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550 results on '"Beckman, Joseph S."'

151. CuII(atsm) improves the neurological phenotype and survival of SOD1G93A mice and selectively increases enzymatically active SOD1 in the spinal cord

Author

Hilton, James B., primary, Mercer, Stephen W., additional, Lim, Nastasia K. H., additional, Faux, Noel G., additional, Buncic, Gojko, additional, Beckman, Joseph S., additional, Roberts, Blaine R., additional, Donnelly, Paul S., additional, White, Anthony R., additional, and Crouch, Peter J., additional

Published
2017
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153. Direct Determination of Antibody Chain Pairing by Top-down and Middle-down Mass Spectrometry Using Electron Capture Dissociation and Ultraviolet Photodissociation

Author

Shaw, Jared B., Liu, Weijing, Vasil′ev, Yury V., Bracken, Carter C., Malhan, Neha, Guthals, Adrian, Beckman, Joseph S., and Voinov, Valery G.

Abstract

One challenge associated with the discovery and development of monoclonal antibody (mAb) therapeutics is the determination of heavy chain and light chain pairing. Advances in MS instrumentation and MS/MS methods have greatly enhanced capabilities for the analysis of large intact proteins yielding much more detailed and accurate proteoform characterization. Consequently, direct interrogation of intact antibodies or F(ab′)2 and Fab fragments has the potential to significantly streamline therapeutic mAb discovery processes. Here, we demonstrate for the first time the ability to efficiently cleave disulfide bonds linking heavy and light chains of mAbs using electron capture dissociation (ECD) and 157 nm ultraviolet photodissociation (UVPD). The combination of intact mAb, Fab, or F(ab′)2 mass, intact LC and Fd masses, and CDR3 sequence coverage enabled determination of heavy chain and light chain pairing from a single experiment and experimental condition. These results demonstrate the potential of top-down and middle-down proteomics to significantly streamline therapeutic antibody discovery.

Published
2020
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155. Infrared absorption of cis- and trans-alkali-metal peroxynitrites (MOONO, M=Li, Na, and K) in solid argon.

Author

Lo, Wen-Jui, Lee, Yuan-Pern, Tsai, Jyh-Hsin M., Tsai, Hui-Hsu, Hamilton, Tracy P., Harrison, Joseph G., and Beckman, Joseph S.

Subjects
ABSORPTION, ARGON, NITRITES, CONFORMAL invariants
Abstract

Potassium nitrate (KNO3) isolated in solid argon at 13 K was irradiated with emission from an ArF excimer laser at 193 nm. Recombination of the photofragments led to formation of both cis- and trans-potassium peroxynitrites (KOONO). The cyclic conformer, cis-KOONO, absorbs at 1444.5, 952.3, 831.6, and 749.1 cm-1, whereas trans-KOONO absorbs at 1528.4, 987.4, and 602.2 cm-1. The assignments are based on observed 18O- and 15N-isotopic shifts and comparison with similar compounds, cis–cis and trans–perp HOONO. Ab initio calculations using density functional theory at a Becke3LYP level predicted similar line positions and isotopic shifts for both conformers. Photoconversion among these three isomers was achieved at various wavelengths and periods of irradiation; cis-KOONO was photolyzed readily at 308 nm, whereas trans-KOONO increased slightly in intensity initially and was eventually transformed to KNO3 on prolonged irradiation. Similar results were obtained for LiNO3 and NaNO3; cis-LiOONO and cis-NaOONO absorb at (1423.4, 1422.0), 966.2, 874.2, 792.3 cm-1 and (1437.4, 1434.6), 961.4, 840.7, (770.9, 768.7) cm-1, respectively, whereas trans-LiOONO and trans-NaOONO absorb at (1581.6, 1580.4), (998.3, 995.6), 600.4 cm-1 and (1549.3, 1540.6), (996.3, 994.1), (609.4, 607.4) cm-1, respectively; the numbers in parentheses are due to line splitting. © 1995 American Institute of Physics. [ABSTRACT FROM AUTHOR]

Published
1995
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156. Evidence for peroxynitrite as a signaling molecule in flow-dependent activation of c-Jun [NH.sub.2]-terminal kinase

Author

GO, YOUNG-MI, PATEL, RAKESH P., MALAND, MATTHEW C., PARK, HEONYONG, BECKMAN, JOSEPH S., DARLEY-USMAR, VICTOR M., and JO, HANJOONG

Subjects
Superoxide dismutase -- Research, Protein kinases -- Research, Nitric oxide -- Research, Biological sciences
Abstract

Go, Young-Mi, Rakesh P. Patel, Matthew C. Maland, Heonyong Park, Joseph S. Beckman, Victor M. Darley-Usmar, and Hanjoong Jo. Evidence for peroxynitrite as a signaling molecule in flow-dependent activation of c-Jun [NH.sub.2]-terminal kinase. Am. J. Physiol. 277 (Heart Circ. Physiol. 46): H1647-H1653, 1999.--The c-Jun [NH.sub.2]-terminal kinase (JNK), also known as stress-activated protein kinase, is a mitogen-activated protein kinase that determines cell survival in response to environmental stress. Activation of JNK involves redox-sensitive mechanisms and physiological stimuli such as shear stress, the dragging force generated by blood flow over the endothelium. Laminar shear stress has antiatherogenic properties and controls structure and function of endothelial cells by mechanisms including production of nitric oxide (NO) and superoxide ([MATHEMATICAL EXPRESSION NOT REPRODUCIBLE IN ASCII]). Here we show that both NO and [MATHEMATICAL EXPRESSION NOT REPRODUCIBLE IN ASCII] are required for activation of JNK by shear stress in endothelial cells. The present study also demonstrates that exposure of endothelial cells to shear stress increases tyrosine nitration, a marker of reactive nitrogen species formation. Furthermore, inhibitors or scavengers of NO, [MATHEMATICAL EXPRESSION NOT REPRODUCIBLE IN ASCII], or reactive nitrogen species prevented shear-dependent increase in tyrosine nitration and activation of JNK. Peroxynitrite alone, added to cells as a bolus or generated over 60 min by 3-morpholinosydnonimine, also activates JNK. These results suggest that reactive nitrogen species, in this case most likely peroxynitrite, act as signaling molecules in the mechanoactivation of JNK. nitric oxide synthase; NAD(P)H oxidase; superoxide dismutase; manganese(III)tetrakis (4-benzoic acid) porphyrin

Published
1999

159. Post-paralysis tyrosine kinase inhibition with masitinib abrogates neuroinflammation and slows disease progression in inherited amyotrophic lateral sclerosis

Author

Trias, Emiliano, primary, Ibarburu, Sofía, additional, Barreto-Núñez, Romina, additional, Babdor, Joël, additional, Maciel, Thiago T., additional, Guillo, Matthias, additional, Gros, Laurent, additional, Dubreuil, Patrice, additional, Díaz-Amarilla, Pablo, additional, Cassina, Patricia, additional, Martínez-Palma, Laura, additional, Moura, Ivan C., additional, Beckman, Joseph S., additional, Hermine, Olivier, additional, and Barbeito, Luis, additional

Published
2016
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160. Copper delivery to the CNS by CuATSM effectively treats motor neuron disease in SODG93A mice co-expressing the Copper-Chaperone-for-SOD

Author

Williams, Jared R., primary, Trias, Emiliano, additional, Beilby, Pamela R., additional, Lopez, Nathan I., additional, Labut, Edwin M., additional, Bradford, C. Samuel, additional, Roberts, Blaine R., additional, McAllum, Erin J., additional, Crouch, Peter J., additional, Rhoads, Timothy W., additional, Pereira, Cliff, additional, Son, Marjatta, additional, Elliott, Jeffrey L., additional, Franco, Maria Clara, additional, Estévez, Alvaro G., additional, Barbeito, Luis, additional, and Beckman, Joseph S., additional

Published
2016
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162. Focal Transplantation of Aberrant Glial Cells Carrying the SOD1G93A Mutation into Rat Spinal Cord Induces Extensive Gliosis.

Author

Ibarburu, Sofía, Trias, Emiliano, Lago, Natalia, Peluffo, Hugo, Barreto-Núñez, Romina, Varela, Valentina, Beckman, Joseph S., and Barbeito, Luis

Abstract

Objective: We aimed to determine the potential of aberrant glial cells (AbAs) isolated from the spinal cord of adult SOD1G93A symptomatic rats to induce gliosis and neuronal damage following focal transplantation into the lumbar spinal cord of wild-type rats. Methods: AbAs were obtained from the spinal cords of SOD1G93A symptomatic rats. One hundred thousand cells were injected using a glass micropipette into the lumbar spinal cords (L3-L5) of syngeneic wildtype adult rats. Equal volumes of culture medium or wildtype neonatal microglia were used as controls. Seven days after transplantation, immunohistochemistry analysis was carried out using astrocytic and microglia cell markers. Transplanted SOD1G93A AbAs were recognized by specific antibodies to human SOD1 (hSOD1) or misfolded human SOD1. Results: Seven days after transplantation, AbAs were mainly detected in the medial region of the lumbar ventral horn as a well-limited cell cluster formed at the site of injection by their immunoreactivity to either misfolded SOD1 or normally folded hSOD1. Compared with controls, transplanted AbAs were surrounded by marked microgliosis and reactive astrocytes. Marked microgliosis was observed to extend bilaterally up to the cervical cord. Motor neurons close to AbA transplants were surrounded by activated glial cells and displayed ubiquitin aggregation. Conclusions: AbAs bearing mutant SOD1G93A have the potential to induce neuroinflammation along the spinal cord and incipient damage to the motor neurons. The emergence of AbAs during amyotrophic lateral sclerosis pathogenesis may therefore be a mechanism to boost neuroinflammation and spread motor neuron damage along the neuroaxis. [ABSTRACT FROM AUTHOR]

Published
2017
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177. Ischaemic injury mediator

Author

Beckman, Joseph S.

Subjects
Ischemia -- Drug therapy, Superoxide dismutase -- Health aspects, Environmental issues, Science and technology, Zoology and wildlife conservation
Published
1990

182. Prevention of Peroxynitrite-induced Apoptosis of Motor Neurons and PC12 Cells by Tyrosine-containing Peptides

Author

Ye, Yaozu, primary, Quijano, Celia, additional, Robinson, Kristine M., additional, Ricart, Karina C., additional, Strayer, Amy L., additional, Garner, Mary Anne, additional, Shacka, John J., additional, Kirk, Marion, additional, Barnes, Stephen, additional, Accavitti-Loper, Mary Ann, additional, Radi, Rafael, additional, Beckman, Joseph S., additional, and Estévez, Alvaro G., additional

Published
2007
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199. Superoxide dismutase and the death of motoneurons in ALS. (Review)

Author

Beckman, Joseph S., Estevez, Alvaro G., Crow, John P., and Barbeito, Luis

Subjects
Superoxide dismutase -- Research, Motor neurons -- Evaluation, Amyotrophic lateral sclerosis -- Research, Diseases -- Causes and theories of causation, Health, Psychology and mental health
Abstract

Amyotrophic lateral sclerosis (ALS) is a lethal disease that is characterized by the relentless death of motoneurons. Mutations to Cu-Zn superoxide dismutase (SOD), though occurring in just 2-3% of individuals with ALS, remain the only proven cause of the disease. These mutations structurally weaken SOD, which indirectly decreases its affinity for Zn. Zn-deficient SOD induces apoptosis in motoneurons through a mechanism involving peroxynitrite. Importantly, Zn-deficient wild-type SOD is just as toxic as Zn-deficient ALS mutant SOD, suggesting that the loss of Zn from wild-type SOD could be involved in the other 98% of cases of ALS. Zn-deficient SOD could therefore be an important therapeutic target in all forms of ALS.

Published
2001

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