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Rosenberry, Terrone L.

https://orcid.org/0000-0003-3579-7681

Mayo Clinic

Mayo Clinic in Florida

Citations 30

Amyloid-β(1−42) Rapidly Forms Protofibrils and Oligomers by Distinct Pathways in Low Concentrations of Sodium Dodecylsulfate
Rangachari, Vijayaraghavan , Moore, Brenda D. , Reed, Dana Kim , Sonoda, Leilani K., Bridges, Alexander W., Conboy, Erin , Hartigan, David E. , Rosenberry, Terrone L.

Biochemistry | October 2, 2007 | Volume: 46 | Issue: 43 | Pages: 12451-12462

10.1021/bi701213s Get It

Insights into the mechanisms of action of anti‐Aβ antibodies in Alzheimer's disease mouse models
Levites, Yona , Smithson, Lisa, Price, Robert, Dakin, Rachel , Yuan, Bin , Kim, Jungsu , Reed, Dana Kim , Rosenberry, Terrone L. , Das, Pritam , Golde, Todd E. , Sierks, Michael R. , McGowan, Eileen , Kim, Jungsu

The FASEB Journal | October 26, 2006 | Volume: 20 | Issue: 14 | Pages: 2576-2578

10.1096/fj.06-6463fje Get It

A number of hypotheses regarding how anti‐Aβ antibodies alter amyloid deposition have been postulated, yet there is no consensus as to how Aβ immunotherapy works. We have examined the in vivo binding properties, pharmacokinetics, brain penetrance, and alterations in Aβ levels after a single peripheral dose of anti‐Aβ antibodies to both wild‐type (WT) and young non‐Aβ depositing APP and BRI‐Aβ42 mice. The rapid rise in plasma Aβ observed after antibody (Ab) administration is attributable to prolongation of the half‐life of Aβ bound to the Ab. Only a miniscule fraction of Ab enters the brain, and despite dramatic increases in plasma Aβ, we find no evidence that total brain Aβ levels are significantly altered. Surprisingly, cerebral spinal fluid Aβ levels transiently rise, and when Ab:Aβ complex is directly injected into the lateral ventricles of mice, it is rapidly cleared from the brain into the plasma where it remains stable. When viewed in context of daily turnover of Aβ, these data provide a framework to evaluate proposed mechanisms of Aβ attenuation mediated by peripheral administration of an anti‐Aβ monoclonal antibody (mAb) effective in passive immunization paradigm. Such quantitative data suggest that the mAbs are either indirectly enhancing clearance of Aβ or targeting a low abundance aggregation intermediate.—Levites, Y., Smithson, L. A., Price, R. W., Dakin. R. S., Yuan, B., Sierks, M. R., Kim, J., McGowan, E., Reed, D. K., Rosenberry, T. L., Das, P., Golde, T. E. Insights into the mechanisms of action of anti‐Aβ antibodies in Alzheimer's disease mouse models. FASEB J. 20, E2002–E2014 (2006)
Secondary Structure and Interfacial Aggregation of Amyloid-β(1−40) on Sodium Dodecyl Sulfate Micelles
Rangachari, Vijayaraghavan , Reed, Dana Kim , Moore, Brenda D. , Rosenberry, Terrone L.

Biochemistry | June 22, 2006 | Volume: 45 | Issue: 28 | Pages: 8639-8648

10.1021/bi060323t Get It

Rapid Assembly of Amyloid-β Peptide at a Liquid/Liquid Interface Produces Unstable β-Sheet Fibers
Nichols, Michael R. , Moss, Melissa A. , Reed, Dana Kim , Hoh, Jan H. , Rosenberry, Terrone L.

Biochemistry | January 4, 2005 | Volume: 44 | Issue: 1 | Pages: 165-173

10.1021/bi048846t Get It

Unmasking Tandem Site Interaction in Human Acetylcholinesterase. Substrate Activation with a Cationic Acetanilide Substrate
Johnson, Joseph L., Cusack, Bernadette, Davies, Matthew , Fauq, Abdul H. , Rosenberry, Terrone L.

Biochemistry | May 6, 2003 | Volume: 42 | Issue: 18 | Pages: 5438-5452

10.1021/bi027065u Get It

Growth of β-Amyloid(1−40) Protofibrils by Monomer Elongation and Lateral Association. Characterization of Distinct Products by Light Scattering and Atomic Force Microscopy
Nichols, Michael R. , Moss, Melissa A. , Reed, Dana Kim , Lin, Wen-Lang, Mukhopadhyay, Rajendrani, Hoh, Jan H. , Rosenberry, Terrone L.

Biochemistry | July 26, 2002 | Volume: 41 | Issue: 19 | Pages: 6115-6127

10.1021/bi015985r Get It

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

Biochemistry | July 26, 2002 | Volume: 39 | Issue: 26 | Pages: 7753-7763

10.1021/bi000210o Get It

Substrate Binding to the Peripheral Site of Acetylcholinesterase Initiates Enzymatic Catalysis. Substrate Inhibition Arises as a Secondary Effect
Szegletes, T., Mallender, William D. , Thomas, Patrick J., Rosenberry, Terrone L.

Biochemistry | July 26, 2002 | Volume: 38 | Issue: 1 | Pages: 122-133

10.1021/bi9813577 Get It

Nonequilibrium Analysis Alters the Mechanistic Interpretation of Inhibition of Acetylcholinesterase by Peripheral Site Ligands
Szegletes, T., Mallender, William D. , Rosenberry, Terrone L.

Biochemistry | July 26, 2002 | Volume: 37 | Issue: 12 | Pages: 4206-4216

10.1021/bi972158a Get It

Short, Strong Hydrogen Bonds at the Active Site of Human Acetylcholinesterase:  Proton NMR Studies
Massiah, Michael A., Viragh, C., Reddy, Putta Mallikarjuna, Kovach, Ildiko M., Johnson, Joseph L., Rosenberry, Terrone L. , Mildvan, Albert S.

Biochemistry | July 26, 2002 | Volume: 40 | Issue: 19 | Pages: 5682-5690

10.1021/bi010243j Get It