Phase separation of DUX family proteins drives totipotent-like state via 3D genome reorganization and retrotransposon activation. [PDF]
Gao L +14 more
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Self-Contained Lateral-Flow Microfluidic Bead-Based Assay for Rapid Quantification of Early-Stage Kidney Biomarkers. [PDF]
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ADORA2A activation restores lysosomal function and photoreceptor outer segment degradation in stressed retinal pigment epithelium. [PDF]
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Sensitive detection of unopposed estrogen using estrogen receptor functionalized nanoprobes for cancer diagnosis. [PDF]
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Isolation and Characterisation of Phage-Displayed scFv Antibodies Targeting PfHSP70 and PfLDH of <i>Plasmodium falciparum</i>. [PDF]
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A fluorescence-based detergent binding assay for protein hydrophobicity
Analytical Biochemistry, 1986Protein hydrophobicity is often detected by binding of protein to micelles of a mild detergent. A new fluorescence method for detection of this binding is presented. The method is based on a long-range quenching of tryptophan fluorescence by energy transfer to a pyrene-labeled phospholipid probe incorporated into micelles of Brij 96.
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Phallotoxin and actin binding assay by fluorescence enhancement
Analytical Biochemistry, 1992The fluorescence of five fluorophores conjugated to phallotoxins was found to be specifically enhanced upon binding to F-actin in a polymerizing buffer. Rhodamine phalloidin had the greatest fluorescence enhancement of ninefold. The fluorescence titration of rhodamine phalloidin by actin was shown to be consistent with stoichiometric binding.
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Development of a fluorescence polarization binding assay for asialoglycoprotein receptor
Analytical Biochemistry, 2012Asialoglycoprotein receptor (ASGP-R) has been actively investigated for targeted delivery of therapeutic agents into hepatocytes because this receptor is selectively and highly expressed in liver and has a high internalization rate. Synthetic cluster glycopeptides (e.g., triGalNAc) bind with high affinity to ASGP-R and, when conjugated to a therapeutic
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Fluorescent assay for riboflavin binding to cytochrome P450 2B4
Journal of Inorganic Biochemistry, 2004The interactions between the hemoprotein cytochrome P450 2B4 (CYP 2B4) and riboflavin - a low molecular weight component of the flavoprotein NADPH-dependent cytochrome P450 reductase - were investigated by fluorescence spectroscopy. Riboflavin fluorescence quenching by cytochrome P450 2B4 was used to probe the ligand-enzyme binding (lambda(ex)=385 nm ...
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A Fluorescence Polarization Based Src-SH2 Binding Assay
Analytical Biochemistry, 1997The tyrosine kinase pp60c.src has been implicated as being a potential therapeutic target in several human diseases including cancer and osteoporosis. An important region within this kinase is the SH2 domain (Src homology 2) which binds to phosphorylated tyrosine residues contained within specific peptide sequences.
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