Results 11 to 20 of about 28,989 (238)

Management of transthyretin amyloidosis. [PDF]

Swiss medical weekly, 2021
Transthyretin amyloidosis (ATTR amyloidosis) is a disease caused by deposition of transthyretin fibrils in organs and tissues, which causes their dysfunction.
Monney, P., Alessio Mylonas, Hübers, A., Gaspert, Ariana, Kessler, C., Ulrike Bacher, Guido Stirnimann, Magini, G., Mihaylova, Violeta, Ariana Gaspert, Gerber, Bernhard; https://orcid.org/, Fehr, Thomas, Adalgisa Condoluci, Gerull, S., Adrian Schmidt, Djerbi, N., Nadia Djerbi, Vetter, F., Treglia, Giorgio; https://orcid.org/, Kessler, Chiara, Laptseva, Natallia, Arosio, P., Laptseva, N., Bode, P., Mihaylova, V., Giulia Magini, Harald Seeger, Bacher, U., Flammer, Andreas J; https://orcid.org/, Thomas Suter, Alexandar Tzankov, Théaudin, M., Stefan Dirnhofer, Seeger, Harald, Pazhenkottil, A.P., Chiara Kessler, Stämpfli, Simon F, Axel Rüfer, Djerbi, Nadia, Flammer, A.J., Flammer, Andreas J, Zweier, Markus, Meyer, Martin, Fehr, T., Dirnhofer, Stefan, Peter Bode, Averaimo, Manuela, Hübers, Annemarie, Vetter, Friederike, Friederike Vetter, Schmidt, A., Andreas J. Flammer, Averaimo, M., Rüfer, A., Giorgio Treglia, Markus Zweier, Raphael Knöpfel, Nkoulou, René, Gerber, Bernhard, Thomas Fehr, Gerull, Sabine, Manuela Averaimo, Martin Meyer, Manka, Robert, Manka, R., Pierre Monney, Schwotzer, Rahel, Heimgartner, R., Mazzucchelli, Luca, Rüfer, Axel, Knöpfel, Raphael, Gerber, B., Monney, Pierre, Suter, Thomas, Thomas Pabst, Simon F. Stämpfli, Théaudin, Marie, Suter, T., Treglia, Giorgio, Tzankov, A., Garofalo, M., Stirnimann, Guido, Sabine Gerull, Schmidt, Adrian, Pfister, Otmar, Pabst, Thomas, Stämpfli, S.F., Stirnimann, G., Dirnhofer, S., Mylonas, A., Andrea Cavalli, Violeta Mihaylova, Bode, Peter, Arosio, Paolo, Dobner, Stephan, René Nkoulou, Condoluci, Adalgisa, Garofalo, Maura, Rahel Schwotzer, Zweier, M., Mazzucchelli, L., Bacher, Ulrike, Otmar Pfister, Jung, Hans H, Schwotzer, R., Annemarie Hübers, Dobner, S., Meyer, M., Tzankov, Alexandar, Magini, Giulia, Cavalli, Andrea, Tzankov, Alexandar; https://orcid.org/, Robert Manka, Luca Mazzucchelli, Mylonas, Alessio, Heimgartner, Raphael, Gaspert, A., Aju P. Pazhenkottil, Seeger, H., Hans H. Jung, Paolo Arosio, Condoluci, A., Pabst, T., Maura Garofalo, Zweier, Markus; https://orcid.org/, Natallia Laptseva, Bernhard Gerber, Pfister, O., Treglia, G., Knöpfel, R., Raphael Heimgartner, Cavalli, A., Pazhenkottil, Aju P, Stephan Dobner, Nkoulou, R., Jung, H.H., Marie Théaudin   +136 more
core   +4 more sources

Evolution of transthyretin in marsupials [PDF]

European Journal of Biochemistry, 1995
The evolution of the expression and the structure of the gene for transthyretin, a thyroxine-binding plasma protein formerly called prealbumin, was studied in three marsupial species: the South American polyprotodont Monodelphis domestica, the Australian
Dziegielewska, KM (15476936), Richardson, SJ (15476918), Harms, PJ (15476930), Wettenhall, REH (15476933), Selwood, L (15476939), Brack, C (15476945), Schreiber, G (15476948), Heyes, RJ (15476924), Duan, W (15476915), Babon, JJ (15476921), Bradley, AJ (15476942), Southwell, BR (15476927)   +11 more
core   +7 more sources

The transthyretin cDNA sequence is normal in transthyretin-derived senile systemic amyloidosis [PDF]

FEBS Letters, 1991
A variety of mutations leading to amino acid substitutions have been described in the transthyretin gene in association with different familial amyloidoses and have been implicated to be involved in the pathogenesis of amyloid deposits.
Gustavsson, Å., Betsholtz, C., L. Christmanson, Johansson, B., Sletten, K., Westermark, P., B. Johansson, K. Sletten, Christmanson, L., C. Betsholtz, Å. Gustavsson, P. Westermark   +11 more
core   +3 more sources

Computational Studies on Transthyretin

Current Medicinal Chemistry, 2012
Among the 23 different fibril proteins described in human amyloidosis, transthyretin is associated with the most common hereditary form of the disease and its knowledge is corroborated through about 150 crystal structures in addition to thousands of ...
MARTINELLI, ADRIANO, ORTORE, GABRIELLA MARIA PIA   +1 more
core   +4 more sources

EGCG-Mediated Protection of Transthyretin Amyloidosis by Stabilizing Transthyretin Tetramers and Disrupting Transthyretin Aggregates

International Journal of Molecular Sciences, 2023
Transthyretin amyloidosis (ATTR) is a progressive and systemic disease caused by the misfolding and amyloid aggregation of transthyretin (TTR). Stabilizing the TTR tetramers and disrupting the formed TTR aggregation are treated as a promising strategy for the treatment of ATTR.
Huizhen Zou, Shuangyan Zhou
openaire   +2 more sources

Evaluation of the Current ATTR-CM Treatment Landscape via a Mathematical Model of TTR Dissociation and Amyloid Formation. [PDF]

CPT Pharmacometrics Syst Pharmacol
ABSTRACT Transthyretin amyloid cardiomyopathy (ATTR‐CM) is a progressive, often fatal disease arising from the dissociation of circulating transthyretin (TTR) tetramers into monomers that misfold and form amyloid fibrils that deposit in the myocardium and other tissues. Approved treatment paradigms involve tetramer stabilization with small molecules or
Methven Jeknić S, Ahn-Horst TA, Ji AX, Ju JH, Paull M, Ji SG, Sinha U.   +6 more
europepmc   +2 more sources

TNF receptor–related factor 3 inactivation promotes the development of intrahepatic cholangiocarcinoma through NF‐κB‐inducing kinase–mediated hepatocyte transdifferentiation

Hepatology, EarlyView., 2022
Abstract Background and Aims Intrahepatic cholangiocarcinoma (ICC) is a deadly but poorly understood disease, and its treatment options are very limited. The aim of this study was to identify the molecular drivers of ICC and search for therapeutic targets.
Yuto Shiode, Takahiro Kodama, Satoshi Shigeno, Kazuhiro Murai, Satoshi Tanaka, Justin Y. Newberg, Jumpei Kondo, Shogo Kobayashi, Ryoko Yamada, Hayato Hikita, Ryotaro Sakamori, Hiroshi Suemizu, Tomohide Tatsumi, Hidetoshi Eguchi, Nancy A. Jenkins, Neal G. Copeland, Tetsuo Takehara   +16 more
wiley   +1 more source

Proxy markers of serum retinol concentration, used alone and in combination, to assess population vitamin A status in Kenyan children: a cross-sectional study [PDF]

, 2015
Background Serum retinol concentration determined by high-performance liquid chromatography (HPLC) is recommended by the World Health Organization to assess population vitamin A status.
Inge D Brouwer, Verhoef, H., Elise F Talsma, Alida Melse-Boonstra, Brouwer, Inge D, Hulshof, Paul JM, Talsma, E.F., Anne S Mburu-de Wagt, Paul JM Hulshof, Hans Verhoef, Talsma, Elise F, Mburu-de Wagt, Anne S, Melse-Boonstra, Alida, Brouwer, I.D., Hulshof, P.J.M., Mburu-de Wagt, A.S., Verhoef, Hans, Boonstra, A.   +17 more
core   +1 more source

The negative acute phase response of serum transthyretin following Streptococcus suis infection in the pig [PDF]

, 2005
Peer ...
Eckersall, P D, Peter Mikael H. Heegaard,, Waterston, M, Andresen, L O, Eckersall, P.D., Eckersall, PD, Campbell, Fiona, Waterston, Mary, Campbell, F.M., Campbell, Fiona Margaret, Heegaard, PMH, Sorensen, Nanna, P. David Eckersall, Waterston, M., Lars Ole Andresen, Andresen, LO, Peter Mikael H. Heegaard, Campbell, FM, Mary Waterston, Andresen, Lars, Heegaard, P M H, Sørensen, Nanna Skall, David Eckersall, P., Sorensen, NS, Heegaard, Peter M. H., Sorensen, N S, Nanna Skall Sorensen, Andresen, Lars Ole, Fiona M. Campbell   +28 more
core   +1 more source

Evolutionary changes to transthyretin: evolution of transthyretin biosynthesis [PDF]

The FEBS Journal, 2009
Thyroid hormones are involved in growth and development, particularly of the brain. Thus, it is imperative that these hormones get from their site of synthesis to their sites of action throughout the body and the brain. This role is fulfilled by thyroid hormone distributor proteins.
openaire   +2 more sources