Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Enzyme Inhibition

Enzyme Inhibition

Inhibitors are molecules that reduce enzyme activity by binding to the enzyme. In a normally functioning cell, enzymes are regulated by a variety of inhibitors. Drugs and other toxins can also inhibit enzymes. Some inhibitors bind to the enzyme’s active site, while others inhibit enzymatic activity by binding to other sites on the protein structure.

The Electron Transport Chain

The Electron Transport Chain

The electron transport chain or oxidative phosphorylation is an exothermic process in which free energy released during electron transfer reactions is coupled to ATP synthesis. This process is a significant source of energy in aerobic cells, and therefore inhibitors of the electron transport chain can be detrimental to the cell's metabolic processes.
Inhibitors of the electron transport chain
Rotenone, a widely used pesticide, prevents electron transfer from Fe-S cluster to ubiquinone or Q in...

Antimicrobial Proteins

Antimicrobial Proteins

Antimicrobial proteins are important components of the immune system. They aid the body in combating pathogens by either killing them directly or hindering their replication processes. Four main types of antimicrobial substances are interferons, the complement system, iron-binding proteins, and antimicrobial proteins.
Interferons
Interferons (IFNs) are proteins produced by lymphocytes, macrophages, and fibroblasts infected with viruses. While IFNs cannot prevent viruses from entering and...

Inhibitors of Viral Protein Synthesis

Inhibitors of Viral Protein Synthesis

Protein synthesis is indispensable for viral replication, as viruses lack the cellular machinery required for this process and must hijack the host's translational apparatus. In response, host cells deploy a critical innate immune defense involving interferons, specialized cytokines that play a central role in inhibiting viral propagation.Upon viral detection, infected cells release interferons that bind to receptors on adjacent uninfected cells, activating the JAK-STAT signaling pathway and...

Inhibitors Of Virion Release

Inhibitors Of Virion Release

Viral replication and dissemination rely on efficient mechanisms for host cell entry, genome replication, assembly, and release. Influenza viruses, such as types A and B, are negative-sense single-stranded RNA viruses with a segmented genome, that depend on two critical surface glycoproteins to carry out these processes: hemagglutinin (HA) and neuraminidase (NA). HA initiates infection by binding to sialic acid residues on the surface of host epithelial cells, facilitating receptor-mediated...

Inhibitors of Virion Maturation and Assembly

Inhibitors of Virion Maturation and Assembly

As part of their replication cycle, certain viruses synthesize long precursor proteins called polyproteins within infected host cells. In human immunodeficiency virus (HIV), two major polyproteins are produced: Gag and Gag-Pol. The Gag polyprotein supplies the structural components of the virus, while Gag-Pol includes essential viral enzymes such as reverse transcriptase, integrase, and protease. After synthesis, these polyproteins move to the host cell membrane, where they assemble into an...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Camostat Mesylate Versus Lopinavir/Ritonavir in Hospitalized Patients With COVID-19-Results From a Randomized, Controlled, Open Label, Platform Trial (ACOVACT).

Frontiers in pharmacology·2022

Same author

Comparative proteomics reveals unexpected quantitative phosphorylation differences linked to platelet activation state.

Scientific reports·2019

Same author

PCSK9 decreases during experimental endotoxemia.

Journal of internal medicine·2019

Same author

Added value of the DIC score and of D-dimer to predict outcome after successfully resuscitated out-of-hospital cardiac arrest.

European journal of internal medicine·2018

Same author

Statistical analysis of Goal Attainment Scaling endpoints in randomised trials.

Statistical methods in medical research·2018

Same author

Anti-C1s monoclonal antibody BIVV009 in late antibody-mediated kidney allograft rejection-results from a first-in-patient phase 1 trial.

American journal of transplantation : official journal of the American Society of Transplantation and the American Society of Transplant Surgeons·2017

Search research articles

Related Experiment Video

Updated: Jul 10, 2026

A High-throughput Cre-Lox Activated Viral Membrane Fusion Assay to Identify Inhibitors of HIV-1 Viral Membrane Fusion

A High-throughput Cre-Lox Activated Viral Membrane Fusion Assay to Identify Inhibitors of HIV-1 Viral Membrane Fusion

Published on: August 14, 2018

Heparin blunts endotoxin-induced coagulation activation.

T Pernerstorfer¹, U Hollenstein, J Hansen

¹Department of Clinical Pharmacology-The Adhesion Research Group Elaborating Therapeutics (TARGET), University of Tromsø, Norway. thomas.pernerstorfer@univie.ac.at

|December 22, 1999

Summary

Unfractionated heparin (UFH) and low-molecular-weight heparin (LMWH) effectively reduced coagulation activation triggered by lipopolysaccharide (LPS) in a human endotoxemia model. Both anticoagulants inhibited thrombin generation and upstream/downstream coagulation factor activation.

More Related Videos

Combined Genetic and Chemical Capsid Modifications of Adenovirus-Based Gene Transfer Vectors for Shielding and Targeting

Combined Genetic and Chemical Capsid Modifications of Adenovirus-Based Gene Transfer Vectors for Shielding and Targeting

Published on: October 26, 2018

Affinity Purification of a Fibrinolytic Enzyme from Sipunculus nudus

Affinity Purification of a Fibrinolytic Enzyme from Sipunculus nudus

Published on: June 2, 2023

Related Experiment Videos

Last Updated: Jul 10, 2026

A High-throughput Cre-Lox Activated Viral Membrane Fusion Assay to Identify Inhibitors of HIV-1 Viral Membrane Fusion

A High-throughput Cre-Lox Activated Viral Membrane Fusion Assay to Identify Inhibitors of HIV-1 Viral Membrane Fusion

Published on: August 14, 2018

Combined Genetic and Chemical Capsid Modifications of Adenovirus-Based Gene Transfer Vectors for Shielding and Targeting

Combined Genetic and Chemical Capsid Modifications of Adenovirus-Based Gene Transfer Vectors for Shielding and Targeting

Published on: October 26, 2018

Affinity Purification of a Fibrinolytic Enzyme from Sipunculus nudus

Affinity Purification of a Fibrinolytic Enzyme from Sipunculus nudus

Published on: June 2, 2023

Area of Science:

Coagulation science
Pharmacology
Sepsis research

Background:

Lipopolysaccharide (LPS) triggers sepsis-induced disseminated intravascular coagulation (DIC) via the tissue factor (TF)/factor VIIa pathway.
Clinical use of anticoagulants in LPS-induced coagulation remains under-explored.
This study investigates UFH and LMWH effects on LPS-induced coagulation.

Purpose of the Study:

To compare the effects of unfractionated heparin (UFH) and low-molecular-weight heparin (LMWH) against placebo.
To evaluate anticoagulation potency in an experimental LPS-induced coagulation model.
To assess inhibition of thrombin generation and coagulation factor activation.

Main Methods:

Randomized, double-blind, placebo-controlled trial in 30 healthy male volunteers.
Administration of LPS (2 ng/kg IV) followed by UFH, LMWH, or placebo infusion.
Measurement of prothrombin fragment F(1+2), thrombus precursor protein (TpP), TF-positive monocytes, activated factor VII, and TF pathway inhibitor levels.

Main Results:

Placebo group showed marked increases in F(1+2) and TpP; TF-positive monocytes doubled.
UFH and LMWH significantly reduced F(1+2) and TpP levels.
Both heparins reduced TF expression on monocytes, increased TF pathway inhibitor, and decreased factor VIIa levels.

Conclusions:

UFH and LMWH demonstrate anticoagulatory potency in early experimental LPS-induced coagulation.
Successful inhibition of thrombin generation was observed.
Heparins blunt activation of coagulation factors upstream and downstream of thrombin.