Tecan

Laser Scanner - Scientific citations

 ««  «  1  2  »  »» 1 - 5 from 8

Anal. Chem., 77 (11), 3437 -3443, 2005. 10.1021/ac0483421 S0003-2700(04)08342-8
Title An Aptamer-Based Protein Biochip.
Authors Karin Stadtherr, Hans Wolf, Petra Lindner
Institution Institut für Medizinische Mikrobiologie und Hygiene, Universität Regensburg, Regensburg, Germany.
Journal Anal. Chem., 77 (11), 3437 -3443, 2005. 10.1021/ac0483421 S0003-2700(04)08342-8
Abstract This study shows the suitability of nucleic acid aptamers as low molecular weight receptors on biochips for sensitive and specific protein detection.
Impact Factor 5.287 
 
J Am Chem Soc. 2006 May 3;128(17):5913-22.
Title Uncovering Quantitative Protein Interaction Networks for Mouse PDZ Domains using Protein Microarrays.
Authors Stiffler MA, Grantcharova VP, Sevecka M, MacBeath G.
Institution Department of Chemistry and Chemical Biology, Harvard University, 12 Oxford Street, Cambridge, Massachusetts 02138, USA.
Journal J Am Chem Soc. 2006 May 3,128(17):5913-22.
Abstract One of the principal challenges in systems biology is to uncover the networks of protein-protein interactions that underlie most biological processes. To date, experimental efforts directed at this problem have largely produced only qualitative networks that are replete with false positives and false negatives. Here, we describe a domain-centered approach--compatible with genome-wide investigations--that enables us to measure the equilibrium dissociation constant (K(D)) of recombinant PDZ domains for fluorescently labeled peptides that represent physiologically relevant binding partners. Using a pilot set of 22 PDZ domains, 4 PDZ domain clusters, and 20 peptides, we define a gold standard dataset by determining the K(D) for all 520 PDZ-peptide combinations using fluorescence polarization. We then show that microarrays of PDZ domains identify interactions of moderate to high affinity (K(D) < or = 10 microM) in a high-throughput format with a false positive rate of 14% and a false negative rate of 14%. By combining the throughput of protein microarrays with the fidelity of fluorescence polarization, our domain/peptide-based strategy yields a quantitative network that faithfully recapitulates 85% of previously reported interactions and uncovers new biophysical interactions, many of which occur between proteins that are co-expressed. From a broader perspective, the selectivity data produced by this effort reveal a strong concordance between protein sequence and protein function, supporting a model in which interaction networks evolve through small steps that do not involve dramatic rewiring of the network.
 
J. Biol. Chem., Vol. 281, Issue 12, 8126-8134, March 24, 2006
Title Gemin8 Is a Novel Component of the Survival Motor Neuron Complex and Functions in Small Nuclear Ribonucleoprotein Assembly.
Authors Claudia Carissimi, Luciano Saieva, Jennifer Baccon, Pieranna Chiarella, Alessio Maiolica , Alan Sawyer, Juri Rappsilber, Livio Pellizzoni
Institution Dulbecco Telethon Institute, Institute of Cell Biology, Consiglio Nazionale delle Ricerche, 00016 Monterotondo Scalo, Rome, Italy.
Journal J. Biol. Chem., Vol. 281, Issue 12, 8126-8134, March 24, 2006
Abstract By mass spectrometry analysis of SMN complexes purified from HeLa cells, a novel protein that is evolutionarily conserved in metazoans was identified, and named Gemin8. It is a novel integral component of the SMN complex and extend the repertoire of cellular proteins involved in the pathway of snRNP biogenesis.
Text Page 2, Column 1, Paragraph 4
Impact Factor 5.581 
 
J. Biol. Chem., Vol. 281, Issue 48, 37009-37016, December 1, 2006
Title Gemin8 Is Required for the Architecture and Function of the Survival Motor Neuron Complex.
Authors Claudia Carissimi, Luciano Saieva, Francesca Gabanella, Livio Pellizzoni
Institution Dulbecco Telethon Institute, Institute of Cell Biology, Consiglio Nazionale delle Ricerche, Monterotondo Scalo, Rome 00016, Italy.
Journal J. Biol. Chem., Vol. 281, Issue 48, 37009-37016, December 1, 2006
Abstract Gemin8 has an essential role for the proper structural organization of the survival motor neuron (Sm) complex and the involvement of the heteromeric subunit containing Gemin6, Gemin7, Gemin8, and Unrip in the recruitment of Sm proteins to the snRNP assembly pathway.
Text Page 2, Column 1, Paragraph 3
Impact Factor 5.581 
 
Nature 439, 168-174 (12 January 2006) | doi:10.1038/nature04177; Received 7 July 2005; Accepted 30 August 2005; Published online 6 November 2005
Title A quantitative protein interaction network for the ErbB receptors using protein microarrays.
Authors Richard B. Jones, Andrew Gordus, Jordan A. Krall, Gavin MacBeath
Institution Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts 02138, USA.
Journal Nature 439, 168-174 (12 January 2006) | doi:10.1038/nature04177, Received 7 July 2005, Accepted 30 August 2005, Published online 6 November 2005
Abstract By performing a comprehensive analysis of SH2/PTB-mediated inter-actions with the ErbB receptors, a quantitative network that reveals the ability of each receptor to recruit signalling proteins upon activation was uncovered and 116 new biophysical interactions were identified.
Text NA
Impact Factor 28.751 
 
 ««  «  1  2  »  »» 1 - 5 from 8

Overview
Product Details
Related topics
Products » Microarray Products » Laser Scanner »