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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 11 Dec 2014.


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, fibrillin-1, AGE, 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
Oculoleptomeningeal Amyloidosis associated with transthyretin Leu12Pro in an African patient.
Reilly et al., London, United Kingdom. In J Neurol, 09 Jan 2015
UNLABELLED: Oculoleptomeningeal amyloidosis is a rare manifestation of hereditary transthyretin (TTR) amyloidosis.
Integrin genetic variants and stage-specific tumor recurrence in patients with stage II and III colon cancer.
Lenz et al., Los Angeles, United States. In Pharmacogenomics J, 09 Jan 2015
Moving from the hypothesis that ITGs could have different effects in stage II and III colon cancer, we tested whether a comprehensive panel of germline single-nucleotide polymorphisms (SNPs) in ITG genes could predict stage-specific time to tumor recurrence (TTR).
Liver Transplantation in Transthyretin Amyloidosis: Issues and Challenges.
Lobato et al., Porto, Portugal. In Liver Transpl, 06 Jan 2015
UNLABELLED: Hereditary transthyretin amyloidosis (ATTR) is a rare worldwide autosomal dominant disease caused by systemic deposition of an amyloidogenic variant of transthyretin (TTR), usually derived from a single amino acid substitution in the TTR gene.
Binding site asymmetry in human transthyretin: insights from a joint neutron and X-ray crystallographic analysis using perdeuterated protein.
Forsyth et al., United Kingdom. In Iucrj, 01 Dec 2014
UNLABELLED: Human transthyretin has an intrinsic tendency to form amyloid fibrils and is heavily implicated in senile systemic amyloidosis.
Pathophysiology and treatment of cardiac amyloidosis.
Sher et al., Rochester, United States. In Nat Rev Cardiol, 14 Nov 2014
Mass spectroscopy can be used to determine the protein subunit and classify the disease as immunoglobulin light-chain amyloidosis or transthyretin-related amyloidosis associated with mutant or wild-type TTR (formerly known as familial amyloid cardiomyopathy and senile cardiac amyloidosis, respectively).
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.
[Transthyretin-related amyloidotic cardiomyopathy: looking for the etiological treatment].
Rapezzi et al., In G Ital Cardiol (rome), May 2014
Transthyretin (TTR)-related amyloidosis is a disease caused by the deposition of insoluble fibrils deriving from the misfolding of TTR, a protein mainly produced by the liver.
Repurposing diflunisal for familial amyloid polyneuropathy: a randomized clinical trial.
Diflunisal Trial Consortium et al., Umeå, Sweden. In Jama, Jan 2014
IMPORTANCE: Familial amyloid polyneuropathy, a lethal genetic disease caused by aggregation of variant transthyretin, induces progressive peripheral nerve deficits and disability.
Contemporary treatment of amyloid heart disease.
Rysava et al., Praha, Czech Republic. In Curr Pharm Des, Dec 2013
Although cardiac involvement may occur in all types of amyloidoses, clinically relevant amyloid cardiomyopathy is a typical feature of AL amyloidosis and transthyretin-related amyloidoses.
Amyloid-clearing proteins and their epigenetic regulation as a therapeutic target in Alzheimer's disease.
Turner et al., Leeds, United Kingdom. In Front Aging Neurosci, Dec 2013
We have also observed that another amyloid-clearing protein, namely transthyretin (TTR), is also regulated in the neuronal cell by a mechanism similar to NEP.
Recent advances in transthyretin amyloidosis therapy.
Ando et al., Kumamoto, Japan. In Transl Neurodegener, Dec 2013
Mutant (MT) forms of transthyretin (TTR) cause the most common type of autosomal-dominant hereditary systemic amyloidosis-familial amyloidotic polyneuropathy (FAP).
Transport of thyroid hormone in brain.
Köhrle et al., Berlin, Germany. In Front Endocrinol (lausanne), Dec 2013
One of these proteins, transthyretin is also present in the cerebrospinal fluid (CSF) after being secreted by the choroid plexus.
Safety and efficacy of RNAi therapy for transthyretin amyloidosis.
Suhr et al., Porto, Portugal. In N Engl J Med, Sep 2013
BACKGROUND: Transthyretin amyloidosis is caused by the deposition of hepatocyte-derived transthyretin amyloid in peripheral nerves and the heart.
Robust circadian oscillations in growing cyanobacteria require transcriptional feedback.
O'Shea et al., Cambridge, United States. In Science, Jun 2013
Layered on top of the PTR is transcriptional-translational feedback regulation (TTR), common to all circadian systems, consisting of a negative feedback loop in which KaiC regulates its own production.
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.
Panobinostat in patients with relapsed/refractory Hodgkin's lymphoma after autologous stem-cell transplantation: results of a phase II study.
Engert et al., Houston, United States. In J Clin Oncol, 2012
Secondary end points included ORR by independent central review, time to response (TTR), duration of response (DOR), progression-free survival (PFS), overall survival, and safety.
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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