Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Sepehr Haerianardakani"'
Autor:
Adam G. Kreutzer, Chelsea Marie T. Parrocha, Sepehr Haerianardakani, Gretchen Guaglianone, Jennifer T. Nguyen, Michelle N. Diab, William Yong, Mari Perez-Rosendahl, Elizabeth Head, James S. Nowick
Publikováno v:
ACS Central Science, Vol 10, Iss 1, Pp 104-121 (2023)
Externí odkaz:
https://doaj.org/article/098b29bada2f49a389917a993817e744
Autor:
Sabyasachi Maity, Samal Nauhria, Narendra Nayak, Shreya Nauhria, Tamara Coffin, Jadzia Wray, Sepehr Haerianardakani, Ramsagar Sah, Andrew Spruce, Yujin Jeong, Mary C. Maj, Abhimanyu Sharma, Nicole Okpara, Chidubem J. Ike, Reetuparna Nath, Jack Nelson, Anil V. Parwani
Publikováno v:
Diagnostics, Vol 13, Iss 3, p 558 (2023)
Background: The usage of whole-slide images has recently been gaining a foothold in medical education, training, and diagnosis. Objectives: The first objective of the current study was to compare academic performance on virtual microscopy (VM) and li
Externí odkaz:
https://doaj.org/article/ce340799bd8b4f0a9f83b59062e15e02
Autor:
Adam G. Kreutzer, Tuan D. Samdin, Sepehr Haerianardakani, James S. Nowick, Patrick J. Salveson, Gretchen Guaglianone
Publikováno v:
J Am Chem Soc
Oligomers of the β-amyloid peptide, Aβ, play a central role in the pathogenesis and progression of Alzheimer’s disease. Trimers and higher-order oligomers composed of trimers are thought to be the most neurotoxic Aβ oligomers. To gain insights i
Autor:
Stan Yoo, Adam G. Kreutzer, Patrick J. Salveson, Alexander Thuy-Boun, Borries Demeler, Sepehr Haerianardakani, James S. Nowick
Publikováno v:
J Am Chem Soc
Soluble oligomers of the β-amyloid peptide, Aβ, are associated with the progression of Alzheimer’s disease. Although many small molecules bind to these assemblies, the details of how these molecules interact with Aβ oligomers remain unknown. Thi
Autor:
Adam G. Kreutzer, James S. Nowick, Alexander Thuy-Boun, Patrick J. Salveson, Sepehr Haerianardakani
Publikováno v:
Journal of the American Chemical Society. 140(17)
A key challenge in studying the biological and biophysical properties of amyloid-forming peptides is that they assemble to form heterogeneous mixtures of soluble oligomers and insoluble fibrils. Photolabile protecting groups have emerged as tools to
Autor:
Stan Yoo, Sepehr Haerianardakani, Borries Demeler, Adam G. Kreutzer, Patrick J. Salveson, James S. Nowick, Alexander Thuy-Boun
Publikováno v:
Journal of the American Chemical Society. 140:15546-15546