Open Access. Powered by Scholars. Published by Universities.®
Biochemistry, Biophysics, and Structural Biology Commons™
Open Access. Powered by Scholars. Published by Universities.®
- Institution
- Keyword
-
- Animals (1)
- B cell (1)
- B lymphoma cells (1)
- Bioremediation (1)
- Cell Differentiation (1)
-
- Cell Line, Tumor (1)
- Desulfovibrio (1)
- Down-Regulation (1)
- Early Growth Response Protein 1 (1)
- Egr-1 (1)
- Extracellular Signal-Regulated MAP Kinases (1)
- Female (1)
- Growth Inhibitors (1)
- JNK Mitogen-Activated Protein Kinases (1)
- Lymphoma, B-Cell (1)
- MAP Kinase Signaling System (1)
- MAPKs (1)
- Metal reduction (1)
- Mice (1)
- Mice, Inbred BALB C (1)
- Mice, Inbred CBA (1)
- Oligonucleotides, Antisense (1)
- P38 Mitogen-Activated Protein Kinases (1)
- Receptors, Antigen, B-Cell (1)
- Retroviridae (1)
- Tetraheme cytochrome c 3 (1)
- WT1 Proteins (1)
- X-ray crystallograph (1)
- Publication
- Publication Type
Articles 1 - 3 of 3
Full-Text Articles in Biochemistry, Biophysics, and Structural Biology
The Role Of Mapks In B Cell Receptor-Induced Down-Regulation Of Egr-1 In Immature B Lymphoma Cells, Jiyuan Ke, Murali Gururajan, Anupam Kumar, Alan Simmons, Lilia Turcios, Ralph Lakshman Chelvarajan, David M. Cohen, David L. Wiest, John G. Monroe, Subbarao Bondada
The Role Of Mapks In B Cell Receptor-Induced Down-Regulation Of Egr-1 In Immature B Lymphoma Cells, Jiyuan Ke, Murali Gururajan, Anupam Kumar, Alan Simmons, Lilia Turcios, Ralph Lakshman Chelvarajan, David M. Cohen, David L. Wiest, John G. Monroe, Subbarao Bondada
Microbiology, Immunology, and Molecular Genetics Faculty Publications
Cross-linking of the B cell receptor (BCR) on the immature B lymphoma cell line BKS-2 induces growth inhibition and apoptosis accompanied by rapid down-regulation of the immediate-early gene egr-1. In these lymphoma cells, egr-1 is expressed constitutively and has a prosurvival role, as Egr-1-specific antisense oligonucleotides or expression of a dominant-negative inhibitor of Egr-1 also prevented the growth of BKS-2 cells. Moreover, enhancement of Egr-1 protein with phorbol 12-myristate 13-acetate or an egr-1 expression vector rescued BKS-2 cells from BCR signal-induced growth inhibition. Nuclear run-on and mRNA stability assays indicated that BCR-derived signals act at the transcriptional level to …
Membrane Organization And Multimeric Interactions Of The Aer Receptor In E. Coli, Divya Dashrathkumar Amin
Membrane Organization And Multimeric Interactions Of The Aer Receptor In E. Coli, Divya Dashrathkumar Amin
Loma Linda University Electronic Theses, Dissertations & Projects
Escherichia coli swims toward niches ideal for generating maximum energy by monitoring the environment with the aerotaxis sensor, Aer. This receptor has an N-terminal PAS domain, which is a sensor module present in a variety of proteins from all kingdoms of life (including humans). To date, the mechanism of signaling from a PAS sensor domain to a single signaling receiver domain has not been resolved. In Aer, the PAS sensor is separated from the signaling region by a membrane anchor. Most "transmembrane prediction" programs forecast a single membrane span for this membrane anchor, but such a topology is inconsistent our …
Desulfovibrio Desulfuricans G20 Tetraheme Cytochrome Structure At 1.5 A˚ And Cytochrome Interaction With Metal Complexes, Mrunalini Pattarkine, J J. Tanner, C A. Bottoms, Y H. Lee, Judy D. Wall
Desulfovibrio Desulfuricans G20 Tetraheme Cytochrome Structure At 1.5 A˚ And Cytochrome Interaction With Metal Complexes, Mrunalini Pattarkine, J J. Tanner, C A. Bottoms, Y H. Lee, Judy D. Wall
Faculty Works
The structure of the type I tetraheme cytochrome c3 from Desulfovibrio desulfuricans G20 was determined to 1.5 A˚ by X-ray crystallography. In addition to the oxidized form, the structure of the molybdate-bound form of the protein was determined from oxidized crystals soaked in sodium molybdate. Only small structural shifts were obtained with metal binding, consistent with the remarkable structural stability of this protein. In vitro experiments with pure cytochrome showed that molybdate could oxidize the reduced cytochrome, although not as rapidly as U(VI) present as uranyl acetate. Alterations in the overall conformation and thermostability of the metal-oxidized protein were investigated …