2- and 8-Azido photoaffinity probes. 1. Enzymic synthesis, characterization and biological properties of 2- and 8-azido photoprobes of 2-5A and photolabeling of 2-5A binding proteins

Biochemistry ◽  
1988 ◽  
Vol 27 (24) ◽  
pp. 8840-8846 ◽  
Author(s):  
Robert J. Suhadolnik ◽  
Katalin Kariko ◽  
Robert W. Sobol ◽  
Shi Wu Li ◽  
Nancy L. Reichenbach ◽  
...  
Keyword(s):  
Binding Proteins ◽  
Biological Properties ◽  
Enzymic Synthesis ◽  
Photoaffinity Probes

scholarly journals Insulin-like growth factor (IGF)-II binding to IGF-binding proteins and IGF receptors is modified by deletion of the N-terminal hexapeptide or substitution of arginine for glutamate-6 in IGF-II

1993 ◽  
Vol 293 (3) ◽  
pp. 713-719 ◽  
Author(s):  
G L Francis ◽  
S E Aplin ◽  
S J Milner ◽  
K A McNeil ◽  
F J Ballard ◽  
...  
Keyword(s):  
Growth Factor ◽  
Binding Proteins ◽  
Biological Activities ◽  
Biological Properties ◽  
Hepatoma Cells ◽  
Insulin Like Growth Factor ◽  
Igf Binding Proteins ◽  
Anabolic Response ◽  
Igf I ◽  
Igf Binding

Recombinant insulin-like growth factor-II (IGF-II) and two structural analogues, des(1-6)IGF-II and [Arg6]-IGF-II, were produced to investigate the role of N-terminal residues in binding to IGF-binding proteins (IGFBPs) and hence the biological properties of the modified peptides. The growth factors were modelled on two previously characterized variants of IGF-I, des(1-3)IGF-I and [Arg3]-IGF-I, which both show substantially decreased binding to IGFBPs and were expressed as fusion proteins in Escherichia coli. The biological activities of the corresponding analogues of IGF-I and IGF-II were compared in rat L6 myoblasts and H35B hepatoma cells. In the L6-myoblast protein-synthesis assay, the IGF-II analogues, des(1-6)IGF-II and [Arg6]-IGF-II, were slightly more potent than IGF-II but about 10-fold less potent than IGF-I and 100-fold less potent than the respective IGF-I analogues, des(1-3)IGF-I and [Arg3]IGF-I. In H35 hepatoma cells the anabolic response measured was the inhibition of protein breakdown, and the potency order was insulin >>> [Arg3]-IGF-I > des(1-3)IGF-I > [Arg6]-IGF-II > des(1-6)IGF-II > IGF-I > IGF-II. Binding of the IGFs and their analogues to the type 1 IGF receptor in L6 myoblasts and to the insulin receptor in H35 hepatoma cells did not fully explain the observed anabolic potency differences. Moreover, binding of all four analogues to the IGFBPs secreted by L6 myoblasts and H35B hepatoma cells was greatly decreased compared with the parent IGF. We conclude that the observed anabolic response to each IGF was determined by their relative binding to the competing cell receptor and IGFBP binding sites present.

Chemical Synthesis of Diubiquitin-Based Photoaffinity Probes for Selectively Profiling Ubiquitin-Binding Proteins

2017 ◽  
Vol 129 (10) ◽  
pp. 2788-2792 ◽  
Author(s):  
Jun Liang ◽  
Lin Zhang ◽  
Xiang-Long Tan ◽  
Yun-Kun Qi ◽  
Shan Feng ◽  
...  
Keyword(s):  
Chemical Synthesis ◽  
Binding Proteins ◽  
Ubiquitin Binding ◽  
Photoaffinity Probes

scholarly journals Protocol for identification and validation of 2′3′-cGAMP-binding proteins by photoaffinity probes

2022 ◽  
Vol 3 (1) ◽  
pp. 101076
Author(s):  
Yingjie Hou ◽  
Heng Lu ◽  
Le Sun ◽  
Yaoyang Zhang ◽  
Hong Jiang
Keyword(s):  
Binding Proteins ◽  
Photoaffinity Probes

scholarly journals APRICOT: an integrated computational pipeline for the sequence-based identification and characterization of RNA-binding proteins

2016 ◽  
Author(s):  
Malvika Sharan ◽  
Konrad U. Förstner ◽  
Ana Eulalio ◽  
Jörg Vogel
Keyword(s):  
Large Scale ◽  
Binding Proteins ◽  
Rna Binding ◽  
Markov Models ◽  
Rna Binding Proteins ◽  
Experimental Studies ◽  
Biological Properties ◽  
Computational Pipeline ◽  
Identification And Characterization

ABSTRACTRNA-binding proteins (RBPs) have been established as core components of several post-transcriptional gene regulation mechanisms. Experimental techniques such as cross-linking and co-immunoprecipitation have enabled the identification of RBPs, RNA-binding domains (RBDs), and their regulatory roles in the eukaryotic species such as human and yeast in large-scale. In contrast, our knowledge of the number and potential diversity of RBPs in bacteria is poorer due to the technical challenges associated with the existing global screening approaches.We introduce APRICOT, a computational pipeline for the sequence-based identification and characterization of proteins using RBDs known from experimental studies. The pipeline identifies functional motifs in protein sequences using Position Specific Scoring Matrices and Hidden Markov Models of the functional domains and statistically scores them based on a series of sequence-based features. Subsequently, APRICOT identifies putative RBPs and characterizes them by several biological properties. Here we demonstrate the application and adaptability of the pipeline on large-scale protein sets, including the bacterial proteome of Escherichia coli. APRICOT showed better performance on various datasets compared to other existing tools for the sequence-based prediction of RBPs by achieving an average sensitivity and specificity of 0.90 and 0.91 respectively. The command-line tool and its documentation are available at https://pypi.python.org/pypi/bio-apricot

Photoaffinity probes for gibberellin-binding proteins

1992 ◽  
Vol 31 (5) ◽  
pp. 1459-1464 ◽  
Author(s):  
Michael H. Beale ◽  
Richard Hooley ◽  
Sally J. Smith ◽  
Robert P. Walker
Keyword(s):  
Binding Proteins ◽  
Photoaffinity Probes

Chemical Synthesis of Diubiquitin-Based Photoaffinity Probes for Selectively Profiling Ubiquitin-Binding Proteins

2017 ◽  
Vol 56 (10) ◽  
pp. 2744-2748 ◽  
Author(s):  
Jun Liang ◽  
Lin Zhang ◽  
Xiang-Long Tan ◽  
Yun-Kun Qi ◽  
Shan Feng ◽  
...  
Keyword(s):  
Chemical Synthesis ◽  
Binding Proteins ◽  
Ubiquitin Binding ◽  
Photoaffinity Probes
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