Heterogeneous elastic response of human lung microvascular endothelial cells to barrier modulating stimuli von Arce, Fernando Terán, PhD, Meckes, Brian, BS, Camp, Sara M., BA, Garcia, Joe G.N., MD, Dudek, Steven M., MD, Lal, Ratnesh, PhD

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Antimicrobial Properties of Amyloid Peptides von Kagan, Bruce L, Jang, Hyunbum, Capone, Ricardo, Teran Arce, Fernando, Ramachandran, Srinivasan, Lal, Ratnesh, Nussinov, Ruth

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Polymorphism of amyloid β peptide in different environments: implications for membrane insertion and pore formation von Arce, Fernando Terán, Jang, Hyunbum, Ramachandran, Srinivasan, Landon, Preston B, Nussinov, Ruth, Lal, Ratnesh

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Nanoscale Structural and Mechanical Properties of Nontypeable Haemophilus influenzae Biofilms von TERAN ARCE, Fernando, CARLSON, Ross, MONDS, James, VEEH, Richard, HU, Fen Z, STEWART, Philip S, LAL, Ratnesh, EHRLICH, Garth D, AVCI, Recep

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Nanomechanics of Hemichannel Conformations: CONNEXIN FLEXIBILITY UNDERLYING CHANNEL OPENING AND CLOSING von Liu, Fei, Arce, Fernando Terán, Ramachandran, Srinivasan, Lal, Ratnesh

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Regulation of the Micromechanical Properties of Pulmonary Endothelium by S1P and Thrombin: Role of Cortactin von Arce, Fernando Terán, Whitlock, Jenny L., Birukova, Anna A., Birukov, Konstantin G., Arnsdorf, Morton F., Lal, Ratnesh, Garcia, Joe G.N., Dudek, Steven M.

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Disordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs von Jang, Hyunbum, Teran Arce, Fernando, Ramachandran, Srinivasan, Kagan, Bruce L, Lal, Ratnesh, Nussinov, Ruth

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Antimicrobial Protegrin-1 Forms Amyloid-Like Fibrils with Rapid Kinetics Suggesting a Functional Link von Jang, Hyunbum, Arce, Fernando Teran, Mustata, Mirela, Ramachandran, Srinivasan, Capone, Ricardo, Nussinov, Ruth, Lal, Ratnesh

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Mechanisms for the Insertion of Toxic, Fibril-like β‑Amyloid Oligomers into the Membrane von Jang, Hyunbum, Connelly, Laura, Teran Arce, Fernando, Ramachandran, Srinivasan, Kagan, Bruce L, Lal, Ratnesh, Nussinov, Ruth

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A Live Bioprobe for Studying Diatom-Surface Interactions von Arce, Fernando Terán, Avci, Recep, Beech, Iwona B., Cooksey, Keith E., Wigglesworth-Cooksey, Barbara

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Truncated β-amyloid peptide channels provide an alternative mechanism for Alzheimer's Disease and Down syndrome von Jang, Hyunbum, Arce, Fernando Teran, Ramachandran, Srinivasan, Capone, Ricardo, Azimova, Rushana, Kagan, Bruce L, Nussinov, Ruth, Lal, Ratnesh

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Potential role of atomic force microscopy in systems biology von Ramachandran, Srinivasan, Teran Arce, Fernando, Lal, Ratnesh

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Atomic Force Microscopy and MD Simulations Reveal Pore-Like Structures of All-d-Enantiomer of Alzheimer’s β-Amyloid Peptide: Relevance to the Ion Channel Mechanism of AD Pathology... von Connelly, Laura, Jang, Hyunbum, Teran Arce, Fernando, Capone, Ricardo, Kotler, Samuel A, Ramachandran, Srinivasan, Kagan, Bruce L, Nussinov, Ruth, Lal, Ratnesh

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Structural Convergence Among Diverse, Toxic β-Sheet Ion Channels von Jang, Hyunbum, Teran Arce, Fernando, Ramachandran, Srinivasan, Capone, Ricardo, Lal, Ratnesh, Nussinov, Ruth

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Activity and Architecture of Pyroglutamate-Modified Amyloid‑β (AβpE3‑42) Pores von Gillman, Alan L, Jang, Hyunbum, Lee, Joon, Ramachandran, Srinivasan, Kagan, Bruce L, Nussinov, Ruth, Teran Arce, Fernando

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Role of the Fast Kinetics of Pyroglutamate-Modified Amyloid‑β Oligomers in Membrane Binding and Membrane Permeability von Lee, Joon, Gillman, Alan L, Jang, Hyunbum, Ramachandran, Srinivasan, Kagan, Bruce L, Nussinov, Ruth, Teran Arce, Fernando

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Effects of Point Substitutions on the Structure of Toxic Alzheimer’s β-Amyloid Channels: Atomic Force Microscopy and Molecular Dynamics Simulations von Connelly, Laura, Jang, Hyunbum, Teran Arce, Fernando, Ramachandran, Srinivasan, Kagan, Bruce L, Nussinov, Ruth, Lal, Ratnesh

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Familial Alzheimer’s Disease Osaka Mutant (ΔE22) β‑Barrels Suggest an Explanation for the Different Aβ1–40/42 Preferred Conformational States Observed by Experiment von Jang, Hyunbum, Teran Arce, Fernando, Ramachandran, Srinivasan, Kagan, Bruce L, Lal, Ratnesh, Nussinov, Ruth

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The diphenylpyrazole compound anle138b blocks Aβ channels and rescues disease phenotypes in a mouse model for amyloid pathology von Martinez Hernandez, Ana, Urbanke, Hendrik, Gillman, Alan L, Lee, Joon, Ryazanov, Sergey, Agbemenyah, Hope Y, Benito, Eva, Jain, Gaurav, Kaurani, Lalit, Grigorian, Gayane, Leonov, Andrei, Rezaei‐Ghaleh, Nasrollah, Wilken, Petra, Arce, Fernando Teran, Wagner, Jens, Fuhrmann, Martin, Caruana, Mario, Camilleri, Angelique, Vassallo, Neville, Zweckstetter, Markus, Benz, Roland, Giese, Armin, Schneider, Anja, Korte, Martin, Lal, Ratnesh, Griesinger, Christian, Eichele, Gregor, Fischer, Andre

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K3 Fragment of Amyloidogenic β2-Microglobulin Forms Ion Channels: Implication for Dialysis Related Amyloidosis von Mustata, Mirela, Capone, Ricardo, Jang, Hyunbum, Arce, Fernando Teran, Ramachandran, Srinivasan, Lal, Ratnesh, Nussinov, Ruth

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