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Dr. Hai Lin
Assistant Professor, Department of Bioengineering
| Email: |
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| Phone: |
(412) 624-7196 |
| Fax: |
(412) 383-8788 |
| Office: |
743 Benedum Hall |
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Education
B.S. (Physics), Peking University, China.
Ph.D. (Biophysics), University of California, Berkeley
Professional Interests
The main area of our research is the study of structure, function,
and interactions of individual biological macromolecules at the
cellular and molecular levels with a multimodal approach, using
the Atomic Force Microscope (AFM) combined with molecular biology,
cell biology, and electrophysiological techniques.
Current projects include:
- Structure and aggregation of amyloid beta peptide and its functional
role in the pathogenesis of the Alzheimer's disease
- Structure and function of ion channels: gap junctional channels
and amyloid beta peptide channels
- Force interaction between individual biomolecules: receptor-ligand
interation
- Cellular biomechanics: cellular and subcellular structural and
mechanical changes induced by cellular transformation and migration
Selected Publications
- Amyloid b protein forms ion channels: implications for Alzheimer's
disease pathophysiology . [Lin, H., R. Bhatia, and R. Lal. FASEB
Journal, 2001, 15: 2433-2444.]
- Imaging molecular structure and physiological function of gap
junctions and hemijunctions by multimodal atomic force microscopy.
[Lal, R. and H. Lin. Microscopy Research and Technique
2001, 52:273-88.]
- Mapping heparin-binding sites on fibronectin with atomic force
microscope. [Lin, H, R. Lal, and D.O. Clegg. Biochemistry,
2000, 39: 3192-3196.]
- Amyloid beta protein (1-40) induces calcium-dependent rapid
cytoskeletal reorganization and cellular degeneration in cultured
fibroblast cells. [Zhu, Y, H. Lin, and R. Lal. FASEB Journal.
2000, 14:1244-54.]
- Fresh and globular amyloid beta protein (1-42) but not amyloid
beta proteins (1-40) and (25-35) induces calcium-dependent mediated
rapid degeneration of cultured endothelial cells. [Bhatia, R.K.,
H. Lin, and R. Lal. FASEB Journal. 2000, 14:1233-43.
- Gap junctional hemichannels is a calcium-sensititive cell volume
modulator. [Rhee, S.K., A.P. Quist, H. Lin, and R. Lal. Journal
of Cell Biology, 2000, 148:1063-1074.]
- Amyloid beta protein (1-40) forms calcium-permeable, Zn2+-sensitive
channel in reconstituted lipid vesicles. [Lin, H, Y.J. Zhu, and
R. Lal. Biochemistry, 1999, 38:11189-96.]
- Imaging real-time proteolysis of single collagen I molecules
with an atomic force microscope. [Lin, H, D.O.Clegg, and R. Lal.
Biochemistry, 1999, 38:9956-63.]
- Integrin alpha-v/beta-5 participates in the phagocytosis of
photoreceptor rod outer segments by cultured human retinal pigment
epithelium. [Lin, H. and D.O. Clegg. Investigative Ophthalmology
and Visual Science, 39: 1703-12, 1998.]
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