Literature DB >> 14649894

Non-denaturing electrospray ionisation-mass spectrometry reveals ligand selectivity in histamine-binding protein RaHBP2.

Neil J Oldham1, Olga Lissina, Miles A Nunn, Guido C Paesen.   

Abstract

ESI-MS has been used to probe the non-covalent interactions between a histamine-binding protein, from Rhipicephalus appendiculatus, and a range of bioactive amine ligands.

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Year:  2003        PMID： 14649894     DOI： 10.1039/b306929j

Source DB:  PubMed          Journal:  Org Biomol Chem        ISSN： 1477-0520            Impact factor:   3.876


  3 in total

1.  Collision induced unfolding of protein ions in the gas phase studied by ion mobility-mass spectrometry: the effect of ligand binding on conformational stability.

Authors:  Jonathan T S Hopper; Neil J Oldham
Journal:  J Am Soc Mass Spectrom       Date:  2009-07-01       Impact factor: 3.109

2.  Covalent modification of stathmin by CCNU determined by FTMS analysis of modified proteins and tryptic peptides.

Authors:  Wells W Wu; Guanghui Wang; Xing-Jie Liang; John K Park; Rong-Fong Shen
Journal:  Biochem Biophys Res Commun       Date:  2007-12-26       Impact factor: 3.575

Review 3.  Structure and mechanism in salivary proteins from blood-feeding arthropods.

Authors:  John F Andersen
Journal:  Toxicon       Date:  2009-11-26       Impact factor: 3.033
  3 in total

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