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the TBG promoter has a role in sustaining transgene expression in liver-specific pattern
A new SERPINA7 variant associated with thyroxine-binding globulin deficiency in three siblings.
THBG is a potential plasma biomarker for COPD.
mutation in a liver-specific enhancer region of the TBG gene caused inherited TBG deficiency. To our knowledge, the present study is the first report of an inherited endocrine disorder caused by a mutation in an enhancer region.
TBG allosteric regulation is entropy driven. The presence of multiple S states may allow more efficient T4 release due to protease activity.
Allosteric modulation of hormone release from thyroxine and corticosteroid-binding globulins.
Freshly isolated TBG-Chicago exists in loop expelled conformation. At 37C, the protein readily converts to a more stable loop inserted conformation with enhanced heat stability.
an intragenic A/G polymorphism (125 bp upstream from exon 2) was identified. complete TBG deficiency was homozygous for the polymorphic TBG allele.
Two novel variants in the thyroxine-binding globulin gene behind the diagnosis of TBG deficiency. homozygous. One involved codon 23 (TCA-->TAA) and the other, codon 223.
Loop variants of the serpin thyroxine-binding globulin: implications for hormone release upon limited proteolysis.
guanine deletion at position 1711, codon 201 (Asp) in exon 2 (GAC --> AC) led to a frame shift and premature termination at codon 206, causing a short TBG protein of 205 amino acids (AA) compared to 395 AA of the normal TBG.
new serpina7 gene variant in three members of the same family results in the replacement of the normal asparagine 233 by isoleucine and, subsequently, in disruption of a glycosylation site
The first exon (exon 0) is a short noncoding sequence located 1.62 kilobase pairs (kbp) upstream from exon 1. HNF-1 site (located 65 bp upstream of the TSS) is required for the hepatocyte specific expression of the hTBG gene.
polymorphism in exon 2 in thyroxine-binding globulin is a candidate for the causative variation affecting testis size in boars.
There are three proteins including thyroxine-binding globulin (TBG), transthyretin and albumin responsible for carrying the thyroid hormones thyroxine (T4) and 3,5,3'-triiodothyronine (T3) in the bloodstream. This gene encodes the major thyroid hormone transport protein, TBG, in serum. It belongs to the serpin family in genomics, but the protein has no inhibitory function like many other members of the serpin family. Mutations in this gene result in TGB deficiency, which has been classified as partial deficiency, complete deficiency, and excess, based on the level of serum TBG. Alternatively spliced transcript variants encoding different isoforms have been found, but the full-length nature of these variants has not been determined.
, serine (or cysteine) peptidase inhibitor, clade A (alpha-1 antipeptidase, antitrypsin), member 7
, serine (or cysteine) proteinase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 7
, serpin A7
, thyroxine-binding globulin
, thyroxin-binding globulin
, serine (or cysteine) peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 7
, serine (or cysteine) proteinase inhibitor clade A (alpha-1 antiproteinase antitrypsin) member 7
, serine (or cysteine) proteinase inhibitor, clade A, member 7