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Minerva Cardioangiologica|December 15, 2006
Papillary fibroelastoma of the ascending aorta presenting with cardiogenic shockO Coskun, T Coskun, L Arusoglu, et al.
Chinese Medical Journal|January 5, 2002
Mutation in the leucine-rich repeat of platelet glycoprotein Ib alpha results in defects in its interaction with immobilized von Willebrand factor under flowJ Dong, C Li, A J Schade, et al.
Archives of Dermatology|August 1, 1985
Characterization of the humoral immune response to bovine collagen implantsJ P McCoy, W J Schade, R J Siegle, et al.
The Journal of Biological Chemistry|June 6, 2000
Novel gain-of-function mutations of platelet glycoprotein IBalpha by valine mutagenesis in the Cys209-Cys248 disulfide loop. Functional analysis under statis and dynamic conditionsJ Dong, A J Schade, G M Romo, et al.
The Journal of Biological Chemistry|March 30, 2001
Tyrosine sulfation of glycoprotein I(b)alpha. Role of electrostatic interactions in von Willebrand factor bindingJ Dong, P Ye, A J Schade, et al.
Biochemistry|February 20, 2003
Cytoplasmic truncation of glycoprotein Ib alpha weakens its interaction with von Willebrand factor and impairs cell adhesionAlicia J Schade, Maneesh Arya, Shan Gao, et al.
Osteoporosis International : a Journal Established As Result of Cooperation Between the European Foundation for Osteoporosis and the National Osteoporosis Foundation of the USA|December 21, 2017
Vitamin D supplementation and bone turnover in advanced heart failure: the EVITA trialA Zittermann, J B Ernst, S Prokop, et al.
Herz|January 24, 2014
[Heart and combined heart-lung transplantation. Indications, chances and risks]T Puehler, S Ensminger, U Schulz, et al.
Biochemistry|March 22, 2000
Necessity of conserved asparagine residues in the leucine-rich repeats of platelet glycoprotein Ib alpha for the proper conformation and function of the ligand-binding regionV Afshar-Kharghan, G Gineys, A J Schade, et al.
Proceedings of the National Academy of Sciences of the United States of America|July 5, 2001
The human formin-binding protein 17 (FBP17) interacts with sorting nexin, SNX2, and is an MLL-fusion partner in acute myelogeneous leukemiaU Fuchs, G Rehkamp, O A Haas, et al.
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