Publications
Showing 108 results for Author: Richard J. Giannone
Sep, 2011
Journal
Use of Label-Free Quantitative Proteomics To Distinguish the Secreted Cellulolytic Systems of Caldicellulosiruptor bescii and Caldicellulosiruptor obsidiansis
The understanding of microbial cellulose degradation systems is a crucial prerequisite to designing an effective operating process for the bioconversion of lignocellulosic biomass into sustainable biofuels. Relevant in this context are members of the extremely thermophilic Gram-positive bacteria genus Caldicellulosiruptor that have been shown to efficiently degrade cellulo…
Apr, 2011
Journal
Deletion of the Cel48S cellulase from Clostridium thermocellum
Clostridium thermocellum is a thermophilic anaerobic bacterium that rapidly solubilizes cellulose with the aid of a multienzyme cellulosome complex. Creation of knockout mutants for Cel48S (also known as CelS, SS, and S8), the most abundant cellulosome subunit, was undertaken to gain insight into its role in enzymatic and microbial cellulose solubilization. Cultures of the…
Aug, 2010
Journal
The protein network surrounding the human telomere repeat binding factors TRF1, TRF2, and POT1
Telomere integrity (including telomere length and capping) is critical in overall genomic stability. Telomere repeat binding factors and their associated proteins play vital roles in telomere length regulation and end protection. In this study, we explore the protein network surrounding telomere repeat binding factors, TRF1, TRF2, and POT1 using dual-tag affinity purificat…
Sep, 2009
Book Chapter
The Monitoring and Affinity Purification of Proteins Using Dual-Tags with Tetracysteine Motifs
Identification and characterization of protein-protein interaction networks is essential for the elucidation of biochemical mechanisms and cellular function. Affinity purification in combination with liquid chromatography-tandem mass spectrometry (LC-MS/MS) has emerged as a very powerful tactic for the identification of specific protein-protein interactions. In this chapte…
Sep, 2007
Journal
A dual-tagging system for the affinity purification of mammalian protein complexes
One popular method to elucidate protein-protein interactions involves the native co-purification of an affinity tagged protein and its interacting partners, which are subsequently identified through mass spectrometry (MS) (1). Although straightforward, reproducible, and broadly employed, this strategy is hampered by the efficacy of protein recoveries both in terms of sensi…