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Prealbumin, transthyretin, TTR
This gene encodes transthyretin, one of the three prealbumins including alpha-1-antitrypsin, transthyretin and orosomucoid. Transthyretin is a carrier protein; it transports thyroid hormones in the plasma and cerebrospinal fluid, and also transports retinol (vitamin A) in the plasma. The protein consists of a tetramer of identical subunits. More than 80 different mutations in this gene have been reported; most mutations are related to amyloid deposition, affecting predominantly peripheral nerve and/or the heart, and a small portion of the gene mutations is non-amyloidogenic. The diseases caused by mutations include amyloidotic polyneuropathy, euthyroid hyperthyroxinaemia, amyloidotic vitreous opacities, cardiomyopathy, oculoleptomeningeal amyloidosis, meningocerebrovascular amyloidosis, carpal tunnel syndrome, etc. [provided by RefSeq, Jan 2009] (from NCBI)
Top mentioned proteins: CAN, HAD, AGE, fibrillin-1, ACID
Papers using Prealbumin antibodies
Oral Transmissibility of Prion Disease Is Enhanced by Binding to Soil Particles
Mourton-Gilles Chantal et al., In BMC Veterinary Research, 2006
... 6: healthy ARR/ARR sheep; border line control "Ctl": 100 ng of Recombinant full length Human Prealbumin, amino acids 21-147, 13,8 kDa abcam n°92931) ...
Oxidative and nitrative DNA damage as biomarker for carcinogenesis with special reference to inflammation
Bernstein Carol et al., In Clinical and Experimental Gastroenterology, 2005
All wells contained the TransMessenger Transfection Reagent (TTR) from QIAGEN.
Mice homozygous for a targeted disruption of the proto-oncogene int-2 have developmental defects in the tail and inner ear
Deng Chu-Xia et al., In International Journal of Biological Sciences, 1992
... TTR-Cre transgenic mice (X.Y ...
Papers on Prealbumin
The Free Thiol of Transthyretin in Human Plasma is Most Accessible to Modification/Oxidation.
Takao et al., In Anal Chem, 06 Nov 2015
However, contrary to our expectations, transthyretin (TTR), which also has a single free thiol, was found to be the major protein that was the most susceptible to modification/oxidation.
The Val142Ile transthyretin cardiac amyloidosis: not only an Afro-American pathogenic variant? A single-centre Italian experience.
Perfetto et al., Florence, Italy. In J Cardiovasc Med (hagerstown), 01 Nov 2015
UNASSIGNED: Transthyterin amyloidosis is a life-threatening disorder caused by the deposition of hepatocyte-derived transthyretin (TTR) amyloid in various tissues and organs.
Cyclin E1 plays a key role in balancing between totipotency and differentiation in human embryonic cells.
Van de Velde et al., Brussels, Belgium. In Mol Hum Reprod, 27 Oct 2015
This CCNE1-positive cell population was associated with visceral endoderm based on transthyretin expression and marked the third cell lineage within the ICM, besides EPI and PrE, which had never been described before.
Plasma Transthyretin as a Biomarker of Lean Body Mass and Catabolic States.
Bernstein et al., Strasbourg, France. In Adv Nutr, 30 Sep 2015
Plasma transthyretin (TTR) is a plasma protein secreted by the liver that circulates bound to retinol-binding protein 4 (RBP4) and its retinol ligand.
Proteomic pilot study of tuberculosis pleural effusion.
Dai et al., Kunming, China. In Biomed Mater Eng, 17 Sep 2015
We found five characteristic proteins: C1-inhibitor (C1-INH), transthyretin (TTR), human complement fragment 3b (C3b), human ceruloplasmin (CP), and Z34c protein fragment Fc (Z34c-Fc).
Cardiac amyloidosis: where are we today?
Hawkins et al., London, United Kingdom. In J Intern Med, Aug 2015
A genetic variant in the gene for transthyretin (TTR), which is present in 3-4% of African Americans and probably a similar proportion of black individuals of African descent generally, appears to be associated with increased susceptibility to developing cardiac ATTR amyloidosis in older age.
The transthyretin amyloidoses: advances in therapy.
Gillmore et al., Carlsbad, United States. In Postgrad Med J, Aug 2015
There are two forms of transthyretin (TTR) amyloidosis: non-hereditary and hereditary.
Non-invasive Identification of ATTRwt Cardiac Amyloid (aka Senile Cardiac Amyloid): The Re-emergence of Nuclear Cardiology.
Maurer, New York City, United States. In Am J Med, Jul 2015
Amyloid infiltration of the myocardial is an underappreciated contributing factor to HFpEF that is often caused by misfolded monomers or oligomers of the protein transthyretin.
EFF-1-mediated regenerative axonal fusion requires components of the apoptotic pathway.
Hilliard et al., Brisbane, Australia. In Nature, Feb 2015
PSR-1 functions cell-autonomously in the regrowing neuron and, instead of acting in its canonical signalling pathway, acts in a parallel phagocytic pathway that includes the transthyretin protein TTR-52, as well as CED-7, NRF-5 and CED-6 (refs 9, 10, 11, 12).
The amyloidogenic V122I transthyretin variant in elderly black Americans.
Solomon et al., Houston, United States. In N Engl J Med, Feb 2015
METHODS: We determined genotype status for the transthyretin gene (TTR) in 3856 black participants in the Atherosclerosis Risk in Communities study and assessed clinical profiles, mortality, and the risk of incident heart failure in V122I TTR variant carriers (124 participants [3%]) versus noncarriers (3732 participants).
Transport of thyroid hormones via the choroid plexus into the brain: the roles of transthyretin and thyroid hormone transmembrane transporters.
Van Herck et al., Australia. In Front Neurosci, Dec 2014
In reptiles, birds and mammals, the main protein synthesized and secreted by the choroid plexus is a thyroid hormone distributor protein: transthyretin.
Therapeutic Oligonucleotides Targeting Liver Disease: TTR Amyloidosis.
Schmidt et al., Münster, Germany. In Molecules, Dec 2014
Mutations of the gene encoding transthyretin (TTR), expressed in vast amounts by the liver, result in a complex degenerative disease, termed familial amyloid polyneuropathy (FAP).
Amyloid fibrils nucleated and organized by DNA origami constructions.
Seeman et al., New York City, United States. In Nat Nanotechnol, Jul 2014
The fibrils are built by modifying the synthetic peptide fragment corresponding to residues 105-115 of the amyloidogenic protein transthyretin and a DNA origami construct is used to form 20-helix DNA nanotubes with sufficient space for the fibrils inside.
Repurposing diflunisal for familial amyloid polyneuropathy: a randomized clinical trial.
Diflunisal Trial Consortium et al., Umeå, Sweden. In Jama, 2014
IMPORTANCE: Familial amyloid polyneuropathy, a lethal genetic disease caused by aggregation of variant transthyretin, induces progressive peripheral nerve deficits and disability.
Safety and efficacy of RNAi therapy for transthyretin amyloidosis.
Suhr et al., Porto, Portugal. In N Engl J Med, 2013
BACKGROUND: Transthyretin amyloidosis is caused by the deposition of hepatocyte-derived transthyretin amyloid in peripheral nerves and the heart.
Transthyretin (TTR) cardiac amyloidosis.
Berk et al., Boston, United States. In Circulation, 2012
Transthyretin cardiac amyloidosis is an underappreciated contributor to heart failure in elderly patients.
STT3B-dependent posttranslational N-glycosylation as a surveillance system for secretory protein.
Kai et al., Kumamoto, Japan. In Mol Cell, 2012
Data show that prolonged transthyretin (TTR) unfolding induces externalization of cryptic N-glycosylation site and triggers STT3B-dependent posttranslational N-glycosylation.
Identification of beta-amyloid-binding sites on transthyretin.
Murphy et al., Madison, United States. In Protein Eng Des Sel, 2012
Strong binding of beta-amyloid peptide to TIAALLSPYSYS (residues 106-117) was detected, corresponding to strand G on the inner beta-sheet of TTR.
The electrocardiographic features associated with cardiac amyloidosis of variant transthyretin isoleucine 122 type in Afro-Caribbean patients.
Anderson et al., London, United Kingdom. In Am Heart J, 2012
Electrocardiographic voltages meet the criteria for LVH in one quarter of patients with ATTR V122I cardiac amyloidosis.
Supercentenarians and transthyretin amyloidosis: the next frontier of human life extension.
Young et al., Los Angeles, United States. In Prev Med, 2012
Discusses TTR gene mutations in amyloidosis and if amyloidosis has a role in the aging process. Explores if treating amyloidosis increases human lifespan and increases quality of life in the oldest old.
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