Towards multiplexed protein–protein interaction analysis using protein tag-specific nanobodies

Groll, Nicola; Emele, Felix Emele; Poetz, Oliver; Rothbauer, Ulrich

doi:10.1016/j.jprot.2015.04.017

Cited by 7 publications

(4 citation statements)

References 55 publications

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“…[ 31 ] In addition, recombinant affinity reagents such as SOMAmers, which are short single-stranded oligonucleotides based on aptamer reagents,[ 32 ] were recently used to study Alzheimer’s disease (AD) [ 33 ] and muscular dystrophies. [ 34 ] There are other novel available affinity reagents used in immunoassays including nanobodies, camelids single-domain antibodies,[ 35 , 36 ] designed ankyrin repeat proteins [ 37 ] and affibody molecules. [ 38 ]…”

Section: Potentials and Challenges Of Affinity-based Proteomicsmentioning

confidence: 99%

Immunocapture strategies in translational proteomics

Fredolini

Byström

et al. 2015

Expert Review of Proteomics

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Aiming at clinical studies of human diseases, antibody-assisted assays have been applied to biomarker discovery and toward a streamlined translation from patient profiling to assays supporting personalized treatments. In recent years, integrated strategies to couple and combine antibodies with mass spectrometry-based proteomic efforts have emerged, allowing for novel possibilities in basic and clinical research. Described in this review are some of the field’s current and emerging immunocapture approaches from an affinity proteomics perspective. Discussed are some of their advantages, pitfalls and opportunities for the next phase in clinical and translational proteomics.

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Section: Potentials and Challenges Of Affinity-based Proteomicsmentioning

confidence: 99%

Immunocapture strategies in translational proteomics

Fredolini

Byström

et al. 2015

Expert Review of Proteomics

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“…To introduce the important key proteins in the network achieve by the use of Network Analyzer. Protein-protein interactions are intrinsic to virtually every cellular process (38) and was applied for network relationship study and can make spatial proteins an attractive source of therapeutic targets (39). The integrated network (table 2).…”

Section: Resultsmentioning

confidence: 99%

Evaluation of protein clustering of pancreatic cancer

Safaei¹,

Tavirani²,

Oskouei³

et al. 2016

Arvand Journal of Health and Medical Sciences

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Pancreatic cancer (PC) is one of the most malignant tumors with a very poor prognosis. Late diagnosis and lack of effective therapeutic method is the weak point in pancreatic cancer therapy. For pancreatic cancer clustering analysis, thirty proteins were selected from Wiki pathway and sequence comparison was prepared by Needleman-Wunsch algorithm. Similarity scores were obtained by comparing of these proteins and the relevant dissimilarity matrix was constructed. Graphical illustrations of clustering data were performed by R software using package cluster to find subgraphs with maximal density. Finally the interactions of these proteins with their neighbors that was obtained from Mentha, Reactome-Fls Databases by the application of PSICQUIC source in Cytoscape software are presented. The result of this study showed that CREB-binding protein and epidermal growth factor receptor are reported in Wiki Pathway Androgen receptor and most significant hub that involved in pancreatic cancer, but not in the high close relationship. In conclusion cell cycle and signaling pathway have highlighted its importance in pancreatic cancer, as well as its potential as a therapeutic target in PC.

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“…The microsphere-based b-catenin assay for the detection of different molecular forms of b-catenin and for measuring proteinprotein interactions was performed as described previously (Groll et al, 2015a(Groll et al, , 2015b. In brief, the b-catenin bead array panel employs antibodies and known interaction partners of b-catenin to study the phosphorylation status of the protein and its complexation status within the same multiplexed assay system.…”

Section: Microsphere-based B-catenin Assaysmentioning

confidence: 99%

“…In all assay set-ups, the same antibody specific for the C-terminus of b-catenin (BD Biosciences) is used as a detector. Generation of ECT-, ICAT-, and TCF-GST fusion proteins and their utilization in microsphere-based proteinprotein interaction assays have been described in detail previously (Groll et al, 2015a).…”

Section: Microsphere-based B-catenin Assaysmentioning

confidence: 99%

Inhibition of β-catenin signaling by phenobarbital in hepatoma cells in vitro

et al. 2016

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The antiepileptic drug phenobarbital (PB) exerts hepatic effect based on indirect activation of the constitutive androstane receptor (CAR) via inhibition of the epidermal growth factor receptor (EGFR) and the kinase Src. It has furthermore been observed that in mice PB suppresses the growth of hepatocellular carcinoma with overactive signaling through the oncogenic Wnt/β-catenin pathway, thus suggesting an interference of PB with β-catenin signaling. The present work was aimed to characterize effects of PB on β-catenin signaling at different cellular levels and to elucidate molecular details of the interaction of PB and β-catenin in an in vitro system of mouse hepatoma cells. PB efficiently inhibited signaling through β-catenin. This phenomenon was in-depth characterized at the levels of β-catenin protein accumulation and transcriptional activity. Mechanistic analyses revealed that the effect of PB on β-catenin signaling was independent of the activation of CAR and also independent of the cytosolic multi-protein complex responsible for physiological post-translation control of the β-catenin pathway via initiation of β-catenin degradation. Instead, evidence is provided that PB diminishes β-catenin protein production by inhibition of protein synthesis via signal transduction through EGFR and Src. The proposed mechanism is well in agreement with previously published activities of PB at the EGFR and Src-mediated regulation of β-catenin mRNA translation. Inhibition of β-catenin signaling by PB through the proposed mechanism might explain the inhibitory effect of PB on the growth of specific sub-populations of mouse liver tumors. In conclusion, the present data comprehensively characterize the effect of PB on β-catenin signaling in mouse hepatoma cells in vitro and provides mechanistic insight into the molecular processes underlying the observed effect.

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Towards multiplexed protein–protein interaction analysis using protein tag-specific nanobodies

Cited by 7 publications

References 55 publications

Immunocapture strategies in translational proteomics

Immunocapture strategies in translational proteomics

Evaluation of protein clustering of pancreatic cancer

Inhibition of β-catenin signaling by phenobarbital in hepatoma cells in vitro

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