Project description:The dataset consists of 266 NCCN very low/low or favorable-intermediate risk PCa patients who underwent diagnostic prostate biopsy between 2000 and 2014 and were treated with RP in six community or academic practices: University of Calgary, Cedars-Sinai, Spectrum Health, Cleveland Clinic, MD Anderson Cancer Center and Johns Hopkins. All patients had complete tumor pathology from biopsy and prostatectomy. Low risk PCa was defined as T1c or cT2a, and Gleason score (GS) ≤ 6, and PSA < 10ng/ml and favorable-intermediate risk was no greater than predominant GS 3 and percent positive biopsy cores < 50%, and either cT2b-cT2c or PSA 10-20ng/ml.
Project description:To find out the binding partners of EhRacJ, crosslinking and coimmunoprecipitation were performed. Then, eluted samples were submitted to Mass Spectrometry and Proteomics Core Facility, Johns Hopkins University School of Medicine and analyzed by mass spctrometry (shotgun proteomics). The coimmunoprecipitation and following analysis were conducted only a single time. You can find data of HA-EhRacJ from "2023_3_13_28_AM_FileSize_1261863517_Byte_F012933.mzid.gz", "2023_3_13_28_AM_FileSize_1261863517_Byte_F012933.mzid_2023_3_13_28_AM_File_Size__1261863517__Byte__F012933.MGF", "JS-E480-CS_230524_NozakiT_MS_DDA_S1_10pct.msf", "JS-E480-CS_230524_NozakiT_MS_DDA_S1_10pct.mzML", and "JS-E480-CS_230524_NozakiT_MS_DDA_S1_10pct.RAW". You can find data of pEhEx-HA (mock) from "2023_6_54_27_PM_FileSize_1168419053_Byte_F012936.mzid.gz", "2023_6_54_27_PM_File Size_1168419053_Byte_F012936.mzid_2023_6_54_27_PM_File_Size__1168419053__Byte__F012936.MGF", "JS-E480-CS_230524_NozakiT_MS_DDA_S4_10pct.msf", "JS-E480-CS_230524_NozakiT_MS_DDA_S4_10pct.mzML", and "JS-E480-CS_230524_NozakiT_MS_DDA_S4_10pct.RAW".
Project description:Johns Hopkins clinical research office quality assurance group will monitor and audit this study at Johns Hopkins. The Sub Investigator at each site will be responsible for internal monitoring at their site.
| 2156010 | ecrin-mdr-crc
Project description:Johns Hopkins Center of Excellence for Influenza Research and Surveillance (JHCEIRS)
Project description:1Sheng Yushou Center of Cell Biology and Immunology, Department of Genetics and Developmental Biology, School of Life Sciences and Biotechnology, Shanghai Jiao Tong University, Shanghai, 200240, China. 2Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, New York, NY 10065, USA. 3Systems Biology Center, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, MD 20892, USA. 4CCTS Bioinformatic Program, The Rockefeller University, New York, NY 10065, USA. 5State Key Laboratory of Genetic Engineering & Ministry of Education Key Laboratory of Contemporary Anthropology, Collaborative Innovation Center of Genetics and Development, School of Life Sciences, Fudan University, Shanghai, 200438, China
Project description:Kynureninase is a member of a large family of catalytically diverse but structurally homologous pyridoxal 5'-phosphate (PLP) dependent enzymes known as the aspartate aminotransferase superfamily or alpha-family. The Homo sapiens and other eukaryotic constitutive kynureninases preferentially catalyze the hydrolytic cleavage of 3-hydroxy-l-kynurenine to produce 3-hydroxyanthranilate and l-alanine, while l-kynurenine is the substrate of many prokaryotic inducible kynureninases. The human enzyme was cloned with an N-terminal hexahistidine tag, expressed, and purified from a bacterial expression system using Ni metal ion affinity chromatography. Kinetic characterization of the recombinant enzyme reveals classic Michaelis-Menten behavior, with a Km of 28.3 +/- 1.9 microM and a specific activity of 1.75 micromol min-1 mg-1 for 3-hydroxy-dl-kynurenine. Crystals of recombinant kynureninase that diffracted to 2.0 A were obtained, and the atomic structure of the PLP-bound holoenzyme was determined by molecular replacement using the Pseudomonas fluorescens kynureninase structure (PDB entry 1qz9) as the phasing model. A structural superposition with the P. fluorescens kynureninase revealed that these two structures resemble the "open" and "closed" conformations of aspartate aminotransferase. The comparison illustrates the dynamic nature of these proteins' small domains and reveals a role for Arg-434 similar to its role in other AAT alpha-family members. Docking of 3-hydroxy-l-kynurenine into the human kynureninase active site suggests that Asn-333 and His-102 are involved in substrate binding and molecular discrimination between inducible and constitutive kynureninase substrates.
Project description:Analysis of transcriptional profiles in Sbds(ATG) MO-injected embryos with and without coinjection of p53(ATG) MO. We identified a large number of changes in transcript abundance associated with loss of Sbds. Among the 24,278 annotated zebrafish genes in the platform, 4,892 significantly differentially expressed genes were identified. Embryos were carefully staged at 24 hpf and RNA was extracted from approximately 50 embryos per condition in Trizol, followed by purification using RNA miniprep columns (Qiagen). Four independent experiments were extracted. cDNA microarrays were performed at the Sidney Kimmel Comprehensive Cancer Center at Johns Hopkins Microarray Core Facility using 4x44K Zebrafish gene expression microarray slides (Agilent, Santa Clara, CA).