8 results match your criteria Current Chemical Biology[Journal]

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Using Copper to Improve the Well-Being of the Skin.

Authors:
Gadi Borkow

Curr Chem Biol 2014 Aug;8(2):89-102

Cupron Inc. Hasadnaot 10, Herzelia, Israel.

Copper has two key properties that are being exploited in consumer and medical device products in the last decade. On the one hand, copper has potent biocidal properties. On the other hand, copper is involved in numerous physiological and metabolic processes critical for the appropriate functioning of almost all tissues in the human body. Read More

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http://dx.doi.org/10.2174/2212796809666150227223857DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4556990PMC
August 2014
14 Reads

Novel Citronellyl-Based Photoprobes Designed to Identify ER Proteins Interacting with Dolichyl Phosphate in Yeast and Mammalian Cells.

Curr Chem Biol 2015;9(2):123-141

Department of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, Kentucky 40536, USA; University of Kentucky College of Medicine, Markey Cancer Center, University of Kentucky, Lexington, Kentucky 40536, USA; Kentucky Center for Structural Biology, University of Kentucky, Lexington, Kentucky 40536, USA; Department of Chemistry, University of Kentucky, Lexington, Kentucky 40536, USA.

Background: Dolichyl phosphate-linked mono- and oligosaccharides (DLO) are essential intermediates in protein N-glycosylation, C- and O-mannosylation and GPI anchor biosynthesis. While many membrane proteins in the endoplasmic reticulum (ER) involved in the assembly of DLOs are known, essential proteins believed to be required for the transbilayer movement (flip-flopping) and proteins potentially involved in the regulation of DLO synthesis remain to be identified.

Methods: The synthesis of a series of Dol-P derivatives composed of citronellyl-based photoprobes with benzophenone groups equipped with alkyne moieties for Huisgen "click" chemistry is now described to utilize as tools for identifying ER proteins involved in regulating the biosynthesis and transbilayer movement of lipid intermediates enzymatic assays were used to establish that the photoprobes contain the critical structural features recognized by pertinent enzymes in the dolichol pathway. Read More

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http://dx.doi.org/10.2174/2212796810666160216221610DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4834925PMC
January 2015
14 Reads

Environmental contaminants perturb fragile protein assemblies and inhibit normal protein function.

Curr Chem Biol 2013 ;7(2):196-206

Developmental Therapeutics, Fox Chase Cancer Center 333 Cottman Avenue, Philadelphia, PA, 19111 (USA).

The molecular mechanisms whereby small molecules that contaminate our environment cause physiological effects are largely unknown, in terms of both targets and mechanisms. The essential human enzyme porphobilinogen synthase (PBGS, a.k. Read More

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http://dx.doi.org/10.2174/2212796811307020011DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4102012PMC
January 2013
15 Reads

RNA Granules Living a Post-transcriptional Life: the Trypanosomes' Case.

Curr Chem Biol 2011 May;5(2):108-117

Instituto de Investigaciones Biotecnológicas-Instituto Tecnológico Chascomús, UNSAM-CONICET, 1650 San Martín, Provincia de Buenos Aires, Argentina.

Trypanosomes are protozoan parasites responsible for recalcitrant infectious diseases such as Sleeping sickness and Chagas disease in Africa and America, respectively. Their complex life-cycles are accompanied by alternation of forms specific of the insect vectors and vertebrate hosts, each with different metabolic and structural requirements. Unlike most other eukaryotes, these single-cell microorganisms seem to control the expression of protein-coding genes mostly by mRNA degradation, silencing and translation efficiency. Read More

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3179377PMC
May 2011
25 Reads

Diving Into the Lipid Bilayer to Investigate the Transmembrane Organization and Conformational State Transitions of P-type Ion ATPases.

Curr Chem Biol 2011 May;5(2):118-129

Instituto de Química y Fisicoquímica Biológicas, Facultad de Farmacia y Bioquímica, Universidad de Buenos Aires, CONICET, Junín 956 (1113) Buenos Aires, Argentina.

Although membrane proteins constitute more than 20% of the total proteins, the structures of only a few are known in detail. An important group of integral membrane proteins are ion-transporting ATPases of the P-type family, which share the formation of an acid-stable phosphorylated intermediate as part of their reaction cycle. There are several crystal structures of the sarcoplasmic reticulum Ca(2+) pump (SERCA) revealing different conformations, and recently, crystal structures of the H(+)-ATPase and the Na(+)/K(+)-ATPase were reported as well. Read More

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http://dx.doi.org/10.2174/187231311795243319DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3117579PMC
May 2011
14 Reads

Chemical Tumor Biology of Heparan Sulfate Proteoglycans.

Curr Chem Biol 2010 Jan;4(1):20-31

Department of Bioengineering, University of Utah, Salt Lake City, UT 84112, USA.

Heparan sulfate proteoglycans (HSPGs) play vital roles in every step of tumor progression allowing cancer cells to proliferate, escape from immune response, invade neighboring tissues, and metastasize to distal sites away from the primary site. Several cancers including breast, lung, brain, pancreatic, skin, and colorectal cancers show aberrant modulation of several key HS biosynthetic enzymes such as 3-O Sulfotransferase and 6-O Sulfotransferase, and also catabolic enzymes such as HSulf-1, HSulf-2 and heparanase. The resulting tumor specific HS fine structures assist cancer cells to breakdown ECM to spread, misregulate signaling pathways to facilitate their proliferation, promote angiogenesis to receive nutrients, and protect themselves against natural killer cells. Read More

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http://dx.doi.org/10.2174/187231310790226206DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2892923PMC
January 2010
11 Reads

Chemical and Biochemical Basis of Cell-Bone Matrix Interaction in Health and Disease.

Authors:
Xu Feng

Curr Chem Biol 2009 May;3(2):189-196

Department of Pathology, University of Alabama at Birmingham, Birmingham, AL 35294, USA.

Bone, a calcified tissue composed of 60% inorganic component (hydroxyapatite), 10% water and 30% organic component (proteins), has three functions: providing mechanical support for locomotion, protecting vital organs, and regulating mineral homeostasis. A lifelong execution of these functions depends on a healthy skeleton, which is maintained by constant bone remodeling in which old bone is removed by the bone-resorbing cell, osteoclasts, and then replaced by new bone formed by the bone-forming cell, osteoblasts. This remodeling process requires a physical interaction of bone with these bone cells. Read More

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http://dx.doi.org/10.2174/187231309788166398DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2790195PMC
May 2009
16 Reads

S100A1: Structure, Function, and Therapeutic Potential.

Curr Chem Biol 2009 May;3(2):138-145

Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, 108 N. Greene St., Baltimore, Maryland, 21201.

S100A1 is a member of the S100 family of calcium-binding proteins. As with most S100 proteins, S100A1 undergoes a large conformational change upon binding calcium as necessary to interact with numerous protein targets. Targets of S100A1 include proteins involved in calcium signaling (ryanidine receptors 1 & 2, Serca2a, phopholamban), neurotransmitter release (synapsins I & II), cytoskeletal and filament associated proteins (CapZ, microtubules, intermediate filaments, tau, mocrofilaments, desmin, tubulin, F-actin, titin, and the glial fibrillary acidic protein GFAP), transcription factors and their regulators (e. Read More

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http://dx.doi.org/10.2174/187231309788166460DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2771873PMC
May 2009
12 Reads
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