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Structural Properties of Cruciferin and Napin of Brassica napus (Canola) Show Distinct Responses to Changes in pH and Temperature
46/46 checkable references clean · checked 2026-07-22
Every reference with a DOI in the deposited reference list resolved to a known work in Crossref or DataCite at the dated check, and none carried a retraction, withdrawal, or removal notice.
15 without a DOI — not checked. A reference deposited without a DOI is never matched by title or guessed at; it stays outside the checked set, and this line discloses that.
The 46 checked references that resolve
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Development and storage-protein synthesis in Brassica napus L. embryos in vivo and in vitro
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Detailed Physicochemical Characterization of the 2S Storage Protein from Rape (<i>Brassica napus</i> L.)
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The Native Structure and Composition of the Cruciferin Complex in Brassica napus
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Proteins of<i>Brassicaceae</i>Oilseeds and their Potential as a Plant Protein Source
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The structure of the 12 S globulin from rapeseed (<i>Brassica napus L.</i>)
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Conservation and divergence on plant seed 11S globulins based on crystal structures
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Characterization of the 12S globulin complex of <i>Brassica napus</i>
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Redundant Proteolytic Mechanisms Process Seed Storage Proteins in the Absence of Seed-Type Members of the Vacuolar Processing Enzyme Family of Cysteine Proteases
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The Proteolytic Processing of Seed Storage Proteins in<i>Arabidopsis</i>Embryo Cells Starts in the Multivesicular Bodies
resolves10.1016/S0021-9258(18)45337-9
Nucleotide sequence of a member of the napin storage protein family from Brassica napus.
resolves10.1016/0378-1119(91)90036-B
Characterization and evolution of napin-encoding genes in radish and related crucifers
resolves10.1021/bi961748q
<sup>1</sup>H NMR Assignment and Global Fold of Napin BnIb, a Representative 2S Albumin Seed Protein
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THE EFFECT OF pH ON RAPESEED GLOBULIN (CRUCIFERIN) BINDING TO ANILINONAPHTHALENE-8-SULFONATE
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Stabilization of Fish Oil‐in‐Water Emulsions with Oleosin Extracted from Canola Meal
resolves10.1002/(SICI)1097-0282(199905)49:6<451::AID-BIP3>3.0.CO;2-6
1-Anilino-8-naphthalene sulfonate as a protein conformational tightening agent
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Canola Proteins for Human Consumption: Extraction, Profile, and Functional Properties
resolves10.1002/1097-0010(200103)81:4<391::AID-JSFA823>3.0.CO;2-S
Polypeptide profile and functional properties of defatted meals and protein isolates of canola seeds
resolves10.1111/j.1432-1033.1993.tb18318.x
Disulfide interchange reactions in 11S globulin subunits of <i>Cruciferae</i> seeds
resolves10.1016/j.bbapap.2007.04.008
Napin from Brassica juncea: Thermodynamic and structural analysis of stability
resolves10.1007/s11746-011-1975-9
Solubility Differences of Major Storage Proteins of Brassicaceae Oilseeds
resolves10.1016/0168-9452(86)90151-2
Subunit composition of the globulin fraction of rapeseed (Brassica napus L.)
resolves10.1104/pp.105.062778
Patterns of Protein Oxidation in Arabidopsis Seeds and during Germination
resolves10.1021/bi400625v
Distinct β-Sheet Structure in Protein Aggregates Determined by ATR–FTIR Spectroscopy
resolves10.1016/0304-4157(82)90012-0
Anilinonaphthalene sulfonate as a probe of membrane composition and function
resolves10.1002/9780470110560.ch2
Protein—Ligand Interaction as a Method to Study Surface Properties of Proteins
resolves10.1007/BF00208864
pH-dependent binding of the fluorophore bis-ANS to influenza virus reflects the conformational change of hemagglutinin
resolves10.1021/jf9908704
Heat Denaturation of Soy Glycinin: Influence of pH and Ionic Strength on Molecular Structure
resolves10.1016/S0006-3495(94)80799-4
The use of fluorescence methods to monitor unfolding transitions in proteins
resolves10.1111/j.1365-2621.2004.00795.x
Changes of glycinin conformation due to pH, heat and salt determined by differential scanning calorimetry and circular dichroism
resolves10.1139/o68-178
The proteins of rapeseed (<i>Brassica napus</i> L.) soluble in salt solutions
resolves10.1002/food.19820260139
A reversible dissociation of the 12 S globulin from rapeseed (Brassica napus L.) depending on ionic strength
resolves10.1002/bip.360250307
Examination of the secondary structure of proteins by deconvolved FTIR spectra
resolves10.1002/bip.1968.360061006
Stereochemical criteria for polypeptides and proteins. V. Conformation of a system of three linked peptide units
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Automatic identification of secondary structure in globular proteins
resolves10.1002/food.19900340307
Structural studies on native and chemically modified storage proteins from rapeseed (Brassica napus L.) and related plant proteins
resolves10.1002/(SICI)1521-3803(199808)42:03/04<201::AID-FOOD201>3.3.CO;2-L
The structure and properties of Napin-seed storage protein from rape (Brassica napus L.)
resolves10.1023/A:1007085627485
Minireview: Analysis of Rape Seed Napin Structure and Potential Roles of the Storage Protein
resolves10.1021/bi0352217
Solution Structure of RicC3, a 2S Albumin Storage Protein from <i>Ricinus communis</i><sup>,</sup>
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The effect of heat- and acid-treatment on the structure of rapeseed albumin (napin)
resolves10.1021/jf0202537
Comparison of Protein Chemical and Physicochemical Properties of Rapeseed Cruciferin with Those of Soybean Glycinin
resolves10.1038/227680a0
Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
The 15 references without a DOI — listed, not checked
no DOI — not checkedLarge scale purification of rapeseed proteins (Brassica napus L.)
no DOI — not checkedBlack, M., and Bewley, J. (2000). Seed Technology and Its Biological Basis, CRC Press.
no DOI — not checkedSeed storage proteins: Structures and biosynthesis
no DOI — not checkedWithana-Gamage, T.S. (2013). Structure and Properties of Cruciferin: Investigation of Homohexameric Cruciferin Expressed in Arabidopsis. [Ph.D. Thesis, University of Saskatchewan].
no DOI — not checkedUniPort. Available online: http://www.uniprot.org/.
no DOI — not checkedFluorescence Data Analysis Methods. Available online: http://www.isogen-lifescience.com/uploads/o4/21/o4210uzD8OIHHtyOEhZEkQ/Optim06v1.0---Fluorescence-data-analysis-methods-ILS.pdf.
no DOI — not checkedWanasundara, J.P.D., and McIntosh, T.C. Process of aqueous protein extraction from Brassicaceae oilseeds. Available online: http://www.google.com/patents/US8557963.
no DOI — not checkedRole of the sulfhydryl redox state and disulfide bonds in processing and assembly of 11S seed globulins
no DOI — not checkedWerner, S., Winkler, U., and Stabenau, H. Separation of Native Basic Protein by Cathodic, Discontinuous Polyacrylamide Gel Electrophoresis. Available online: http://www.bio-rad.com/webroot/web/pdf/lsr/literature/Bulletin_2376.pdf.
no DOI — not checkedPurification and characterization of isoforms of b-N-acetylhexosaminidase from mungbean seedlings
no DOI — not checkedDetermination of secondary structure in protein aggregates using attenuated total reflectance FTIR infrared
no DOI — not checkedWeichel, M., Bassarab, S., and Garidel, P. Probing Thermal Stability of MAbs by Intrinsic Tryptophan Fluorescence. Available online: http://www.bioprocessintl.com/manufacturing/antibody-non-antibody/probing-thermal-stability-of-mabs-by-intrinsic-tryptophan-fluorescence-182648/.
no DOI — not checkedFink, A.L. (2001). eLS, John Wiley & Sons, Ltd.
no DOI — not checkedFirestone, D.E. (1997). Official Methods and Recommended Practices of the AOCS, AOCS Press. [5th ed.].
no DOI — not checkedLatimer, D.G.W., and Horwitz, D.W. (2005). Official Methods of Analysis of AOAC International, AOAC International. [18th ed.].
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