The abetalipoproteinemia gene is a member of the vitellogenin family and encodes an α–helical domain

@article{Shoulders1994TheAG,
  title={The abetalipoproteinemia gene is a member of the vitellogenin family and encodes an $\alpha$–helical domain},
  author={Carol C. Shoulders and T M Narcisi and J Read and Scot A Chester and D J Brett and James Scott and T A Anderson and David G Levitt and Leonard J. Banaszak},
  journal={Nature Structural Biology},
  year={1994},
  volume={1},
  pages={285-286}
}
A Novel Abetalipoproteinemia Genotype
TLDR
Results indicate that a positively charged amino acid at position 540 in the 97-kDa subunit is critical for the productive association with protein disulfide isomerase.
The structure of vitellogenin provides a molecular model for the assembly and secretion of atherogenic lipoproteins.
TLDR
It is shown that the globular amino-terminal regions of apoB and MTP are closely related in structure to the ancient egg yolk storage protein, vitellogenin (VTG).
The use of a highly informative CA repeat polymorphism within the abetalipoproteinaemia locus (4q22–24)
TLDR
The use of a polymorphic CA dinucleotide repeat in intron 10, MTPIVS10, of the large subunit of the human MTP protein in the analysis of a pregnancy in a consanguineous family, in which abetalipoproteinaemia was suspected, although prenatal diagnosis was subsequently refused.
The role of the microsomal triglygeride transfer protein in abetalipoproteinemia.
TLDR
It was recently demonstrated that abetalipoproteinemia, a hereditary disease characterized as an inability to produce chylomicrons and very low-density lipoproteins in the intestine and liver, results from mutations in the gene encoding the 97-kDa subunit of the microsomal triglyceride transfer protein.
Molecular and functional analysis of two new MTTP gene mutations in an atypical case of abetalipoproteinemia[S]
TLDR
This investigation provides an example of a functional analysis of unclassified variations, which is an absolute necessity for the molecular diagnosis of atypical ABL cases.
Mutations of the microsomal triglyceride-transfer-protein gene in abetalipoproteinemia.
TLDR
It is established that defects of the MTP gene are the predominant, if not sole, cause of hereditary ABL and that an intact carboxyl terminus is necessary for activity.
Apolipophorin II/I, Apolipoprotein B, Vitellogenin, and Microsomal Triglyceride Transfer Protein Genes Are Derived from a Common Ancestor
TLDR
Data indicate that the genes coding for apoLp-II/I, apoB, VTG, and the MTP large subunit are members of the same multigene superfamily, suggesting an ancestral molecule designed to ensure a pivotal event in the intracellular and extracellular transfer of lipids and liposoluble substances.
Instability of crab vitellogenin and its immunological relatedness with mammalian atherogenic lipoproteins
TLDR
It was observed that purified Vg, but not Lv, possessed an intrinsic protease activity with which it underwent autoproteolysis giving rise to several smaller proteins, suggesting the existence of common epitope recognition sites in crab Vg and mammalian lipid transferring proteins.
Molecular Characterization and Developmental Expression of a Retinoid- and Fatty Acid-binding Glycoprotein from Drosophila
TLDR
Immunolocalizations using specific antibodies against RFABG reveal that the protein is initially dispersed through the embryonic amnioserosa sac and latter concentrated at skeletal muscle-epidermis apodemeal contact junctions during larval development, suggesting this novel gene may play an important role in the transport of lipids, including retinoids and fatty acids, in insects.
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References

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Abetalipoproteinemia is caused by defects of the gene encoding the 97 kDa subunit of a microsomal triglyceride transfer protein.
TLDR
Cloned and sequenced the human cDNA encoding microsomal triglyceride transfer protein, which exists as a complex with protein disulphide isomerase in the endoplasmic reticulum, and elucidate a key process in the packaging of apolipoprotein B with lipid.
Absence of microsomal triglyceride transfer protein in individuals with abetalipoproteinemia.
TLDR
This work has shown that MTP activity and the 88-kilodalton component of MTP were present in intestinal biopsy samples from eight control individuals but were absent in four abetalipoproteinemic subjects, suggesting that a defect in MTP is the basis for abetAlipoproteinemia and that M TP is indeed required for lipoprotein assembly.
Cloning and gene defects in microsomal triglyceride transfer protein associated with abetalipoproteinaemia
TLDR
The results indicate that a defect in the gene for the large subunit of MTP is the proximal cause of abetalipopro-teinaemia in these two subjects, and that MTP are required for the secretion of plasma lipoproteins that contain apolipoprotein B.
Lipid transfer proteins: catalysts, transmembrane carriers and signalling intermediates for intracellular and extracellular lipid reactions
TLDR
Recent data suggesting that many intracellular and extracellular lipid transfers formerly considered to be spontaneous may be catalyzed by lipid-binding transfer proteins are reviewed.
Precursor-product relationship between vitellogenin and the yolk proteins as derived from the complete sequence of a Xenopus vitellogenin gene.
TLDR
Comparison of the amino acid sequence of the vitellogenin A2 molecule with biochemical data obtained from the different yolk proteins allowed us to localize the cleavage products on thevitellagenin precursor as follows: NH2 - lipovitellin I - phosvitin (or phosvette II - phOSvette I - LipoviteLLin II - COOH.
The location of bound lipid in the lipovitellin complex.
TLDR
The lipid appears to be bound in the form of a bilayer with the major protein-lipid interactions being hydrophobic and with the lipid headgroups projecting into the bulk solvent and into a solvent-filled space in the cavity.
A comprehensive set of sequence analysis programs for the VAX
TLDR
A group of programs that will interact with each other has been developed for the Digital Equipment Corporation VAX computer using the VMS operating system.
ALSCRIPT: a tool to format multiple sequence alignments.
TLDR
The ALSCRIPT program was developed specifically to allow the easy formatting and graphical display of large multiple alignments, and should be easy to learn by anyone familiar with plotting graphs.
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