Comparison of the Binding of Reversible Inhibitors to Human Butyrylcholinesterase and Acetylcholinesterase: A Crystallographic, Kinetic and Calorimetric Study von Rosenberry, Terrone L, Brazzolotto, Xavier, Macdonald, Ian R, Wandhammer, Marielle, Trovaslet-Leroy, Marie, Darvesh, Sultan, Nachon, Florian

Volltext

Solvent Deuterium Oxide Isotope Effects on the Reactions of Organophosphorylated Acetylcholinesterase von Rosenberry, Terrone L

Volltext

Structures of Human Acetylcholinesterase Bound to Dihydrotanshinone I and Territrem B Show Peripheral Site Flexibility von Cheung, Jonah, Gary, Ebony N, Shiomi, Kazuro, Rosenberry, Terrone L

Volltext

A Second Look at the Crystal Structures of Drosophila melanogaster Acetylcholinesterase in Complex with Tacrine Derivatives Provides Insights Concerning Catalytic Intermediates and... von Nachon, Florian, Rosenberry, Terrone L, Silman, Israel, Sussman, Joel L

Volltext

Oligomer Formation by Amyloid-β42 in a Membrane-Mimicking Environment in Alzheimer's Disease von Rosenberry, Terrone L, Zhou, Huan-Xiang, Stagg, Scott M, Paravastu, Anant K

Volltext

Opposing roles of the triggering receptor expressed on myeloid cells 2 and triggering receptor expressed on myeloid cells-like transcript 2 in microglia activation von Zheng, Honghua, Liu, Chia-Chen, Atagi, Yuka, Chen, Xiao-Fen, Jia, Lin, Yang, Longyu, He, Wencan, Zhang, Xilin, Kang, Silvia S., Rosenberry, Terrone L., Fryer, John D., Zhang, Yun-Wu, Xu, Huaxi, Bu, Guojun

Volltext

Accumulation of Pathological Tau Species and Memory Loss in a Conditional Model of Tauopathy von Berger, Zdenek, Roder, Hanno, Hanna, Amanda, Carlson, Aaron, Rangachari, Vijayaraghavan, Yue, Mei, Wszolek, Zbigniew, Ashe, Karen, Knight, Joshua, Dickson, Dennis, Andorfer, Cathy, Rosenberry, Terrone L, Lewis, Jada, Hutton, Mike, Janus, Christopher

Volltext

Cathepsin D regulates cerebral Aβ42/40 ratios via differential degradation of Aβ42 and Aβ40 von Suire, Caitlin N., Abdul-Hay, Samer O., Sahara, Tomoko, Kang, Dongcheul, Brizuela, Monica K., Saftig, Paul, Dickson, Dennis W., Rosenberry, Terrone L., Leissring, Malcolm A.

Volltext

Distinct spatiotemporal accumulation of N-truncated and full-length amyloid-β42 in Alzheimer's disease von Shinohara, Mitsuru, Koga, Shunsuke, Konno, Takuya, Nix, Jeremy, Shinohara, Motoko, Aoki, Naoya, Das, Pritam, Parisi, Joseph E, Petersen, Ronald C, Rosenberry, Terrone L, Dickson, Dennis W, Bu, Guojun

Volltext

Acetylcholinesterase: From 3D structure to function von Dvir, Hay, Silman, Israel, Harel, Michal, Rosenberry, Terrone L., Sussman, Joel L.

Volltext

A common pathway for detergent-assisted oligomerization of Aβ42 von Muhammedkutty, Fidha Nazreen Kunnath, Prasad, Ramesh, Gao, Yuan, Sudarshan, Tarunya Rao, Robang, Alicia S., Watzlawik, Jens O., Rosenberry, Terrone L., Paravastu, Anant K., Zhou, Huan-Xiang

Volltext

The Alzheimer's Amyloid-β(1–42) Peptide Forms Off-Pathway Oligomers and Fibrils That Are Distinguished Structurally by Intermolecular Organization von Tay, William M., Huang, Danting, Rosenberry, Terrone L., Paravastu, Anant K.

Volltext

Rate-limiting step in the decarbamoylation of acetylcholinesterases with large carbamoyl groups von Rosenberry, Terrone L., Cheung, Jonah

Volltext

Probing the Peripheral Site of Human Butyrylcholinesterase von Macdonald, Ian R, Martin, Earl, Rosenberry, Terrone L, Darvesh, Sultan

Volltext

VEGF receptor‐1 modulates amyloid β 1–42 oligomer‐induced senescence in brain endothelial cells von Angom, Ramcharan Singh, Wang, Ying, Wang, Enfeng, Pal, Krishnendu, Bhattacharya, Santanu, Watzlawik, Jens O., Rosenberry, Terrone L., Das, Pritam, Mukhopadhyay, Debabrata

Volltext

Antiparallel β-Sheet Structure within the C-Terminal Region of 42-Residue Alzheimer's Amyloid-β Peptides When They Form 150-kDa Oligomers von Huang, Danting, Zimmerman, Maxwell I., Martin, Patricia K., Nix, A.Jeremy, Rosenberry, Terrone L., Paravastu, Anant K.

Volltext

Out-of-Register Parallel β-Sheets and Antiparallel β-Sheets Coexist in 150-kDa Oligomers Formed by Amyloid-β(1–42) von Gao, Yuan, Guo, Cong, Watzlawik, Jens O., Randolph, Peter S., Lee, Elizabeth J., Huang, Danting, Stagg, Scott M., Zhou, Huan-Xiang, Rosenberry, Terrone L., Paravastu, Anant K.

Volltext

Acetylthiocholine Binds to Asp74 at the Peripheral Site of Human Acetylcholinesterase as the First Step in the Catalytic Pathway von Mallender, William D, Szegletes, Tivadar, Rosenberry, Terrone L

Volltext

Decarbamoylation of acetylcholinesterases is markedly slowed as carbamoyl groups increase in size von Venkatasubban, Kunisi S., Johnson, Joseph L., Thomas, Jamie L., Fauq, Abdul, Cusack, Bernadette, Rosenberry, Terrone L.

Volltext

Crystal Structure of Thioflavin T Bound to the Peripheral Site of Torpedo californica Acetylcholinesterase Reveals How Thioflavin T Acts as a Sensitive Fluorescent Reporter of Liga... von Harel, Michal, Sonoda, Leilani K, Silman, Israel, Sussman, Joel L, Rosenberry, Terrone L

Volltext