He, Xiaolin, PhD

Selected Publications

Selected Publications

Selected publications (out of 26):
1. He XL, Chow, D., Martick, M.M., Garcia, K.C. Allosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone. Science 2001, 293: 1657-1662.
2. He XL, Grigg, M.E., Boothroyd, J.C., Garcia, K.C. Crystal structure of the immunodominant surface antigen of Toxoplasma Gondii. Nat Struct Biol 2002, 9(8): 606-11.
3. He XL, Radu, C., Sidney, J., Sette, A., Ward, E.S., Garcia, K.C. Structural snapshot of aberrant antigen presentation linked to autoimmunity: the immunodominant epitope of myelin basic protein complexed with I-Au. Immunity 2002, 17(1): 83-94.
4. He XL, Bazan, J.F., McDermott, G. Park, J.B., Wang, K., Tessier-Lavigne, M., He, Z. and Garcia, K.C. Structure of the Nogo receptor ectodomain: a recognition module implicated in myelin inhibition. Neuron 2003, 38: 177-185.
5. He XL, Garcia, K.C. Structure of nerve growth factor complexed with the shared neurotrophin receptor p75. Science, 2004, 304(5672):870-5.
6. Wehrman T*, He XL*, Raab B, Dukipatti A, Blau H, Garcia KC. (*Co-first authors). Structural and mechanistic insights into nerve growth factor interactions with the TrkA and p75 receptors. Neuron. 2007 Jan 4;53(1):25-38
7. Liu H, Chen X, Focia PJ, He XL. Structural basis for stem cell factor-KIT signaling and activation of class III receptor tyrosine kinases. EMBO J. 2007 Feb 7;26(3):891-901
8. Chen XY, Liu H, Shim AH, Focia PJ, He XL. Structural basis for synaptic adhesion mediated by neuroligin-neurexin interactions. Nat Struct Mol Biol. 2008 Jan;15(1):50-6. Epub 2007 Dec 16.
9. Chen XY, Liu H, Focia, PJ, Shim AH, He XL. Structure of macrophage colony stimulating factor bound to FMS: diverse signaling assemblies of class III receptor tyrosine kinases. Proc Natl Acad Sci U S A. Nov 25;105(47):18267-72. Epub 2008 Nov 18.
10. Liu H, Shim AH, HeXL. Structural characterization of the ectodomain of a disintegrin and metalloproteinase-22 (ADAM22), a neural adhesion receptor instead of metalloproteinase: Insights on ADAM function*. J Biol Chem. 2009 Epub Aug 18. (*Selected as Paper of the Week)
11. Shim AH, Liu H, Focia PJ, Chen X, Lin PC, He XL. Structures of a platelet-derived growth factor/propeptide complex and a platelet-derived growth factor/receptor complex. Proc Natl Acad Sci U S A. 2010 Jun 22;107(25):11307-12. Epub 2010 Jun 2.

Information

Name

He, Xiaolin, PhD

Title

Associate Professor

Email

x-he@northwestern.edu

Office Phone

312-503-8030

Department

Molecular Pharmacology and Biological Chemistry

Office

Searle 8-417 Chicago

Areas of Research

Mechanisms of Drug Action, Molecular Neuroscience, Neurobiology of Disease, Signal Transduction

NU Scholar Profile

http://www.scholars.northwestern.edu/expert.asp?u_id=952

Recent Publications on PubMed

http://www.ncbi.nlm.nih.gov/pubmed?term=He%2C%20Xiaolin%5BFull%20Author%20Name%5D&cmd=DetailsSearch

Current Research

Current Research

Research interest of this lab is understanding the structural mechanisms of signal transduction across the plasma membrane that control the development of cancer and neural system. Our current focus is on how the cell-surface receptors in these systems recognize extracellular signals and initiate intracellular downstream cascades. The approaches used in this lab include a variety of biochemical and biophysical methods, particularly the X-ray crystallography.
<strong>Receptor tyrosine kinases:</strong>
Receptor tyrosine kinases are a family of transmembrane receptors playing vital roles in cell growth and differentiation, and frequently involved in cancer. They have intrinsic catalytic activities carried by the intracellular segments which are regulated by ligand binding to their extracellular segments. The general activation paradigm of this family is known to be ligand-mediated receptor dimerization, but the specific receptor-ligand binding schemes are not well understood for most of the family members. Deciphering these schemes is important in designing cancer drugs targeting at transmembrane signaling. We will investigate multiple sub-families of receptor tyrosine kinases that have been established to be important in cancer, with an emphasis on solving high-resolution structures of receptor/ligand complexes.
<strong>Neuronal receptor signaling:</strong>
Signaling by transmembrane receptors is essential in neural development. Understanding how the neuronal receptors play in the proliferation, differentiation and growth inhibition of nerve cells has profound implications for disorders of the human nervous system. Unraveling the structural mechanisms used by important neuronal receptors may offer potential therapy for treatment of CNS injuries and neuronal degenerative diseases. Our initial interest will be studying those directly mediating trophic or inhibitory signals through membrane, for example, the neurotrophin receptors, the myelin inhibition receptors and the axon guidance receptors.