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    Armour Faculty

    Yuzhu Zhang, Ph.D.

    Assistant Professor of Biology

    Office: 342 Life Sciences Building
    Office Hours:
    Phone: 312.567.3484
    Fax:
    Email: zhangy@iit.edu
    Web: Zhang's Web page

    Expertise

    Education

    • B.S, Zhengzhou University
    • Ph.D, University of Pennsylvania

    Curriculum Vitae

    Research & Major Accomplishments

    OUR INTERESTS:

    My group is interested in studying the structure, interaction, and function of proteins whose mutation or abnormal expression results in misregulation of cellular processes or abnormal expression of other proteins and proteins whose gain or loss of function as a result of mutation or abnormal expression causes diseases such as cancer and neurodegenerative diseases.

    We are also interested in determining the physical, chemical, and structural properties that make some food proteins allergens.

    OUR CURENT PROJECTS:

    Structural basis of chosen transcript factors, splicing factors, and cytokines.

    Structural basis of the allergenicity and allergic cross-reactivity of peanut and tree nut allergens.

    OUR APPROACHES:

    X-ray crystallography, NMR, and other spectrometric methods are our main research tools. Molecular biology and cell biology technologies are also routinely used in our laboratory.

    Current Projects

    Awards/Honors

    Patents

    Books

    Selected Publications

    X-ray crystal structure of TNF ligand family member TL1A at 2.1A. T. Jin, F. Guo, S. Kim, A. Howard, and Y.Z. Zhang, Biochem Biophys Res Commun (2007). 364, 1-6.

    A 1.55 A resolution X-ray crystal structure of HEF2/ERH and insights into its transcriptional and cell-cycle interaction networks. T. Jin, F. Guo, I.G. Serebriiskii, A. Howard, and Y.Z. Zhang, Proteins: Structure, Function, and Bioinformatics (2007). 68, 427-437.

    Structure, stability, and function of hDim1 investigated by NMR, circular dichroism, and mutational analysis. Y.Z. Zhang, H. Cheng, K.L. Gould, E.A. Golemis, and H. Roder, Biochemistry (2003). 42, 9609-9618.

    Evidence that dim1 associates with proteins involved in pre-mRNA splicing, and delineation of residues essential for dim1 interactions with hnRNP F and Npw38/PQBP-1. Y.-Z. Zhang, T. Lindblom, A. Chang, M. Sudol, A.E. Sluder, and E.A. Golemis, Gene (2000). 257, 33-43.

    Rapid amide proton exchange rates in peptides and proteins measured by solvent quenching and two-dimensional NMR. Y.Z. Zhang, Y. Paterson, and H. Roder, Protein Sci (1995). 4, 804-814.

    Publication list

    Professional Society Memberships

    Editorial Board Service

    Professional Society Service

    Grants

    Community Service

    Jialing Xiang
    Department of Biological, Chemical, and Physical Sciences

    Cell death is a normal body function. Each day, cells repair themselves or commit suicide and die. About 15 years ago, researchers began to look more closely at it for clues to diseases involving abnormal cell death, like cancer. more...

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