Fluorescein-5-EX, Succinimidyl Ester - Citations

Fluorescein-5-EX, Succinimidyl Ester - Citations

View additional product information for Fluorescein-5-EX, Succinimidyl Ester - Citations (F6130)

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Citations & References
Abstract
Fluorescent labeling of cell-free synthesized proteins by incorporation of fluorophore-conjugated nonnatural amino acids.
AuthorsKang SH, Jun SY, Kim DM
JournalAnal Biochem
PubMed ID17113028
'Although fluorescent dyes, such as fluorescein derivatives, have bulky and complex structures, nonnatural amino acids carrying these fluorescein derivatives are acceptable by the Escherichia coli ribosome and are useful for the cotranslational fluorescent labeling of cell-free synthesized proteins. Surprisingly, the incorporation efficiency of nonnatural amino acids carrying fluorescein derivatives into ... More
Synthesis and characterization of fluorescent cobalamin (CobalaFluor) derivatives for imaging.
AuthorsSmeltzer CC, Cannon MJ, Pinson PR, Munger JD, West FG, Grissom CB
JournalOrg Lett
PubMed ID11263885
Fluorescent derivatives of cobalamin have been prepared by linking fluorophores to cobalamin through a propylamide spacer. Fluorescein, naphthofluorescein, and Oregon Green derivatives have been prepared in good yield by reaction of the fluorophore NHS-ester with beta-(3-aminopropyl)cobalamin to form fluorescent cobalamin conjugates (CobalaFluors) that are potentially suitable for the in vitro ... More
Noninvasive imaging of cell death using an Hsp90 ligand.
AuthorsPark D, Don AS, Massamiri T, Karwa A, Warner B, MacDonald J, Hemenway C, Naik A, Kuan KT, Dilda PJ, Wong JW, Camphausen K, Chinen L, Dyszlewski M, Hogg PJ,
JournalJ Am Chem Soc
PubMed ID21322555
Cell death plays a central role in normal physiology and in disease. Common to apoptotic and necrotic cell death is the eventual loss of plasma membrane integrity. We have produced a small organoarsenical compound, 4-(N-(S-glutathionylacetyl)amino)phenylarsonous acid, that rapidly accumulates in the cytosol of dying cells coincident with loss of plasma ... More
Synthetic compound libraries displayed on the surface of encoded bacteriophage.
AuthorsWoiwode TF, Haggerty JE, Katz R, Gallop MA, Barrett RW, Dower WJ, Cwirla SE,
JournalChem Biol
PubMed ID14522055
We describe a technology for attaching libraries of synthetic compounds to coat proteins of bacteriophage particles such that the identity of the chemical structure is encoded in the genome of the phage, analogous to peptides displayed on phage surfaces by conventional phage-display techniques. This format allows a library of synthetic ... More
Dendritic cells express multiple chemokine receptors used as coreceptors for HIV entry.
AuthorsRubbert A, Combadiere C, Ostrowski M, Arthos J, Dybul M, Machado E, Cohn MA, Hoxie JA, Murphy PM, Fauci AS, Weissman D
JournalJ Immunol
PubMed ID9558100
Cells of the dendritic lineage are thought to be among the first cells infected after mucosal exposure to HIV. In this study, we have identified the presence of multiple chemokine receptors on dendritic cells (DC) that may function as coreceptors for HIV entry. DC effectively used CCR5 for entry of ... More
Diffusion and convection in collagen gels: implications for transport in the tumor interstitium.
AuthorsRamanujan S, Pluen A, McKee TD, Brown EB, Boucher Y, Jain RK
JournalBiophys J
PubMed ID12202388
Diffusion coefficients of tracer molecules in collagen type I gels prepared from 0-4.5% w/v solutions were measured by fluorescence recovery after photobleaching. When adjusted to account for in vivo tortuosity, diffusion coefficients in gels matched previous measurements in four human tumor xenografts with equivalent collagen concentrations. In contrast, hyaluronan solutions ... More
Kinetic mechanism of the inhibition of cathepsin G by alpha 1-antichymotrypsin and alpha 1-proteinase inhibitor.
AuthorsDuranton J, Adam C, Bieth JG
JournalBiochemistry
PubMed ID9698370
Uncontrolled proteolysis due to cathepsin G (cat G) may cause severe pathological disorders. Cat G is inhibited by alpha 1-antichymotrypsin (ACT) and alpha 1-proteinase inhibitor (alpha 1PI), two members of the serpin superfamily of proteins. To see whether these two inhibitors play a physiological proteolysis-preventing function, we have made a ... More