Literature DB >> 12440943

Plant protein families and their relationships to food allergy.

P R Shewry1, F Beaudoin, J Jenkins, S Griffiths-Jones, E N Mills.   

Abstract

The analysis of plant proteins has a long and distinguished history, with work dating back over 250 years. Much of the work has focused on seed proteins, which are important in animal nutrition and food processing. Early studies classified plant proteins into groups based on solubility ('Osborne fractions') or protein function. More recently, families have been defined based on stuctural and evolutionary relationships. One of the most widespread groups of plant proteins is the prolaminin superfamily, which comprises cereal seed storage proteins, a range of low-molecular-mass sulphur-rich proteins (many of which are located in seeds) and some cell wall glycoproteins. This superfamily includes several major types of plant allergen: non-specific lipid transfer proteins, cereal seed inhibitors of alpha-amylase and/or trypsin, and 2 S albumin storage proteins of dicotyledonous seeds.

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Year:  2002        PMID: 12440943     DOI: 10.1042/bst0300906

Source DB:  PubMed          Journal:  Biochem Soc Trans        ISSN: 0300-5127            Impact factor:   5.407


  20 in total

1.  Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions.

Authors:  Katrin Lehmann; Kristian Schweimer; Gerald Reese; Stefanie Randow; Martin Suhr; Wolf-Meinhard Becker; Stefan Vieths; Paul Rösch
Journal:  Biochem J       Date:  2006-05-01       Impact factor: 3.857

2.  P5-type sulfhydryl oxidoreductase promotes the sorting of proteins to protein body I in rice endosperm cells.

Authors:  Yayoi Onda; Yasushi Kawagoe
Journal:  Plant Signal Behav       Date:  2013-01-08

3.  A microarray-based comparative analysis of gene expression profiles during grain development in transgenic and wild type wheat.

Authors:  Per L Gregersen; Henrik Brinch-Pedersen; Preben B Holm
Journal:  Transgenic Res       Date:  2005-12       Impact factor: 2.788

4.  Purification, identification and preliminary crystallographic studies of Pru du amandin, an allergenic protein from Prunus dulcis.

Authors:  Vineet Gaur; Dhruv K Sethi; Dinakar M Salunke
Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2007-12-20

5.  Comparative sequence analysis of the region harboring the hardness locus in barley and its colinear region in rice.

Authors:  Katherine S Caldwell; Peter Langridge; Wayne Powell
Journal:  Plant Physiol       Date:  2004-10-01       Impact factor: 8.340

6.  Sequencing of the Triticum monococcum hardness locus reveals good microcolinearity with rice.

Authors:  N Chantret; A Cenci; F Sabot; O Anderson; J Dubcovsky
Journal:  Mol Genet Genomics       Date:  2004-03-11       Impact factor: 3.291

7.  Sequence-specific 1H, 13C and 15N resonance assignments of Ara h 6, an allergenic 2S albumin from peanut.

Authors:  Katrin Lehmann; Kristian Schweimer; Philipp Neudecker; Paul Rösch
Journal:  J Biomol NMR       Date:  2004-05       Impact factor: 2.835

8.  2S Albumin Storage Proteins: What Makes them Food Allergens?

Authors:  F Javier Moreno; Alfonso Clemente
Journal:  Open Biochem J       Date:  2008-02-06

Review 9.  Cross-reactivity of peanut allergens.

Authors:  Merima Bublin; Heimo Breiteneder
Journal:  Curr Allergy Asthma Rep       Date:  2014-04       Impact factor: 4.806

Review 10.  Structure of allergens and structure based epitope predictions.

Authors:  Fabio Dall'antonia; Tea Pavkov-Keller; Klaus Zangger; Walter Keller
Journal:  Methods       Date:  2013-07-23       Impact factor: 3.608

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