Seaweed Fucoidans As Viral Inhibitors: An Overview On Its Inhibitory Mechanism

SummaryInteractions between tranexamic acid and protein were studied in respect of the antifibrinolytic actions of tranexamic acid. Tranexamic acid did neither show any interaction with fibrinogen or fibrin, nor was incorporated into cross-linked fibrin structure by the action of factor XIII. On the other hand, tranexamic acid bound to human plasmin with a dissociation constant of 3.5 × 10−5 M, which was very close to the inhibition constant (3.6 × 10−5 M) for this compound in inhibiting plasmin-induced fibrinolysis. The binding site of tranexamic acid on plasmin was not the catalytic site of plasmin, because TLCK-blocked plasmin also showed a similar affinity to tranexamic acid (the dissociation constant, 2.9–4.8 × 10−5 M).In the binding studies with the highly purified plasminogen and TLCK-plasmin preparations which were obtained by affinity chromatography on lysine-substituted Sepharose, the molar binding ratio was shown to be 1.5–1.6 moles tranexamic acid per one mole protein.On the basis of these and other findings, a model for the inhibitory mechanism of tranexamic acid is presented.

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Faculty Opinions recommendation of Neural crests are actively precluded from the anterior neural fold by a novel inhibitory mechanism dependent on Dickkopf1 secreted by the prechordal mesoderm.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1091120.544512 ◽

2007 ◽

Author(s):

Kristin Artinger

Keyword(s):

Inhibitory Mechanism ◽

Prechordal Mesoderm

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Faculty Opinions recommendation of Rapid evolution of protein kinase PKR alters sensitivity to viral inhibitors.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1146995.604105 ◽

2009 ◽

Author(s):

Moosa Mohammadi ◽

Andrew Beenken

Keyword(s):

Protein Kinase ◽

Rapid Evolution ◽

Viral Inhibitors

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Inhibitory mechanism of 5-fluoroorotate action in rat liver

Collection of Czechoslovak Chemical Communications ◽

10.1135/cccc19710271 ◽

1971 ◽

Vol 36 (1) ◽

pp. 271-280 ◽

Cited By ~ 2

Author(s):

A. Čihák ◽

H. C. Pitot

Keyword(s):

Rat Liver ◽

Inhibitory Mechanism

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An inhibitory mechanism of action of coiled‐coil peptides against type three secretion system from enteropathogenicEscherichia coli

Journal of Peptide Science ◽

10.1002/psc.3149 ◽

2019 ◽

Vol 25 (3) ◽

Cited By ~ 1

Author(s):

Mariano Larzábal ◽

Hector A. Baldoni ◽

Fernando D. Suvire ◽

Lucrecia M. Curto ◽

Gabriela E. Gomez ◽

...

Keyword(s):

Mechanism Of Action ◽

Coiled Coil ◽

Secretion System ◽

Inhibitory Mechanism ◽

Type Three Secretion System ◽

Type Three Secretion

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Inhibitory mechanism of O-methylated quercetins, highly potent β-secretase inhibitors isolated from Caragana balchaschensis (Kom.) Pojark

Journal of Ethnopharmacology ◽

10.1016/j.jep.2021.113935 ◽

2021 ◽

Vol 272 ◽

pp. 113935

Author(s):

Kamila Zhumanova ◽

Gihwan Lee ◽

Aizhamal Baiseitova ◽

Abdul Bari Shah ◽

Jeong Ho Kim ◽

...

Keyword(s):

Inhibitory Mechanism

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Micro-analysis of pure deoxyribonucleic acid-dependent ribonucleic acid polymerase from Escherichia coli. Action of heparin and rifampicin on structure and function

Biochemical Journal ◽

10.1042/bj1170623 ◽

1970 ◽

Vol 117 (3) ◽

pp. 623-631 ◽

Cited By ~ 35

Author(s):

Volker Neuhoff ◽

Wolf-Bernhard Schill ◽

Hans Sternbach

Keyword(s):

Escherichia Coli ◽

Rna Polymerase ◽

Rna Synthesis ◽

Deoxyribonucleic Acid ◽

Structure And Function ◽

Disc Electrophoresis ◽

Inhibitory Mechanism ◽

And Function ◽

Micro Analysis ◽

Template Complex

By using micro disc electrophoresis and micro-diffusion techniques, the interaction of pure DNA-dependent RNA polymerase (EC 2.7.7.6) from Escherichia coli with the template, the substrates and the inhibitors heparin and rifampicin was investigated. The following findings were obtained: (1) heparin converts the 24S and 18S particles of the polymerase into the 13S form; (2) heparin inhibits RNA synthesis by dissociating the enzyme–template complex; (3) rifampicin does not affect the attachment of heparin to the enzyme; (4) the substrates ATP and UTP are bound by enzyme loaded with rifampicin; (5) rifampicin is bound by an enzyme–template complex to the same extent as by an RNA-synthesizing enzyme–template complex. From this it is concluded that the mechanism of the inhibition of RNA synthesis by rifampicin is radically different from that by heparin. As a working hypothesis to explain the inhibitory mechanism of rifampicin, it is assumed that it becomes very firmly attached to a position close to the synthesizing site and only blocks this when no synthesis is in progress.

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