Molecular characterization of gene sequences coding for protein disulfide isomerase (PDI) in durum wheat (Triticum turgidum ssp. durum). (Q48375693)

11 February 2018

title

Molecular characterization of gene sequences coding for protein disulfide isomerase (PDI) in durum wheat (Triticum turgidum ssp. durum). (English)

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11 February 2018

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Triticum turgidum

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Ciaffi M

1

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11 February 2018

Paolacci AR

2

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11 February 2018

Dominici L

3

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11 February 2018

Tanzarella OA

4

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11 February 2018

Porceddu E

5

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11 February 2018

language of work or name

English

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publication date

1 March 2001

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11 February 2018

published in

Gene

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11 February 2018

volume

265

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11 February 2018

issue

1-2

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11 February 2018

page(s)

147-156

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11 February 2018

U-rich tracts enhance 3' splice site recognition in plant nuclei

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Nucleotide sequence and developmental expression of duplicated genes encoding protein disulfide isomerase in barley (Hordeum vulgare L.).

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Molecular characterization of an active wheat LMW glutenin gene and its relation to other wheat and barley prolamin genes

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Molecular characterisation of plant endoplasmic reticulum. Identification of protein disulfide-isomerase as the major reticuloplasmin

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Identifying and characterizing a structural domain of protein disulfide isomerase

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Identifying and characterizing a second structural domain of protein disulfide isomerase

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Protein structure prediction. Implications for the biologist

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Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin.

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ERp28, a human endoplasmic-reticulum-lumenal protein, is a member of the protein disulfide isomerase family but lacks a CXXC thioredoxin-box motif

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Protein fold recognition using sequence-derived predictions

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Protein disulphide isomerase: building bridges in protein folding

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Comparison of the expression patterns of genes coding for wheat gluten proteins and proteins involved in the secretory pathway in developing caryopses of wheat.

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Splice site prediction in Arabidopsis thaliana pre-mRNA by combining local and global sequence information

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Nuclear magnetic resonance characterization of the N-terminal thioredoxin-like domain of protein disulfide isomerase

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Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy

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The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules

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Expression of protein disulfide isomerase is elevated in the endosperm of the maize floury-2 mutant

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Intron position as an evolutionary marker of thioredoxins and thioredoxin domains

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Purification, characterization, and intracellular localization of glycosylated protein disulfide isomerase from wheat grains.

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Nucleotide sequence of a wheat cDNA encoding protein disulfide isomerase

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Molecular cloning of a putative plant endomembrane protein resembling vertebrate protein disulfide-isomerase and a phosphatidylinositol-specific phospholipase C

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Splicing of precursors to mRNA in higher plants: mechanism, regulation and sub-nuclear organisation of the spliceosomal machinery

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Mutation of putative branchpoint consensus sequences in plant introns reduces splicing efficiency

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BLAST 2 Sequences, a new tool for comparing protein and nucleotide sequences

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CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

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A new method for predicting signal sequence cleavage sites

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7 January 2021

10.1016/S0378-1119(01)00348-1

Identifiers

DOI

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11 February 2018

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11 February 2018