St. Jude Children's Research Hospital

About: St. Jude Children's Research Hospital is a healthcare organization based out in Memphis, Tennessee, United States. It is known for research contribution in the topics: Population & Virus. The organization has 9344 authors who have published 19233 publications receiving 1233399 citations. The organization is also known as: St. Jude Children's Hospital & St. Jude Hospital.

High speed 1H spectroscopic imaging in human brain by echo planar spatial-spectral encoding.

Abstract: We introduce a fast and robust spatial-spectral encoding method, which enables acquisition of high resolution short echo time (13 ms) proton spectroscopic images from human brain with acquisition times as short as 64 s when using surface coils. The encoding scheme, which was implemented on a clinical 1.5 Tesla whole body scanner, is a modification of an echo-planar spectroscopic imaging method originally proposed by Mansfield Magn. Reson. Med. 1, 370-386 (1984), and utilizes a series of read-out gradients to simultaneously encode spatial and spectral information. Superficial lipid signals are suppressed by a novel double outer volume suppression along the contours of the brain. The spectral resolution and the signal-to-noise per unit time and unit volume from resonances such as N-acetyl aspartate, choline, creatine, and inositol are comparable with those obtained with conventional methods. The short encoding time of this technique enhances the flexibility of in vivo spectroscopic imaging by reducing motion artifacts and allowing acquisition of multiple data sets with different parameter settings.

The t(12;21) translocation converts AML-1B from an activator to a repressor of transcription.

Abstract: The t(12;21) translocation is present in up to 30% of childhood B-cell acute lymphoblastic and fuses a potential dimerization motif from the ets-related factor TEL to the N terminus of AML1. The t(12;21) translocation encodes a 93-kDa fusion protein that localizes to a high-salt- and detergent-resistant nuclear compartment. This protein binds the enhancer core motif, TGTGGT, and interacts with the AML-1-binding protein, core-binding factor beta. Although TEL/AML-1B retains the C-terminal domain of AML-1B that is required for transactivation of the T-cell receptor beta enhancer, it fails to activate transcription but rather inhibits the basal activity of this enhancer. TEL/AML-1B efficiently interferes with AML-1B dependent transactivation of the T-cell receptor beta enhancer, and coexpression of wild-type TEL does not reverse this inhibition. The N-terminal TEL helix-loop-helix domain is essential for TEL/AML-1B-mediated repression. Thus, the t(12;21) fusion protein dominantly interferes with AML-1B-dependent transcription, suggesting that the inhibition of expression of AML-1 genes is critical for B-cell leukemogenesis.