H-GSPAINVAMHVFR^-OH

Ref. 3D-PP42175

Información del producto

• Nombre: H-GSPAINVAMHVFR^-OH

Descripción

Peptide H-GSPAINVAMHVFR^-OH is a Research Peptide with significant interest within the field academic and medical research. This peptide is available for purchase at Cymit Quimica in multiple sizes and with a specification of your choice. Recent citations using H-GSPAINVAMHVFR^-OH include the following: Quantitative analysis of post-translational modifications in human serum transthyretin associated with familial amyloidotic polyneuropathy by targeted LC-MS and M Vilaca -Rico, N Colome-Calls, L Martaca­n-Castel - Journal of , 2015 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S1874391915001979 Effect of age and sex differences on wild-type transthyretin amyloid formation in familial amyloidotic polyneuropathy: a proteomic approach M Tasaki, M Ueda , K Obayashi, H Koike - International journal of , 2013 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S0167527313018470 Generation of familial amyloidotic polyneuropathy-specific induced pluripotent stem cells K Isono, H Jono, Y Ohya, N Shiraki, T Yamazoe - Stem cell , 2014 - Elsevierhttps://www.sciencedirect.com/science/article/pii/S1873506114000075 Beyond genetic factors in familial amyloidotic polyneuropathy: protein glycation and the loss of fibrinogen's chaperone activity G da Costa, RA Gomes , A Guerreiro , aca‰ Mateus - PloS one, 2011 - journals.plos.orghttps://journals.plos.org/plosone/article?id=10.1371/journal.pone.0024850 Identification and quantitative analysis of human transthyretin variants in human serum by Fourier transform ion-cyclotron resonance mass spectrometry G Da Costa, R Gomes , CF Correia , A Freire, E Monteiro - Amyloid, 2009 - Taylor & Francishttps://www.tandfonline.com/doi/abs/10.3109/13506120903421561 Transthyretin amyloidosis: chaperone concentration changes and increased proteolysis in the pathway to disease G da Costa, C Ribeiro-Silva, R Ribeiro, S Gilberto - PLoS , 2015 - journals.plos.orghttps://journals.plos.org/plosone/article?id=10.1371/journal.pone.0125392 A non-invasive method based on saliva to characterize transthyretin in familial amyloidotic polyneuropathy patients using FT-ICR high-resolution MS G da Costa, A Guerreiro, CF Correia - PROTEOMICS , 2010 - Wiley Online Libraryhttps://onlinelibrary.wiley.com/doi/abs/10.1002/prca.200900118 A non-invasive method based on saliva to characterize TTR in FAP patients using FT-ICR high-resolution mass spectrometry G da Costa, A Guerreiro , CF Correia , RJ Gomes - 2010 - academia.eduhttps://www.academia.edu/download/45022046/a-non-invasive-method-based-on-saliva-to-characterize-ttr-in-fap-patients.pdf Characterization of a transthyretin-related amyloid fibril protein from cerebral amyloid angiopathy in type I familial amyloid polyneuropathy F Kametani, S Ikeda, N Yanagisawa, T Ishi - Journal of the , 1992 - Elsevierhttps://www.sciencedirect.com/science/article/pii/0022510X9290048P The relative amounts of plasma transthyretin forms in familial transthyretin amyloidosis: a quantitative analysis by Fourier transform ion-cyclotron resonance mass C Ribeiro-Silva, S Gilberto, RA Gomes , aca‰ Mateus - Amyloid, 2011 - Taylor & Francishttps://www.tandfonline.com/doi/abs/10.3109/13506129.2011.614295 Gene therapy approach to FAP: in vivo influence of T119M in TTR deposition in a transgenic V30M mouse model AR Batista, D Gianni, M Ventosa, AV Coelho - Gene therapy, 2014 - nature.comhttps://www.nature.com/articles/gt201486 Steady turnover of amyloid fibril proteins in gastric mucosa after liver transplantation in familial amyloid polyneuropathy A Tsuchiya-Suzuki, M Yazaki, Y Sekijima, F Kametani - Amyloid, 2013 - Taylor & Francishttps://www.tandfonline.com/doi/abs/10.3109/13506129.2013.807790

• Marca: Biosynth