10 results match your criteria Current Enzyme Inhibition[Journal]

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Targeting HIV-1 Envelope Proteins Using a Fragment Discovery All-Atom Computational Algorithm.

Authors:
Michael H Peters

Curr Enzym Inhib 2017 Apr;13(1):20-26

Department of Chemical and Life Science Engineering, VCU Massey Cancer Center, and the Center for the Study of Biological Complexity, Virginia Commonwealth University, Richmond, VA, USA.

Introduction: HIV viral envelope proteins are targets for small inhibitor molecules aimed at disrupting the cellular entry process. Potential peptide-class inhibitor molecules (rDNA drugs) have been previously identified, with mixed results, through biomimicry and phage display experimental methods. Here we describe a new approach based on computational fragment discovery. Read More

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http://dx.doi.org/10.2174/1573408012666160725095854DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5411995PMC
April 2017
20 Reads

Characterization of a New Allelic Variant of Triosephosphate Isomerase from the LNCaP Human Prostate Cancer Cell Line: Enzyme Inhibition and Spectroscopic Studies.

Curr Enzym Inhib 2015 Aug;13(3):184-190

Departamento de Ingeniería Celular y Biocatálisis, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Apdo. Postal 510-3, 62250Cuernavaca, Morelos, México.

Background: The glycolytic pathway plays an important role in tumor cells. Triosephosphate isomerase (TIM) catalyzes the reversible isomerization of D-glyceraldehyde-3-phosphate (GAP) to dihydroxyacetone phosphate (DHAP) in the glycolysis. Proteomics of a human prostate adenocarcinoma cell line revealed the presence of the G233D TIM variant, a new allelic type whose biochemical properties have not been reported [1]. Read More

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http://dx.doi.org/10.2174/1573408012666160906110330DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5652080PMC
August 2015
15 Reads

An Additional Method for Analyzing the Reversible Inhibition of an 
Enzyme Using Acid Phosphatase as a Model.

Curr Enzym Inhib 2015 Aug;11(2):140-146

Department of Chemistry, Illinois State University Normal, IL 61790-4160, USA.

Using wheat germ acid phosphatase and sodium orthovanadate as a competitive inhibitor, a novel method for analyzing reversible inhibition was carried out. Our alternative approach involves plotting the initial velocity at which product is formed as a function of the ratio of substrate concentration to inhibitor concentration at a constant enzyme concentration and constant assay conditions. The concept of initial concentrations driving equilibrium leads to the chosen axes. Read More

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http://dx.doi.org/10.2174/1573408011666150605223952DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5411997PMC
August 2015
21 Reads

Reconstructing the Hsp90/Tau Machine.

Curr Enzym Inhib 2013 Jan;9(1):41-45

Department of Molecular Medicine, USF Health Byrd Alzheimer's Institute, Tampa, Florida 33613.

Imbalanced protein load within cells is a critical aspect for most diseases of aging. In particular, the accumulation of proteins into neurotoxic aggregates is a common thread for a host of neurodegenerative diseases. Recent work demonstrates that age-related changes to the cellular chaperone repertoire contributes to abnormal buildup of the microtubule-associated protein tau that accumulates in a group of diseases termed tauopathies, the most common being Alzheimer's disease (AD). Read More

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http://dx.doi.org/10.2174/1573408011309010006DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3689215PMC
January 2013
10 Reads

Beyond Thymidylate Synthase and Dihydrofolate Reductase: Impact of Non-coding microRNAs in Anticancer Chemoresistance.

Authors:
Jingfang Ju

Curr Enzym Inhib 2012 Sep;8(2):118-123

Translational Research Laboratory, Department of Pathology, State University of New York at Stony Brook, Stony Brook, NY 11794-8691, USA.

Chemoresistance is one of the major reasons for the failure of anticancer chemotherapy in treating advanced stage cancer. The mechanism of chemoresistance to fluoropyrimidines and antifolates has been extensively investigated in the past 40 years. It has been well established that thymidylate synthase (TYMS, TS) and dihydrofolate reductase (DHFR) are two major targets for fluoropyrimidines and antifolates, respectively. Read More

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http://dx.doi.org/10.2174/157340812800793228DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3966314PMC
September 2012
13 Reads

Clostridium difficile DNA polymerase IIIC: basis for activity of antibacterial compounds.

Curr Enzym Inhib 2011 Oct;7(3):147-153

Istituto di Genetica Molecolare, Consiglio Nazionale delle Ricerche, I-27100 Pavia, Italy.

Based on the finding that aerobic Gram-positive antibacterials that inhibit DNA polymerase IIIC (pol IIIC) were potent inhibitors of the growth of anaerobic Clostridium difficile (CD) strains, we chose to clone and express the gene for pol IIIC from this organism. The properties of the recombinant enzyme are similar to those of related pol IIICs from Gram-positive aerobes, e.g. Read More

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3404731PMC
October 2011
15 Reads

Inhibiting Glutathione Metabolism in Lung Lining Fluid as a Strategy to Augment Antioxidant Defense.

Curr Enzym Inhib 2011 Jul;7(2):71-78

The Pulmonary Center, Boston University School of Medicine, Boston, MA 02118, USA.

Glutathione is abundant in the lining fluid that bathes the gas exchange surface of the lung. On the one hand glutathione in this extracellular pool functions in antioxidant defense to protect cells and proteins in the alveolar space from oxidant injury; on the other hand, it functions as a source of cysteine to maintain cellular glutathione and protein synthesis. These seemingly opposing functions are regulated through metabolism by gamma-glutamyl transferase (GGT, EC 2. Read More

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http://dx.doi.org/10.2174/157340811796575308DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3319921PMC
July 2011
11 Reads

Inhibition Studies on Enzymes Involved in Isoprenoid Biosynthesis: Focus on Two Potential Drug Targets: DXR and IDI-2 Enzymes.

Curr Enzym Inhib 2011 Jul;7(2)

Department of Chemistry, University of Utah, 315 South 1400 East RM 2020, Salt Lake City, UT 84112, USA.

Isoprenoid compounds constitute an immensely diverse group of acyclic, monocyclic and polycyclic compounds that play important roles in all living organisms. Despite the diversity of their structures, this plethora of natural products arises from only two 5-carbon precursors, isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). This review will discuss the enzymes in the mevalonate (MVA) and methylerythritol phosphate (MEP) biosynthetic pathways leading to IPP and DMAPP with a particular focus on MEP synthase (DXR) and IPP isomerase (IDI), which are potential targets for the development of antibiotic compounds. Read More

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http://dx.doi.org/10.2174/157340811796575317DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3856697PMC
July 2011
10 Reads
3 Citations

TGF-β: Titan of Lung Fibrogenesis.

Curr Enzym Inhib 2010 Jul;6(2)

Department of Medicine, Section of Pulmonary Diseases, Critical Care and Environmental Medicine, Tulane University Health Sciences Center, New Orleans, LA 70112, USA.

Pulmonary fibrosis is characterized by epithelial cell injury, accumulation of myofibroblasts, and excessive deposition of collagen and other extracellular matrix elements, leading to loss of pulmonary function. Studies in both humans and animal models strongly suggest that TGF-β1 plays a pivotal role in the pathogenesis of pulmonary fibrosis. This review will first give an overview of TGF-β signaling and the effects of its inhibition on lung fibrogenesis. Read More

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http://dx.doi.org/10.2174/10067DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3812949PMC
July 2010
11 Reads

Diacylglycerol Kinase Inhibition and Vascular Function.

Curr Enzym Inhib 2009 ;5(3):148-152

Department of Physiology, Medical College of Georgia, Augusta, GA 30912-3000, USA.

Diacylglycerol kinases (DGKs), a family of lipid kinases, convert diacylglycerol (DG) to phosphatidic acid (PA). Acting as a second messenger, DG activates protein kinase C (PKC). PA, a signaling lipid, regulates diverse functions involved in physiological responses. Read More

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http://dx.doi.org/10.2174/157340809789071137DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3086769PMC
January 2009
15 Reads
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