A program to predict organic reactions, ROBIA, has been developed. It achieves reaction prediction on the basis of coded rules and molecular modeling calculations, generating possible transition states, intermediates, and products given the starting material and reaction conditions. The program generates all possible reaction pathways, on the basis of the selected transformations within its database, and evaluates them selecting the most feasible ones. The program has been successfully tested against several examples.
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Another-regulin regulates cardiomyocyte calcium handling via integration of neuroendocrine signaling with SERCA2a activity.
J Mol Cell Cardiol
December 2024
The Heart Institute, Division of Molecular Cardiovascular Biology, Cincinnati Children's Hospital Medical Center, Cincinnati, OH, USA; Department of Pediatrics, University of Cincinnati College of Medicine, Cincinnati, OH 45229, USA. Electronic address:
Calcium (Ca) dysregulation is a hallmark feature of cardiovascular disease. Intracellular Ca regulation is essential for proper heart function and is controlled by the sarco/endoplasmic reticulum Ca ATPase (SERCA2a). Another-regulin (ALN) is a newly discovered cardiomyocyte-expressed SERCA2a inhibitor, suggesting cardiomyocyte Ca-handling is more complex than previously appreciated.
View Article and Find Full Text PDFDynamic conformational changes in the rhesus TRIM5α dimer dictate the potency of HIV-1 restriction.
Virology
January 2017
Department of Microbiology and Immunology, Stritch School of Medicine, Loyola University Chicago, Chicago, IL, USA.
The TRIM5α protein from rhesus macaques (rhTRIM5α) mediates a potent inhibition of HIV-1 infection via a mechanism that involves the abortive disassembly of the viral core. We have demonstrated that alpha-helical elements within the Linker 2 (L2) region, which lies between the SPRY domain and the Coiled-Coil domain, influence the potency of restriction. Here, we utilize single-molecule FRET analysis to reveal that the L2 region of the TRIM5α dimer undergoes dynamic conformational changes, which results in the displacement of L2 regions by 25 angstroms relative to each other.
View Article and Find Full Text PDFRestriction of HIV-1 by rhesus TRIM5α is governed by alpha helices in the Linker2 region.
J Virol
August 2014
Cellular and Molecular Biochemistry Program, Stritch School of Medicine, Loyola University Chicago, Maywood, Illinois, USA Department of Microbiology and Immunology, Stritch School of Medicine, Loyola University Chicago, Maywood, Illinois, USA Integrative Cell Biology Program, Stritch School of Medicine, Loyola University Chicago, Maywood, Illinois, USA
Unlabelled: TRIM5α proteins are a potent barrier to the cross-species transmission of retroviruses. TRIM5α proteins exhibit an ability to self-associate at many levels, ultimately leading to the formation of protein assemblies with hexagonal symmetry in vitro and cytoplasmic assemblies when expressed in cells. However, the role of these assemblies in restriction, the determinants that mediate their formation, and the organization of TRIM5α molecules within these assemblies have remained unclear.
View Article and Find Full Text PDFThe anti-apoptotic protein HAX-1 is a regulator of cardiac function.
Proc Natl Acad Sci U S A
December 2009
Department of Pharmacology and Cell Biophysics, University of Cincinnati College of Medicine, Cincinnati, OH 45267-0575, USA.
The HS-1 associated protein X-1 (HAX-1) is a ubiquitously expressed protein that protects cardiomyocytes from programmed cell death. Here we identify HAX-1 as a regulator of contractility and calcium cycling in the heart. HAX-1 overexpression reduced sarcoplasmic reticulum Ca-ATPase (SERCA2) pump activity in isolated cardiomyocytes and in vivo, leading to depressed myocyte calcium kinetics and mechanics.
View Article and Find Full Text PDFThe E3 ubiquitin ligase atrophin interacting protein 4 binds directly to the chemokine receptor CXCR4 via a novel WW domain-mediated interaction.
Mol Biol Cell
March 2009
Program in Molecular Biology, Stritch School of Medicine, Loyola University Chicago, Maywood, IL 60153, USA.
The E3 ubiquitin ligase atrophin interacting protein 4 (AIP4) mediates ubiquitination and down-regulation of the chemokine receptor CXCR4. AIP4 belongs to the Nedd4-like homologous to E6-AP carboxy terminus domain family of E3 ubiquitin ligases, which typically bind proline-rich motifs within target proteins via the WW domains. The intracellular domains of CXCR4 lack canonical WW domain binding motifs; thus, whether AIP4 is targeted to CXCR4 directly or indirectly via an adaptor protein remains unknown.
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