Immediately preceding CHI's Recombinant Antibodies Conference

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CHI's High-Content Screening: Parallel Analysis Fuels Accelerated Discovery and Development
CHI's Proteomics Survey 2003
CHI's GPCRs: Mining the Richest Vein in Drug Discovery
CHI's Kinases: From Targets to Therapeuties

Phage display of peptide and protein libraries is a powerful tool for identifying compounds that recognize and bind to targets that have been identified. These repertoires of proteins and peptides include enzymes and antibodies, which have interest as drug targets. Phage systems are used for the detection of protein-ligand interactions and for improving binding affinities. The diversity of display methodologies that exist (ribosome, yeast, phage, bacterial, antibody) offers a variety of capabilities in panning for affinity interactions. Alternative display systems offer the opportunity to address issues of expression biases that exist with phage display and to explore the possibility of creating compounds of small molecular weight, greater diversity, and druglike properties. Phage display can be used to identify biomarkers of disease in prostate cancer, cardiovascular disease, and angiogenesis. The peptides are capable of homing to specific pathways and targets within those pathways. By generating the proteins expressed from cDNA libraries, display methodologies can provide a direct link between phenotype and genotype.

SCIENTIFIC ADVISORY BOARD
Dr. Andrew Bradbury, Los Alamos National Laboratory
Dr. Hennie R. Hoogenboom, University of Liège
Dr. Renata Pasqualini, M.D. Anderson Cancer Center, University of Texas
Dr. Richard Wagner, Praecis Pharmaceuticals Inc.
Dr. Gregory A. Weiss, University of California, Irvine
Dr. K. Dane Wittrup, Massachusetts Institute of Technology

KEYNOTE PRESENTATIONS NEW PROTEINS FROM IN VITRO COMBINATORIAL AND EVOLUTIONARY APPROACHES Dr. Andreas Plückthun, Professor, Department of Biochemistry, University of Zürich EVOLUTION OF NOVEL PROTEINS BY MRNA DISPLAY Dr. Jack W. Szostak, Investigator, Howard Hughes Medical Institute and Harvard Medical School; Alex Rich Distinguished Investigator, Massachusetts General Hospital

ADDITIONAL SPEAKERS
Dr. Robert F. Balint, KaloBios, Inc.
Dr. Angela Belcher, Massachusetts Institute of Technology
Mr. Steven E. Cwirla, XenoPort Inc. 
Dr. Sven Klussmann, NOXXON Pharma AG
Dr. Shohei Koide, The University of Chicago
Dr. Elias Lazarides, Targeted Molecules Corporation (TMC)
Mr. Hening Lin, Columbia University
Dr. Lee Makowski, Argonne National Laboratory
Dr. Michael McPherson, Phylos, Inc.
Dr. Renata Pasqualini, M.D. Anderson Cancer Center, University of Texas
Dr. Edward F. Patz, Jr., Duke University Medical Center
Dr. Henrik Pedersen, Nuevolution A/S, Denmark
Dr. Christopher P. Rusconi, Duke University Medical Center
Dr. Aaron Sato, Dyax Corp.
Dr. Sachdev Sidhu, Genentech Inc.
Dr. Merilyn Sleigh, Evogenix Pty Ltd.
Dr. Michael A. Tainsky, Wayne State University
Dr. Michael B. Yaffe, Massachusetts Institute of Technology
Dr. Ping Zhong, Abmaxis Inc.

	PRE-CONFERENCE TUTORIAL
Display Technologies, Library Construction, and Screening Dr. Jamie Scott, Simon Fraser University

NEW TECHNOLOGIES AND TARGET SELECTION
Cell-Based Systems for Protein Engineering
High-Diversity Libraries for Rapid Protein Optimization
Monobodies: Small Antibody Mimics
Phage-Based Electronic and Magnetic Materials

USE OF PHAGE DISPLAY TO DISCOVER SMALL MOLECULES
Mapping Small Molecule Binding Sites with Phage Display
Synthetic Compound Libraries Displayed on Bacteriophages
DNA-Encoded Small Molecules and Molecular Evolution
Novel Lead Molecules through in Vivo Phage Display

APPLICATIONS IN PROTEOMICS
A Genetic Assay for Protein Evolution and Proteomics
Decoding Protein Kinase Signaling Networks
Drug Receptor Identification Using mRNA Display
Novel, High-Affinity Tumor Imaging Agents
Cancer Diagnostics Using Microarrays of Phage-Displayed Tumor Antigens
Mapping Molecular Diversity of Blood Vessels by in Vivo Phage Display

APPLICATION IN NOVEL THERAPEUTICS AND DIAGNOSTICS
Use of Phage Display to Identify Antibodies with Exquisite Target Specificity
Mapping Binding Energetics with Statistical Analysis of Combinatorial Libraries
Regulatable Therapeutics: Aptamer-Antidote Pairs
A Novel and Versatile Platform for Antibody Display and Engineering via Heterodimerization

	POST-CONFERENCE TUTORIAL
Comparison of Display Technologies for Making Therapeutic Antibodies Dr. James D. Marks, University of California, San Francisco

 

 

PROGRAM

SUNDAY, MAY 11

	PRE-CONFERENCE TUTORIAL
1:30pm Registration 2:00-5:00 Display Technologies, Library Construction, and Screening Dr. Jamie Scott, Professor, Molecular Biology and Biochemistry, Simon Fraser University This tutorial will cover an explanation and comparison of antibody, yeast, phage, and peptide display as well as various screening methodologies. 4:00-6:00 Early Conference Registration, Poster and Exhibit Set-up

 

MONDAY, MAY 12

7:00am Registration, Poster Viewing, and Light Continental Breakfast

8:30 Chairperson's Opening Remarks
Dr. K. Dane Wittrup, J.R. Mares Professor, Chemical Engineering & Bioengineering, Massachusetts Institute of Technology

KEYNOTE PRESENTATIONS 8:40 New Proteins from in Vitro Combinatorial and Evolutionary Approaches Dr. Andreas Plückthun, Professor of Biochemistry, Department of Biochemistry, University of Zürich Recent progress in selection and evolution technologies has made it possible to select functional proteins completely in vitro. Some of the recent results with ribosome display will be summarized. In these experiments, antibodies were selected from synthetic libraries and at the same time evolved for higher affinity or for higher stability. The crystal structures of some of the antibodies now permit an analysis of the effect of these mutations. More recently, this concept has been generalized to other protein types, such as Ankyrin Repeat Proteins and Leucine-Rich-Repeat Proteins, which may be especially suitable for intracellular expression and thus inhibition of intracellular targets and functional genomics. Finally, one may embark on creating new functional pro-teinswithout any structural precedent. Eventually, this may help address some fundamental questions of why there are so few different protein folds encoded in the known genomes. 9:15 Evolution of Novel Proteins by mRNA Display Dr. Jack W. Szostak, Investigator, Howard Hughes Medical Institute; Professor of Genetics, Harvard Medical School; Alex Rich, Distinguished Investigator, Department of Molecular Biology, Massachusetts General Hospital In vitro translation of an mRNA labeled with a 3’-puromycin residue results in covalent attachment of the resulting protein to its own mRNA. Libraries of such joint molecules may be subjected to selection for protein function, and the encoding nucleic acid may then be amplified, allowing in vitro directed evolution of protein function. The large library sizes accessible through mRNA display allow new functional proteins to be derived from libraries of completely random sequences. 9:45 Poster and Exhibit Viewing, Refreshment Break

NEW TECHNOLOGIES AND TARGET SELECTION

10:30 Chairperson's Remarks
Dr. Richard Wagner, Executive Vice President, Science and Technology, Praecis Pharmaceuticals Inc.

10:35 Bacterial Cell-Based Selection Systems for Protein Engineering
Dr. Robert F. Balint, Chief Scientific Officer, KaloBios, Inc.
We will describe the development of enzyme sensors that can be activated or inactivated by target molecules and protein-protein interactions and the use of these sensors in cell-based systems for epitope-guided selection, humanization, and affinity maturation of antibodies.

11:05 High-Diversity Variant Libraries for Rapid Protein Optimization
Dr. Merilyn Sleigh, Chief Executive Officer, Evogenix Pty Ltd.
EvoGeneTechnology is a newly developed approach to protein optimization. Its advantages lie in rapid, high-level amplification of RNA encoding a parent protein, using error-prone RNA replicases. The resulting RNA population yields highly diverse libraries of protein variants after translation, with each variant differing by one or two amino acids from the parent protein. At a potential diversity at the RNA level approaching 1011, a very high proportion of all possible single amino acid substitution variants should be sampled in a single round of mutation and selection. The method is proving to be highly effective in delivering proteins with improved properties and is adaptable for use with a wide range of display methodologies, either in cell-free or cell-based systems.

11:35 Monobodies: Binding Proteins Based on the Fibronectin Type III Domain
Dr. Shohei Koide, Associate Professor of Biochemistry and Molecular Biology, The University of Chicago
The tenth fibronectin type III domain of human fibronectin (FNfn10) is a small beta-sandwich protein similar to the immunoglobulin domain. It is highly stable without disulfide bonds, and it can be expressed at a high level in bacteria. We have shown that FNfn10 is an excellent scaffold to display multiple surface loops for target binding. I will present recent results of combinatorial screening of FNfn10-based binding proteins, "monobodies," and their applications.
12:05 Phage-Based Electronic and Magnetic Materials
Dr. Angela Belcher, Associate Professor of Materials Science and Engineering and Bioengineering, Massachusetts Institute of Technology
We have been using phage display to identify peptides that select for and specifically bind to inorganic structures such as semiconductor wafers and semiconductor and magnetic nanoparticles. This approach utilizes the inherent self-organizing, highly selective properties of biologically derived molecules. We are currently investigating peptide recognition and interaction with III-V and II-VI semiconductor materials and magnetic materials including Fe3O4, Co, FePt, and CoPt. We have selected peptides that can specifically bind to and discriminate zinc-blende III-V semiconductor surfaces. These peptides show crystal face specificity and are being used to organize nanoparticles heterostructures. We have also selected peptides that can nucleate and control phase, particle diameter, and aspect ratio of semiconductor and magnetic nanoparticles. These peptides are being used to grow nanoparticles and nanowires of specific crystallographic structure and orientation. Using these molecular interactions and specific nanoparticles the phage nanoparticle composites are being assembled into liquid crystal structures that are organized on the nanometer to centimeter-length scale. In addition, organizing organic/inorganic hybrid materials into other supramolecular architectures will be discussed.

12:35 Panel Discussion

1:00 Lunch (on your own)

 

USE OF PHAGE DISPLAY TO DISCOVER SMALL MOLECULES

2:30 Chairperson's Remarks
Dr. Gregory Weiss, Assistant Professor, Department of Chemistry, University of California, Irvine

2:35 Mapping Small Molecule Binding Sites with Phage Display Technology
Dr. Lee Makowski, Director, Biosciences Division, Argonne National Laboratory
We are generating sequences predictive for binding of small molecules to proteins through analysis of affinity-selected, phage-displayed peptides. This technique has been successfully employed to map the contact residues in the targets of a variety of drugs, drug candidates, and small molecule metabolites. This approach represents a novel, rapid, high-resolution method for identifying potential ligand-binding sites in the absence of three-dimensional information and has the potential to greatly enhance the speed of development of novel small molecule pharmaceuticals.

3:05 Synthetic Compound Libraries Displayed on the Surface of Encoded Bacteriophages
Mr. Steven E. Cwirla, Senior Scientist, Discovery Biology, XenoPort Inc.
We have developed a technology for efficiently attaching libraries of synthetic compounds to the coat proteins of bacteriophage particles such that the identity of the chemical structure is encoded in the genome of the phage, analogous to peptides displayed on phage surfaces in conventional phage library techniques. This format allows a library of synthetic compounds to be mixed and screened very efficiently as a pool. The compounds can be displayed in multiple copies on each phage particle, producing a multivalent format-an arrangement that has been shown in the context of peptide libraries to provide a very sensitive method of detecting binding activity. The encoded phage particles serve as an extremely robust reporter of the compounds' presence since individual infective phage particles can be detected, thus providing exquisite sensitivity for the identification of active compounds in complex biological assays. Combining phage display with split and pool combinatorial chemistry to construct and screen libraries of synthetic molecules may provide a powerful new method to facilitate the search for novel bioactive molecules.

3:35 Poster and Exhibit Viewing, Refreshment Break

4:15 DNA-Encoded Small Molecules and Molecular Evolution
Dr. Henrik Pedersen, Chief Executive Officer and Chief Scientific Officer, Nuevolution A/S, Denmark
We have developed a technology called Chemetics™, a technology that makes DNA encode small organic molecules. Moreover, the Chemetics™ technology generates small molecule displays, i.e., the small molecules become attached to the DNA-template that encoded their synthesis. This allows us to perform molecular evolution on druglike small molecules, which will allow the rapid and highly stringent screening of billions of molecules for pharmaceutical purposes.

4:45 Discovery of Novel Lead Molecules through in Vivo Phage Display
Dr. Elias Lazarides, President and Chief Executive Officer, Targeted Molecules Corporation (TMC)
Identifying drug leads that are amenable to optimization and successfully translating in vitro results to a complex in vivo biological system are key challenges for the industry. Invariably, researchers encounter dose shifts, unanticipated toxicity, and suboptimal efficacy when a lead candidate is tested in an in vivo system. Since this step typically occurs at the end of the preclinical research process, the cost of failure can be very high. TMC bypasses these challenges of traditional in vitro-based drug discovery by utilizing its LIVO™ platform to perform lead identification and optimization in vivo. The LIVO™ technology is based on the patented use of in vivo phage display to deliver highly complex (or focused) libraries of candidate molecules in the bloodstream of living animals and then to recover those molecules that are preferentially retained by the vasculature of a target tissue. TMC uses LIVO™ to identify lead molecules that have a high level of selectivity to a target in vivo and then to optimize their structure to achieve a desired pharmacokinetic profile in vivo (using kinetic SAR or kSAR™ technology). Once identified and optimized, the lead is used to identify the molecular receptor in the target tissue. By utilizing LIVO™ and kSAR™ with a disease model having a phenotypic readout, TMC is able to directly discover novel leads that modulate the disease process.

5:15 Panel Discussion

5:45 Reception with Poster and Exhibit Viewing

7:00 Close of Day One

TUESDAY, MAY 13

8:00am Poster and Exhibit Viewing and Light Continental Breakfast

 

APPLICATIONS IN PROTEOMICS

8:30 Chairperson's Remarks
Dr. Renata Pasqualini, Associate Professor of Medicine and Cancer Biology, University of Texas M.D. Anderson Cancer Center

8:35 Chemical Complementation: A Genetic Assay for Protein Evolution and Proteomics
Mr. Hening Lin, Department of Chemistry, Columbia University
A high-throughput assay for enzyme activity has been developed that is reaction independent. In this assay, a small molecule yeast three-hybrid system is used to link enzyme catalysis to transcription of a reporter gene in vivo. Here we demonstrate the feasibility of this approach using a well-studied enzyme-catalyzed reaction, cephalosporin hydrolysis by the Enterobacter cloacae P99 cephalosporinase. We show that the three-hybrid system can be used to read out cephalosporinase activity in vivo as a change in the level of transcription of a lacZ reporter gene and that the wild-type cephalosporinase can be isolated from a pool of inactive mutants using a lacZ screen. The assay has been designed so that it can be applied to different chemical reactions without changing the components of the three-hybrid system. A reaction-independent, high-throughput assay for protein function should be a powerful tool for protein engineering and enzymology, drug discovery, and proteomics.

9:05 Peptide Library Screening and Proteomics: Decoding Protein Kinase Signaling Networks
Dr. Michael B. Yaffe, Assistant Professor, Center for Cancer Research, Department of Biology, Massachusetts Institute of Technology
Oriented peptide library screens can be used to reveal substrate preferences for protein kinases and binding motifs for modular signaling domains. I will describe these techniques and discuss how the motifs can be combined with bioinformatics approaches to reveal interacting partners by proteomic screening in silico. Finally, I will discuss a novel library versus library screening approach that identifies new binding modules and their ligands in proteomic screens for new signaling pathways.

9:35 Drug Receptor Identification Using mRNA Display
Dr. Michael McPherson, Principal Scientist, Phylos, Inc.
MRNA display allows libraries of proteins covalently linked to their encoding mRNA to be probed for interactions of biological interest. When cellular transcripts are used as a source for library construction, the corresponding mRNA display libraries can be used to discover cellular proteins that bind to small molecule ligands. We have applied this approach towards the selection and identification of known and novel drug receptors.

10:05 Poster and Exhibit Viewing, Refreshment Break

10:30 Development of Novel, High-Affinity Tumor Imaging Agents
Dr. Edward F. Patz, Jr., Professor of Radiology and Pathology and Professor of Pharmacology and Cancer Biology, Department of Radiology, Duke University Medical Center
The talk will describe the clinical need for novel tumor imaging agents and then address some of the parameters for in vivo imaging. The talk will then focus on molecular targets and the strategies used with phage display combinatorial libraries to develop imaging ligands.

11:00 Cancer Diagnostics Using Microarrays of Phage-Displayed Tumor Antigens
Dr. Michael A. Tainsky, Professor and Director, Program in Molecular Biology and Genetics, Barbara Ann Karmanos Cancer Institute, Wayne State University
Ovarian cancer is highly curable if diagnosed early but women who are diagnosed with it at a late stage have a very poor prognosis. We have developed a novel screening technology for early detection of ovarian cancer using T7 phage display cDNA libraries. We use selective biopanning to isolate clones of antigens reacting with antibodies present specifically in the sera of patients with ovarian cancer. The goal is to use serum antibody reactivity to proteins expressed in ovarian tumors as diagnostic biomarkers. Serum antibodies arise toward a cellular protein because of the presentation of a mutated form of the protein from the tumor cells or due to overexpression of the protein in the tumor cells. The antibody reaction to large numbers of these antigens is detected in a highly parallel assay on robotically spotted microarrays of the proteins. By assaying serum antibodies from patients and controls with two-color fluorescence detection on antigen biochips, we can differentiate women with ovarian cancer from healthy women without false positives due to other gynecological syndromes classically confounding other diagnostic technologies.

11:30 Mapping the Molecular Diversity of Blood Vessels by in Vivo Phage Display: Steps: Towards the Development of Targeted Therapies and Imaging Agents
Dr. Renata Pasqualini, Associate Professor, GU Oncology, M.D. Anderson Cancer Center, University of Texas
Despite major progress brought about by the Human Genome Project, the molecular diversity of human blood vessels remains largely unexplored. Our research is aimed at targeting diagnostic and therapeutic agents to blood vessels by using probes that can bind to specific vascular addresses. Towards this goal, we developed technologies to identify small peptides that target the endothelium. Different strategies are used to isolate peptides from large libraries displayed in the surface of bacteriophage. Through this platform technology, we have uncovered various tissue-specific and angiogenesis-related vascular addresses. This complex system of ligand-receptor pairs will lead to a better understanding of tumor circulatory microenvironment, changes in blood vessels during tumor progression, and the localization of novel markers in cancer and other diseases with an angiogenesis component. This lecture will review several targeting strategies that may enable the construction of a molecular map outlining vascular diversity in each organ, tissue, or disease.

12:00 Panel Discussion

12:30 Luncheon with Poster and Exhibit Viewing (sponsored by Cambridge Healthtech Institute)

 

APPLICATION IN NOVEL THERAPEUTICS AND DIAGNOSTICS

1:45 Chairperson's Remarks
Dr. Robert Ladner, Senior Vice President and Chief Scientific Officer, Dyax Corp.

1:50 Use of Phage Display to Identify Peptides, Proteins, and Antibodies with Exquisite Target Specificity
Dr. Aaron Sato, Director of Research, Dyax Corp.
Dyax has over two dozen antibody, peptide, and protein phage display libraries, which are screened in high throughput to identify binders that recognize subtle conformational, co- and post-translational modifications. Several examples showing exquisite specificity for clinical targets will be presented. This specificity combined with the high affinity for target allows for the development of therapeutics with greatly reduced cross-reactivity to nontargeted tissue, lower dosing requirements, and improved toxicity profiles.

2:20 Mapping Binding Energetics at Protein-Protein Inter-faces with Statistical Analysis of Combinatorial Libraries
Dr. Sachdev Sidhu, Scientist, Department of Protein Engineering, Genentech Inc.
By using combinatorial libraries with restricted binomial diversity, up to 30 protein residues can be simultaneously mutated in phage-displayed libraries. Following functional selections for binding, DNA sequencing of hundreds of clones can be used to calculate the statistical preference of wild-type relative to a mutant, and, in turn, these data can be used to estimate the binding energy contribution of each sidechain at a protein-protein interface. In addition, analysis of pairwise covariance can be used to detect the presence of nonadditive, cooperative interactions between sidechains. The "shotgun scanning" approach is extremely rapid since analysis relies on simple selections and DNA sequencing rather than complex protein purification and biophysical assays.

2:50 Poster and Exhibit Viewing, Refreshment Break

3:15 Regulatable Therapeutics: Aptamer-Antidote Pairs
Dr. Christopher P. Rusconi, Director of Research, Program in Combinatorial Therapeutics, and Assistant Research Professor, Department of Surgery, Duke University Medical Center
Many therapeutic agents are associated with adverse effects in patients. This is especially true of antithrombotic drugs such as anticoagulants, antiplatelets, and clot-busting drugs (thrombolytics) as the proteins targeted by such drugs maintain a critical balance in the patient between blood fluidity and blood clotting caused by disease or clinical intervention. The ability to control the activity of such drugs will improve patient outcomes by increasing the safety of patients undergoing treatments in which such drugs are used (e.g., heart attack, stroke, angioplasty, cardiovascular surgery, etc.). Antidote control provides the safest means to regulate drug activity, yet very few antidote-controlled drugs are available. To address this unmet need for safer regulatable therapeutics, we have developed a platform to enable generation of drug-antidote pairs, in which the drug comprises an aptamer and the antidote comprises an oligonucleotide that neutralizes the inhibitory activity of the aptamer. We have applied this technology to the development of an antidote-controlled anticoagulant that targets coagulation factor IXa. Previously published in vitro studies (Rusconi et al., Nature 419, p. 90-94, 2002) and ongoing in vivo studies of this novel drug-antidote pair will be presented.

3:45 Recent Developments in the Field of Spiegelmers
Dr. Sven Klussmann, Chief Technology Officer, NOXXON Pharma AG
Spiegelmers are mirror-image oligonucleotides antagonizing or inhibiting target molecules. These ligands can be identified by using an adaptation of the so called SELEX process. Spiegelmers combine the advantageous properties of aptamers - high affintiy and high specificity binding to a given target molecule - with exceptional biological stability. Besides first activity studies in animals other in vivo properties will be reported.

4:15 A Novel and Versatile Platform for Antibody Display and Engineering via Heterodimerization
Dr. Ping Zhong, Director, Display Technology, Abmaxis Inc.
Display of combinatorial antibody library on the surface of bacteriophage is a key step for selection of antibodies of high specificity and high affinity. In traditional phagemid-based platforms, antibody proteins are first co-expressed in E. coli cells along with a bacteriophage coat protein, either as a fusion protein or as a separate protein. After being rescued by helper phage, the antibody protein is shuttled by the co-expressed coat protein and eventually incorporated into the surface of the phagemid particles. We have developed a new generation of phage display system, the adaptor-directed display system. In the new system, the antibody is expressed as fusion with a small adaptor that can specifically form heterodimeric complex with its counterpart adaptor. The antibody protein is then anchored on the surface of a phagemid particle through specific heterodimerization between the two interacting adaptors. The system could be used as a vehicle of bacteriophage display, bacteria surface display, and protein expression. This novel and versatile system has been successfully used for selection antibody libraries against different antigens.

4:45 Close of Conference

POST-CONFERENCE TUTORIAL

(Includes Light Dinner) 5:30-8:30 Comparison of Display Technologies for Making Therapeutic Antibodies Dr. James D. Marks, Professor, Anesthesia & Pharmaceutical Chemistry, University of California, San Francisco A number of competing display technologies have been developed for generating and evolving therapeutic antibodies. Using antibodies to the bioterror agent botulinum neurotoxin, we have studied and compared phage versus yeast display for both generation of lead antibodies from immune libraries as well as for evolution of antibody affinity. Here we describe the differences we have observed with respect to (1) expression host bias, (2) antibody diversity, (3) antibody affinity, (4) expression levels, and (5) ease of manipulation. Conclusions will be presented as to when each system is best employed.

Dyax Corp. is a biopharmaceutical company focused on the discovery, development and commercialization of therapeutic peptides, small proteins and antibodies for various diseases and conditions. Dyax currently has two recombinant proteins in phase II clinical trials for three indications (hereditary angioedema, cardiopulmonary bypass and cystic fibrosis).

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Call for Posters
Cambridge Healthtech Institute encourages attendees to gain further exposure by presenting their work in the poster sessions. Please fill out the registration form, with the poster title and primary author. To ensure inclusion in the conference CD, a one-page summary must be submitted and registration must be paid in full by April 4, 2002.   Click here for poster instructions

Hotel Information
Hyatt Regency Cambridge | 575 Memorial Drive  |  Cambridge, MA 02139
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Cut-off Date: April 21, 2003

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