Jennifer R. Cochran

Honors and Awards

• Martin D. Abeloff Scholar Award, V Foundation (2008)
• Hellman Faculty Scholar Award, Hellman Foundation (2008)
• McCormick Award, McCormick Foundation (2007)
• Mallinckrodt Faculty Scholar Award, Edward Mallinckrodt Jr. Foundation (2007)
• Kimmel Scholars Award, Sidney Kimmel Foundation (2007)
• Translational Partnership Award, Wallace H. Coulter Foundation (2006, 2007)
• Howard Temin Award, NIH / National Cancer Institute (2004)

Professional Education

• Postdoctoral Fellow, MIT Biological Engineering
• Ph. D., MIT Biological Chemistry (2001)
• B.S., University of Delaware Biochemistry (1995)

Postdoctoral Advisees

• Niv Papo

Graduate & Fellowship Program Affiliations

• Biophysics
• Cancer Biology
• Bioengineering

Web Site Links

• Cochran Lab website

Research Interests

The Cochran laboratory uses interdisciplinary approaches in chemistry, engineering, and biophysics to study complex biological systems. Our main goals are to develop new technologies for basic science and biomedical applications. Clinical applications of our research involve bone and wound healing, biomimetic corneas, neural cell regeneration, and cancer imaging and therapy. Our research is driven by the philosophy that in order to control physiological processes it is necessary to understand the molecular mechanisms that drive these processes. We are interested in elucidating molecular details of receptor-mediated cell signaling events; at the same time developing protein and polymer-based tools that will allow us to manipulate cellular processes on a molecular level. For biomedical applications, we are combining rational design and combinatorial methods to create designer protein therapeutics and diagnostic agents. One such example is highlighted in a recent press release: http://news-service.stanford.edu/news/2006/may24/cochran-052406.html.

Publications

• Engineered knottin peptides: a new class of agents for imaging integrin expression in living subjects. Kimura RH,  Cheng Z, Gambhir SS, Cochran JR.  Cancer Res.  2009; 69 (6): 2435-42
• Engineered cystine-knot peptides that bind alpha(v)beta(3) integrin with antibody-like affinities. Silverman AP,  Levin AM, Lahti JL, Cochran JR.  J Mol Biol.  2009; 385 (4): 1064-75
• Antibodies specifically targeting a locally misfolded region of tumor associated EGFR. Garrett TP,  Burgess AW, Gan HK, Luwor RB, Cartwright G, Walker F, Orchard SG, Clayton AH, Nice EC, Rothacker J, Catimel B, Cavenee WK, Old LJ, Stockert E, Ritter G, Adams TE, Hoyne PA, Wittrup D, Chao G, Cochran JR, Luo C, Lou M, Huyton T, Xu Y, Fairlie WD, Yao S, Scott AM, Johns TG.  Proc Natl Acad Sci U S A.  2009; 106 (13): 5082-7
• Interrogating and predicting tolerated sequence diversity in protein folds: application to E. elaterium trypsin inhibitor-II cystine-knot miniprotein. Lahti JL,  Silverman AP, Cochran JR.  PLoS Comput Biol.  2009; 5 (9): e1000499
• Developing therapeutic proteins by engineering ligand-receptor interactions. Jones DS,  Silverman AP, Cochran JR.  Trends Biotechnol.  2008; 26 (9): 498-505
• Engineered cystine knot peptides that bind alphavbeta3, alphavbeta5, and alpha5beta1 integrins with low-nanomolar affinity. Kimura RH,  Levin AM, Cochran FV, Cochran JR.  Proteins.  2009; 77 (2): 359-69
• Bioactive interpenetrating polymer network hydrogels that support corneal epithelial wound healing. Myung D,  Farooqui N, Zheng LL, Koh W, Gupta S, Bakri A, Noolandi J, Cochran JR, Frank CW, Ta CN.  J Biomed Mater Res A.  2009; 90 (1): 70-81
• Development of hydrogel-based keratoprostheses: a materials perspective. Myung D,  Duhamel PE, Cochran JR, Noolandi J, Ta CN, Frank CW.  Biotechnol Prog.  2008 May-Jun; 24 (3): 735-41
• Elucidation of the interleukin-15 binding site on its alpha receptor by NMR. Hanick NA,  Rickert M, Varani L, Bankovich AJ, Cochran JR, Kim DM, Surh CD, Garcia KC.  Biochemistry.  2007; 46 (33): 9453-61
• Design and fabrication of an artificial cornea based on a photolithographically patterned hydrogel construct. Myung D,  Koh W, Bakri A, Zhang F, Marshall A, Ko J, Noolandi J, Carrasco M, Cochran JR, Frank CW, Ta CN.  Biomed Microdevices.  2007; 9 (6): 911-22
• Directed evolution of the epidermal growth factor receptor extracellular domain for expression in yeast. Kim YS,  Bhandari R, Cochran JR, Kuriyan J, Wittrup KD.  Proteins.  2006; 62 (4): 1026-35
• Improved mutants from directed evolution are biased to orthologous substitutions Cochran JR,  Kim YS, Lippow SM, Rao B, Wittrup KD.  Protein Engineering, Design and Selection.  2006; 19 245-53
• Identification of the epitope for the epidermal growth factor receptor-specific monoclonal antibody 806 reveals that it preferentially recognizes an untethered form of the receptor. Johns TG,  Adams TE, Cochran JR, Hall NE, Hoyne PA, Olsen MJ, Kim YS, Rothacker J, Nice EC, Walker F, Ritter G, Jungbluth AA, Old LJ, Ward CW, Burgess AW, Wittrup KD, Scott AM.  J Biol Chem.  2004; 279 (29): 30375-84
• Fine epitope mapping of anti-epidermal growth factor receptor antibodies through random mutagenesis and yeast surface display. Chao G,  Cochran JR, Wittrup KD.  J Mol Biol.  2004; 342 (2): 539-50
• Domain-level antibody epitope mapping through yeast surface display of epidermal growth factor receptor fragments. Cochran JR,  Kim YS, Olsen MJ, Bhandari R, Wittrup KD.  J Immunol Methods.  2004; 287 (1-2): 147-58
• Flow-cytometric isolation of human antibodies from a nonimmune Saccharomyces cerevisiae surface display library. Feldhaus MJ,  Siegel RW, Opresko LK, Coleman JR, Feldhaus JM, Yeung YA, Cochran JR, Heinzelman P, Colby D, Swers J, Graff C, Wiley HS, Wittrup KD.  Nat Biotechnol.  2003; 21 (2): 163-70
• Soluble peptide-MHC monomers cause activation of CD8+ T cells through transfer of the peptide to T cell MHC molecules. Ge Q,  Stone JD, Thompson MT, Cochran JR, Rushe M, Eisen HN, Chen J, Stern LJ.  Proc Natl Acad Sci U S A.  2002; 99 (21): 13729-34
• Receptor proximity, not intermolecular orientation, is critical for triggering T-cell activation. Cochran JR,  Cameron TO, Stone JD, Lubetsky JB, Stern LJ.  J Biol Chem.  2001; 276 (30): 28068-74
• T-cell activation by soluble MHC oligomers can be described by a two-parameter binding model. Stone JD,  Cochran JR, Stern LJ.  Biophys J.  2001; 81 (5): 2547-57
• Receptor clustering and transmembrane signaling in T cells. Cochran JR,  Aivazian D, Cameron TO, Stern LJ.  Trends Biochem Sci.  2001; 26 (5): 304-10
• Cutting edge: detection of antigen-specific CD4+ T cells by HLA-DR1 oligomers is dependent on the T cell activation state. Cameron TO,  Cochran JR, Yassine-Diab B, Sékaly RP, Stern LJ.  J Immunol.  2001; 166 (2): 741-5
• TCR: losing its inhibitions? Cameron TO,  Stone JD, Cochran JR, Stern LJ.  Trends Immunol.  2001; 22 (9): 479-80
• The relationship of MHC-peptide binding and T cell activation probed using chemically defined MHC class II oligomers. Cochran JR,  Cameron TO, Stern LJ.  Immunity.  2000; 12 (3): 241-50
• A diverse set of oligomeric class II MHC-peptide complexes for probing T-cell receptor interactions. Cochran JR,  Stern LJ.  Chem Biol.  2000; 7 (9): 683-96