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Contact Information Office Hours: Spring 2007 Last updated: 3 January 2008 |
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Biochemistry 1 (Biology 301) -- fall
Biochemistry 1 Lab (Biology 303) -- fall
Biochemistry 2 (Biology 302) -- spring
Biochemistry 2 Lab (Biology 304) -- spring
Biological Principles: Biochemistry of Health and Disease (Biology 114) -- spring
Course materials for my current courses are available through HC Moodle
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Click the image for information about the Holy Cross Biochemistry Concentration jointly offered by the Departments of Biology and Chemistry
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My research focuses primarily on the biochemistry of the proteins that compose, or are associated with, the cell cytoskeleton. The cytoskeleton in higher animal cells is generally thought to be composed of three classes of protein-based filaments, the microfilaments, the microtubules and the intermediate filaments. In recent years, the cytoskeleton has become the focus of much disease-related research because it is thought to be involved in a multitude of essential cellular processes including cell division, cell migration, transport of intracellular material, the maintenance of cell integrity and the overall integration of cellular space. Through a multi-faceted approach involving protein purification, cell culture, microscopy and molecular interaction assays, studies in my lab focus on examining the protein-based linkages that tie cytoskeletal filament proteins to each other, and to other cellular proteins to which filaments are linked. Current studies in the lab are specifically focused in two areas: (1) understanding the mechanism of linkage between intermediate filaments and specific cellular structures, such as focal adhesions and organelles, and (2) determining the nature of the linkages between the cytoskeleton and a specific class of transmembrane proteoglycans known as the syndecans.
Students with an interest in biochemistry who would like to consider pursuing a research project in my laboratory are encouraged to contact me at their earliest convenience.
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(For more complete publication information, refer to my CV)
Bellin, R.M. and K.V. Mills (2007) The Holy Cross Biochemistry Concentration: An Integrated Four-Year Program to Develop Undergraduate Research Scholars in Designing, Implementing, and Sustaining a Research-Supportive Undergraduate Curriculum (K.K. Karukstis and T.E. Elgren, eds.), pp. 394-396, Council on Undergraduate Research
LeDuc, P.R. and R.M. Bellin (2006) Nanoscale intracellular organization and functional architecture mediating cellular behavior. Ann. Biomed. Eng. 34:102-113 {PubMed link}
Lee, H.-S., R.M. Bellin, D.L. Walker, B. Patel, P. Powers, H. Liu, B. Garcia-Alvarez, J.M. de Pereda, R.C. Liddington, N. Volkmann, D. Hanein, D.R. Critchley and R.M. Robson (2004) Characterization of an actin-binding site within the talin FERM domain. J. Mol. Biol. 343:771-784 {PubMed link}
Robson, R.M., T.W. Huiatt, and R.M. Bellin (2004) Muscle Intermediate Filament Proteins in Methods in Cell Biology Vol. 78 (M.B. Omary and P.A. Coulombe, eds.), pp. 519-553, Elsevier Science, USA,
Bellin, R.M., I. Capila, J. Lincecum, P.W. Park, O. Reizes and M.R. Bernfield (2003) Unlocking the secrets of syndecans: transgenic organisms as a potential key. Glycoconj. J. 19: 295-304 {PubMed link}
Stromer, M.H., M.S. Mayes, R.M. Bellin (2002) Use of actin isoform-specific antibodies to probe the domain structure in three smooth muscles. Histochem. Cell Biol.118:291-299
Bellin, R.M., T.W. Huiatt, D.R. Critchley, and R.M. Robson
(2001) Synemin may function to directly link muscle cell intermediate filaments
to both myofibrillar Z-lines and costameres. J. Biol. Chem. 276: 32330-32337
Lee, H.S., R.M. Bellin, and R.M. Robson (2001) Talin in The Encyclopedia of Molecular Medicine Vol. 5, pp.
3087-3089, John Wiley & Sons, New York
Schweitzer, S., M.W. Klymkowsky, R.M. Bellin, R.M. Robson,
Y. Capetanaki, and R.M. Evans (2001) Paranemin and the organization of desmin
filament networks J. Cell Sci. 114:1079-1089
Sultana, S., S.W. Sernett, R.M. Bellin, R.M. Robson, and O.
Skalli (2000) Intermediate filament protein synemin is transiently expressed in
a subset of astrocytes during development. Glia 30:143-153
Bellin, R.M., S.W. Sernett, B. Becker, W. Ip., T.W. Huiatt,
and R.M. Robson (1999) Molecular characteristics and interactions of the
intermediate filament protein synemin: Interactions with alpha-actinin may anchor synemin-containing heterofilaments. J.
Biol. Chem. 274: 29493-29499
Bellin, R.M., S.W. Sernett, and R.M. Robson (1999) Synemin in Guidebook to the Cytoskeletal and Motor Proteins,
Second Edition (T. Kreis and R. Vale,
eds.), pp. 322-324, Oxford Univ. Press, UK
Bilak, S.R., S.W. Sernett, M.M. Bilak, R.M. Bellin, M.H. Stromer, T.W. Huiatt, and R. M. Robson (1998) Properties of the novel intermediate filament protein synemin and its identification in mammalian muscle. Arch. Biochem. Biophysics 355: 63-76 {Pubmed link}
Hemken, P.M., R.M. Bellin, S.W. Sernett, B. Becker, T.W.
Huiatt, and R.M. Robson (1997) Molecular characteristics of the novel
intermediate filament protein paranemin: sequence reveals EAP-300 and IFAPa-400
are highly homologous to paranemin. J. Biol. Chem. 272: 32489-32499
Becker, B., R.M. Bellin, S.W. Sernett, T.W. Huiatt, and
R.M. Robson (1995) Synemin contains the rod domain of intermediate filaments. Biochem.
Biophys. Res. Commun. 213: 796-802
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| College of The Holy Cross | 1 College Street, Worcester, MA 01610 | (508) 793 2011 | Copyright 2007 | email rbellin@holycross.edu |