeMo-cofactor for Dinitrogen Activation

2020 ◽  
Author(s):  
Yong Li ◽  
Wan-Lu Li ◽  
Jin-Cheng Liu ◽  
Jun-Bo Lu ◽  
W. H. Eugen Schwarz ◽  
...  
Keyword(s):  
Double Bond ◽  
Binding Site ◽  
Energy Release ◽  
Triple Bond ◽  
Quantum Mechanical ◽  
Essential Step ◽  
Coordination Sites ◽  
Femo Cofactor ◽  
H2 Formation ◽  
Electron Transfers

The present quantum-mechanical and molecular-mechanics study reveals the crucial roles of H<sub>2</sub> formation, of H<sub>2</sub>S shift and of N<sub>2</sub> bond expansion in the nitrogenase process of the reduction of N<sub>2</sub> to <a href="https://en.wikipedia.org/wiki/Ammonia">NH<sub>3</sub></a>. Proton and electron transfers to the Fe(C@Fe<sub>6</sub>S<sub>9</sub>)Mo unit of the FeMo-co complex weaken the Fe-S and Fe-H bonds and expose the <b>Fe</b> coordination sites, coupled with energy release due to H<sub>2</sub> generation. Thereby the two sites <b>Fe2</b> and <b>Fe6</b> become prepared for stronger N<sub>2</sub> adsorption, expanding and attenuating the ǀN≡Nǀ bond. After subsequent detachment of H<sub>2</sub>S from its Fe binding site into a holding site of the rearranged protein residue, the <b>Fe6</b> site becomes completely unfolded, and the N<sub>2</sub> triple bond becomes completely activated to an ‑<u>N</u>=<u>N</u>- double bond for easy subsequent hydrogenation to NH<sub>3</sub>. We explain in particular, why the obligatory H<sub>2</sub> formation is an essential step in N<sub>2</sub> adsorption and activation

Ultrastructure of neuromuscular relationships in the canine heartworm (dirofilaria immitis)

1986 ◽  
Vol 44 ◽  
pp. 278-279
Author(s):  
W. L. Steffens ◽  
Nancy B. Roberts ◽  
J. M. Bowen
Keyword(s):  
Dirofilaria Immitis ◽  
Domestic Dogs ◽  
Structural Description ◽  
Pharmacological Effects ◽  
Free Living ◽  
Canine Heartworm ◽  
The World ◽  
Synaptic Region ◽  
Muscle Innervation ◽  
Insight Into

The canine heartworm is a common and serious nematode parasite of domestic dogs in many parts of the world. Although nematode neuroanatomy is fairly well documented, the emphasis has been on sensory anatomy and primarily in free-living soil species and ascarids. Lee and Miller reported on the muscular anatomy in the heartworm, but provided little insight into the peripheral nervous system or myoneural relationships. The classical fine-structural description of nematode muscle innervation is Rosenbluth's earlier work in Ascaris. Since the pharmacological effects of some nematacides currently being developed are neuromuscular in nature, a better understanding of heartworm myoneural anatomy, particularly in reference to the synaptic region is warranted.

Salvia phytomedicines: from the „salvãre„ properties to demonstration of some pharmacological effects

Planta Medica ◽  
2008 ◽  
Vol 74 (09) ◽  
Author(s):  
CF Lima ◽  
AA Ramos ◽  
C Pereira-Wilson ◽  
MJ Sousa ◽  
PS Braga ◽  
...  
Keyword(s):  
Pharmacological Effects

Antithrombin-mediated Inhibition of Factor Vlla-Tissue Factor Complex by the Synthetic Pentasaccharide Representing the Heparin Binding Site to Antithrombin

1996 ◽  
Vol 76 (01) ◽  
pp. 005-008 ◽  
Author(s):  
Jean Claude Lormeau ◽  
Jean Pascal Herault ◽  
Jean Marc Herbert
Keyword(s):  
Binding Site ◽  
Tissue Factor ◽  
Residual Activity ◽  
Coagulation Factors ◽  
Heparin Binding ◽  
Experimental Conditions ◽  
First Order ◽  
Heparin Binding Site ◽  
Coagulant Activity

SummaryWe examined the effect of the synthetic pentasaccharide representing the minimal binding site of heparin to antithrombin on the antithrombin-mediated inactivation of factor Vila bound to tissue factor. This effect was compared to the effect of unfractionated heparin. Using purified recombinant human coagulation factors and either a clotting or an amidolytic assay for the determination of the residual activity of factor Vila, we showed that the pentasaccharide was an efficient antithrombin-dependent inhibitor of the coagulant activity of tissue factor-factor Vila complex. In our experimental conditions, assuming a mean MW of 14,000 for heparin, the molar pseudo-first order rate constants for ATIII-mediated FVIIa inhibition by ATIII-binding heparin and by the synthetic pentasaccharide were found to be similar with respective values of 104,000 ± 10,500 min-1 and 112,000 ± 12,000 min-1 (mean ± s.e.m., n = 3)

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