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Truncated Hemoglobins: A New Family of Hemoglobins Widely Distributed in Bacteria, Unicellular Eukaryotes, and Plants* 210
- J. Wittenberg, M. Bolognesi, B. Wittenberg, M. Guertin
- BiologyJournal of Biological Chemistry
- 11 January 2002
Crystal structures show that trHb tertiary structure is based on a 2-on-2 -hel-ical sandwich, which represents an unprecedented editing of the highly conserved globin fold, and may provide a path for ligand diffusion to the heme.
CD81 extracellular domain 3D structure: insight into the tetraspanin superfamily structural motifs
It is proposed that tetraspanins may assemble at the cell surface into homo‐ and/or hetero‐dimers through a conserved hydrophobic interface located in the stalk subdomain, while interacting with other liganding proteins, including hepatitis C virus E2, through the head subdomain.
Atlas of the clinical genetics of human dilated cardiomyopathy.
This is to the authors' knowledge, the first study that comprehensively investigated the genetics of DCM in a large-scale cohort and across a broad gene panel of the known DCM genes and underline the high analytical quality and feasibility of Next-Generation Sequencing in clinical genetic diagnostics.
Crystal structure of D-amino acid oxidase: a case of active site mirror-image convergent evolution with flavocytochrome b2.
- A. Mattevi, M. Vanoni, B. Curti
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 23 July 1996
The catalytic sites of D-amino acid oxidase and flavocytochrome b2 appear to have converged to a highly similar but enantiomeric architecture in order to catalvze similar reactions, although with opposite stereochemistry.
CtBP/BARS: a dual‐function protein involved in transcription co‐repression and Golgi membrane fission
The crystal structure together with the site‐directed mutagenesis data and binding experiments suggest a rationale for the molecular mechanisms underlying the two fundamental co‐existing, but diverse, activities supported by CtBP/BARS in the nucleus and in Golgi membranes.
Sequence-Specific Transcription Factor NF-Y Displays Histone-like DNA Binding and H2B-like Ubiquitination
Structure and functionality in flavivirus NS-proteins: Perspectives for drug design
Ivermectin is a potent inhibitor of flavivirus replication specifically targeting NS3 helicase activity: new prospects for an old drug.
- E. Mastrangelo, M. Pezzullo, M. Milani
- Biology, MedicineJournal of Antimicrobial Chemotherapy
- 1 August 2012
Ivermectin, a broadly used anti-helminthic drug, proved to be a highly potent inhibitor of YFV replication and inhibited, although less efficiently, the replication of several other flaviviruses, i.e. dengue fever, Japanese encephalitis and tick-borne encephalopathy viruses.
A novel two‐over‐two α‐helical sandwich fold is characteristic of the truncated hemoglobin family
Crystal structures of trHbs from the ciliated protozoan Paramecium caudatum and the green unicellular alga Chlamydomonas eugametos show that the tertiary structure of both proteins is based on a ‘two‐over‐two’ α‐helical sandwich, reflecting an unprecedented editing of the classical ‘three‐ over‐three’α‐helICAL globin fold.
The Redox State of the Cell Regulates the Ligand Binding Affinity of Human Neuroglobin and Cytoglobin*
The results suggest a novel mechanism for the regulation of oxygen binding; contact with an appropriate electron donor would provoke the release of oxygen, directly linked to the redox state of the cell.