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Albany 2009: Conversation 16

category image Albany 2009
Conversation 16
June 16-20 2009
© Adenine Press (2008)

Topics, Speakers, Chairs and Guests

The 16th Conversation, June 16-20, 2009 will be held at the State University of New York, Albany, NY 12222 USA. Participants will arrive on Tuesday June 16th, there is a dinner and reception that evening. The scientific program starts Wednesday morning June 17th and will end after lunch on Saturday June 20th at 2:00 PM. Immediately following the lunch from 2:00-5:00 PM. there will be a post-Conversation workshop on Nucleosome Positioning. The conference will have roughly 50 lectures by leading scientists, in addition to several short lectures by young scientists who will be selected from abstracts submitted for poster presentations. We will have on display, throughout the conference, some 250 poster discussion papers. We anticipate about 400 participants with diverse background from over 20 countries for these continuing conversations.

Young Scientist Lecture Program
The Organizing Committee has left 5.5 hrs of the Conversation time for the young scientist lecture program. Extraordinarily talented young professional researchers, at the rank of assistant professors, post-doctoral fellows and doctoral students, will be selected from the abstracts submitted for poster presentations to provide oral presentations which will be sandwiched between those by senior scientists.

Director
Ramaswamy H. Sarma, Department of Chemistry
State University of New York, Albany NY 12222 USA
ph: 518-456-9362; fx: 518-452-4955
email: rhs07@albany.edu

Go Main Website Albany 2009
Go Book of Abstracts Albany 2009



Sponsored by:
University at Albany
National Institutes of Health
President Obama's American Recovery and Reinvestment Act of 2009 (pending)
JBSD and Adenine Press

Keynote Address
The Albany Conversation traditionally holds evening lectures in areas of fundamental interest to structural biology. In 2009, on Wednesday June 17th 8:00 PM, Nobel Laureate Andrew Fire, Professor of Pathology and Genetics, Stanford, will provide an overview of nucleic acid structures associated with gene silencing. Biological systems frequently respond to foreign genetic information, both RNA and DNA, by silencing and/or eliminating this information. How do cells know what gene expression is natural/useful and what is unwanted/pathological? Numerous surveillance mechanisms are known, with a common starting point being the structural recognition of "aberrant" nucleic acid structures. Prof. Fire's talk will focus on several known and novel structural features that may contribute to recognition and silencing of foreign genetic information. Edward Trifonov from the ancient city of Haifa, Israel and the University of Haifa will introduce Professor Fire and chair the session.
Alternative Splicing, Disordered Proteins and Embryonic Stem Cells
Alternative splicing is one of the major mechanisms for generating protein diversity in higher eukaryotes on both the functional level within an organism and the evolutionary scale. This session will commence with a general presentation by Mikhail Gelfand, IITP, Moscow, Russia, on the evolution of the exon-intron structure and regulation of alternative splicing via formation of RNA structure; and the other speakers will focus on alternative splicing and embryonic stem (ES) cells, which can proliferate without limit and maintain the ability to form any cell type (pluripotency), properties that allow unprecedented access to components of the human body. James Thomson, Univ. of Wisconsin, School of Medicine, will describe a model system for examining how pluripotency is lost during differentiation of human ES cells, and how it can be restored through reprogramming by defined factors. Gene Yeo, Salk Institute, will present his work on the detection of alternative splicing in human embryonic stem cells that differentiate into neural progenitors, the identification of an RNA binding protein that is important for stem cell survival, and the elucidation of its in vivo binding sites by using a combination of molecular approaches and deep sequencing efforts. Keith Dunker, IUPUI, will describe his work on regions of pre-mRNA that are absent or present in different isoforms due to alternative splicing; these regions often code for protein structures that are intrinsically disordered. Characterization of signaling pathways involved in stem cell replication indicates a high amount of intrinsic disorder in the proteins involved and a substantial degree of alternative splicing at the pre-mRNA level. Keith will discuss linkages between these two observations and how these linkages might be important for stem cell differentiation.
Genomics: System Biology and Networks
Comparative genomics has evolved, with uncommon bravado, to a level that entertains extraordinary and bold predictions, visit our ancestors and look into the future. Takashi Gojobori, NIG, Mishima, Japan, will elucidate, with rare audacity, the evolutionary origin and processes of the Central Nervous System and the brains of vertebrates, including human, from the comparative gene expressionics of hydra and planarian. Masaru Tomita, Keio Univ., Fujisawa, Japan, will talk about multi-omics data based integrative systems biology with special focus on metabolome analysis. L. Aravind, NCBI, NIH, will show how our comprehension of regulatory sytems in general has profoundly changed. Shaped by gene loss and lineage-specific expansions, dominant families of specific transcription factors differ even among sister lineages; predicted chromatin proteins from protists allow reconstruction of the early evolutionary history of histone and DNA modification, nucleosome assembly and chromatin-remodeling systems.
Chromatin and Epigenetics
A crucial, hitherto unraveled, genetic code lies in the epigenetic layer of information present in the chromatin filament, a dynamic assembly of DNA, proteins and other chemicals. In this session we will try to understand chromatin organization beyond the nucleosome level, in particular, on the 30 nm fiber, whose structure still remains a puzzle. What is the topology of the 30 nm fiber? Does the fiber act as a tunable coil in which the extent of DNA wrapping around the histone octamer is topologically coupled to the compaction of the fiber ? What is the real nature of the genomic code in DNA for nucleosome positioning? A new technique, EM-assisted nucleosome interaction capture, will be presented for quantitative mapping of juxtaposed nucleosomes in nucleosome arrays with uniform and variable DNA linkers. This approach enables one to uncover nucleosome interactions inside higher-order chromatin fibers. The core histone N-terminal domains mediate the nucleosome-nucleosome interactions involved in fiber condensation, while the linker histone C-terminal domain stabilizes the condensed states of chromatin fibers. This evolving story on chromatin will be told by: Daniela Rhodes, MRC, LMB,, Cambridge UK; Andrew Travers, MRC, LMB, Cambridge, UK; Sergei Grigoryev, Pennsylvania State Univ.;and Jeffrey C. Hansen, Colorado State Univ. Chemical modifications of DNA or histone proteins with markers such as methyl, acetyl, ubiquitin or phosphate groups have been referred to by such magical names as imprinting and epigenetic tagging; they profoundly affect gene expression. For the past 20 years Stephen Baylin, Johns Hopkins, has studied the role of epigenetic gene silencing in the initiation and progression of human cancer. He will advocate the thesis that DNA hypermethylation of gene promoters, and associated transcriptional silencing, can serve as an alternative to mutations for producing loss of tumor suppressor gene function. Cynthia Wolberger, Johns Hopkins will discuss the structure-based mechanism underlying the unusual chemistry of Sir2 enzymes, which deacetylate proteins in an NAD+ dependent manner to regulate transcriptional silencing, as well as a variety of other cellular processes. She will describe how a subset of these enzymes can catalyze other chemistries such as de-propionylation and ADP ribosylation, and how Sir2 enzymes select potential substrates in the cell.
RNA: Silencing of the Genome
Brenda Bass, Univ. of Utah, will discuss her work on the biological functions of the vast amount of dsRNA encoded in genomes, expressed as noncoding transcripts, or within 3' UTRs of mRNAs. To understand these functions she studies the dsRNA binding proteins involved in RNA interference and RNA editing, which bind to endogenous dsRNA to mediate its functions. David Corey, Univ. of Texas, Dallas, will describe the identification of small RNAs that are complementary to promoter sequences and activate or repress gene expression. These RNAs bind to noncoding RNA transcripts rather than mRNA and recruit proteins to gene promoters. Corey's thesis is that a mechanism for RNA-mediated regulation of gene promoters would have evolutionary advantages because RNA can evolve new specificities for nucleic acid recognition more readily than proteins. Gerhart Wagner, Univ. of Uppsala, Sweden, will expound on the biological roles that small, regulatory RNAs play in bacteria - from stress responses to virulence. Most of these RNAs use an antisense mechanism.
RNA: Ribosome and Control of Protein Synthesis
When the story of the of the ribosome broke back in 2000, it was covered in extenso by major lectures during the 11th Conversation in 2001. Now, after 8 years, we are revisiting the story: We are discovering the history and ancestry of the ribosome and uncovering new knowledge about protein synthesis and gene expression. Ada Yonath, Weizmann, Israel, the virtuoso on ribosomes, will talk about newly identified structural elements that indicate ribosomes evolved by gene fusion and/or duplication. These elements contain mobile nucleotides that control amino acid polymerization and are exploited to create antibiotic binding pockets by induce fit mechanisms and remote interactions networks. Alexander Mankin, Univ. of Illlinois, U-C, will discuss a newly emerging mode of regulating gene expression that involves the sequence-specific interaction of the ribosome with a nascent peptide. He argues that the phenomenon can be of general significance and may affect expression of a number of cellular genes. Marina Rodnina, MPI Goettingen, Germany, employs fluorescence and rapid kinetics to delineate the mechanism of the ribosome and will discuss how it achieves high fidelity of gene expression on the translation level. Mark Safro, Weizmann, Israel, will vividly demonstrate the structural diversity and functional versatility among phenylalanyl-tRNA synthetases in primary kingdoms. Of course, Safro is certain about his conclusions, indeed, he has crystal structures of phenylalanyl-tRNA synthetase from different compartments of an eukaryotic cell, and from bacteria!
RNA: Catalysis, Folding and Interactions
The multifaceted biological roles of RNA, both ancient and modern, have become more and more apparent over the past decades. Dan Herschlag, Stanford Univ. interrogates RNA?s catalytic & folding behavior, and is undertaking comparisons with protein enzymes. His efforts will reveal the core behavior and abilities of RNA. After years of biochemical analysis of the intron architecture and chemical mechanisms, Anna Marie Pyle,, Yale Univ. will describe the recently solved the crystal structure of an intact group II intron. The high-resolution structure reveals a novel active-site architecture that binds Mg2+, and provides insights into RNA tertiary structural motifs and mechanisms for stable RNA folding. Hong Li,, Florida State Univ. will demonstrate that noncoding RNAs direct a multitude of protein factors, including catalytic components, to sites of enzymatic reactions by simultaneously binding proteins and substrate RNAs. In this process, conformational changes take place in both proteins and RNA, revealing rich principles of protein-RNA interactions. Saba Valadkhan,, Case Western Reserve Univ. will explain that in the spliceosome, small nuclear RNAs form the catalytic domain where they can catalyze splicing without proteins. In addition, she investigates the function of large non-coding RNAs that regulate cellular pathways as diverse as stress resistance and neuronal differentiation.
RNA: Structural Informatics
RNA structure enjoys extreme plasticity. Eric Westhof, Univ. of Strasbourg, France, will bring order to RNA architecture by using the twelve possible families of base-base interactions and the hierarchical assembly of recurrent RNA modules. Bruce A. Shapiro, NIH, NCI, will describe novel computational strategies to design RNA based nanoparticles. RNA represents a new molecular material for the design of biologically oriented nano devices, which hold great promise in the therapeutic arena. Jiri Sponer, IBP, Brno, CZ, employs theory, bioinformatics and experimental data to fathom flexibilities of RNA modular building blocks, and will apply this new knowledge to describe the atomic level fabrication of selected ribosomal RNA segments. And finally we have an extraordinarily talented young investigator from Tel Aviv Univ., Israel, Oranit Dror, who developed DARTS, a hierarchical classification DAtabase of RNA Tertiary Structures based on their spatial similarity. Her database will reveal the current structural repertoire of RNA.
Repeats: Selfish DNA and Toxic RNA ?Human Diseases
Wlodzimierz Krzyzosiak, Polish Academy of Science, Poznan, Poland, will show unusual features of RNA interference of triplet repeat sequences and discuss the implications for causative therapy of triplet repeat expansion diseases. Galina Filippova,, Fred Hutchinson Cancer Center, advocates a generalized formalism as a basis for several diseases associated with repetitive loci, including DM1, SCA8, HD, and FRAX. She will relate how this formalism involves RNA-mediated chromatin silencing at multiple repetitive loci in the genome. Galina passionately argues that bidirectional transcription across the repeat results in RNA-mediated local heterochromatin formation that is restricted by chromatin insulators ? small RNAs recruiting repressive chromatin marks, and DNA methylation, flanking the repeats. The expansion of repeats in the above diseases was accompanied by the loss of chromatin insulation function in the region, heterochromatin spreading and DNA methylation. Karen Vasquez,, Univ. of Texas, M D Anderson Cancer Ctr, will demonstrate that genes harboring non-B DNA structure-forming sequences augment the risk of genetic instability and thus are associated with human diseases. Karen has found that H-DNA and Z-DNA are mutagenic in mammalian cells, resulting in genetic instability predominantly in the form of DNA double-strand breaks. Kirill Lobachev,, Georgia Tech, will continue the theme of double strand breaks; using cruciform-forming inverted repeats and H-DNA-forming GAA/TTC triplet repeats to fathom the mechanisms of chromosomal fragility and genome rearrangements mediated by unstable repeats.
Protein-DNA, DNA-DNA, Protein-Protein Contacts and Gene Regulation
Mobile genetic elements are constantly reshaping genomes; they have had a major impact on evolution. Alison Hickman, NIH, will focus on DNA transposition, a recombination reaction that involves the movement of a discrete segment of DNA to a new genomic location. Her recent structural work provides insights into the varied mechanisms of prokaryotic and eukaryotic DNA transposition. Phoebe Rice, Univ. of Chicago, will elaborate on the mechanism and regulation of site specific DNA recombinanases which catalyze DNA inversions, deletions, and insertions, and are useful in genetic engineering. Konstantin Severinov, Rutgers Univ., who employs bacteriophage development, will provide detailed analyses of the interactions between bacteriophage-encoded proteins and host RNA polymerase, as a model system to study temporal regulation of gene expression and to uncover novel mechanisms of transcription regulation. Barry Honig, Columbia Univ., will delineate his studies of Hox proteins and other families of transcription factors which suggest a new mode of protein-DNA recognition: Nucleotide sequence determines minor groove shape which in turn determines the magnitude of electrostatic potentials in the groove. These potentials are then recognized by basic amino acids positioned appropriately in the protein structure. It appears that many DNA binding proteins use major groove contacts to recognize large sets of degenerate binding sites, with individual family members distinguishing among these sites via protein-specific minor groove contacts. Akinori Sarai, Kyushu Institute of Technology, Iizuka, Japan, will talk about the mechanism of protein-DNA recognition and methods to predict target genes for transcription factors. He will focus on a knowledge-based approach, utilizing rapidly increasing structural data of protein-DNA complexes, and computer simulations, to analyze the structure-function relationships in protein-DNA recognition and to make genome-scale predictions.
Proteins: Allostery, Network Communications and Design
Our ability to understand and identify rigidity/plasticity and populations of conformational states have driven us to revisit the problem of allostery. The network representation of non-covalent interactions of side-chains in protein structures helps us to identify the rigid and the flexible regions in proteins within the framework of global topology. The network parameters evaluated for conformational ensembles generated from molecular dynamics simulations enable us to understand allosteric communication in detail. Saraswathi Vishveshwara, IISc, Bangalore, India, will present such investigations on a few tRNA synthetases, which are excellent examples of allostery. Antonio del Sol, Fujirebio, Tokyo, Japan represents protein structures as residue interacting networks, which are assumed to involve a permanent flow of information between amino acids. He will describe the identification of centrally conserved residue folds, which are crucial for sustaining the shortest pathways and thus play key roles in the transmission of structural and dynamical allosteric perturbations. While side chains can reorient and rewire, allostery may not involve a change of (backbone) shape. Based on prediction of side-chain dynamics, dynamically important amino acids are elucidated for allosteric communications. Andrew Lee, Univ. of North Carolina, Chapel Hill, will discuss how protein dynamics, detected by NMR spectroscopy, can increase our understanding of communication within protein structures. A variety of local perturbations frequently lead to long-range propagation of dynamic effects. The role of internal protein fluctuations on timescales from picoseconds to milliseconds are explored in PDZ domains and other proteins. Lynne Regan, Yale Univ., and Brian Kuhlman, Univ. of North Carolina, Chapel Hill, will detail their work on the design of proteins to do whatever you want them to do - from metal binding and allosteric control to rewiring signal transduction pathways.
Single Molecules Visualization at the Level of Cellular Processes
In the past decade, single-molecule approaches have revolutionized biological inquiries and have provided previously unattainable data on elementary biological processes. However, most of the single-molecule studies have been limited to isolated single protein, RNA, and DNA molecules, yet these molecules do not function in isolation in the cell. To better emulate in vivo conditions, we need to study more-complex systems. Sunney Xie, Harvard Univ., will describe the extension of these studies to single cells visualizing such processes as gene expression, transcription factor dynamics and motor proteins stepping in living cells. Taekjip Ha, Univ. of Illinois, U-C, will discuss his work on pushing single-molecule techniques to the extreme (e.g., ultrahigh spatiotemporal resolution, multicolor fluorescence, vesicle encapsulation, fluorescence and force combination) to dramatically extend the reach of methods used to study molecules that are important in maintaining the stability of the genome and in preventing serious threats to human health. Bruno Samori, Univ. of Bologna, Italy, will directly address the problem of untreatable neurodegenerative human disorders, like Parkinson?s, Alzheimer?s, and prion diseases, which are associated with the aggregation of misfolded or natively unfolded proteins into amyloid fibrils. His studies of the conformational equilibria of these intrinsically unstructured proteins are expected to lead to drugs to treat such diseases. Mark C Williams, Northeastern Univ., will describe his use of DNA manipulation experiments to control the rate at which ligands bind to DNA as well as the overall equilibrium fractional ligand binding. This information is in turn used to characterize the DNA interactions of replication proteins from bacterial and viral systems, including bacteriophages and retroviruses. Liviu Movileanu , Syracuse Univ., will discuss his work on engineered protein nanopores, to detect, examine, and characterize proteins, DNA and their assemblies at high temporal and spatial resolutions.
Innovation: Structure of Transients to Synthetic Biology
Among the interesting recent innovations are the direct detection and structure determination of transient intermediates, laboratory synthesis of chemical nucleases, and light powered E. coli bacterium. Marius Clore, NIH, employs paramagnetic relaxation enhancement to detect, characterize and visualize low population transient species, thereby exploring regions of the free energy landscape of biological macromolecular systems (such as protein-protein and protein-DNA complexes) that are inaccessible to conventional structural and biophysical techniques. Elena Bichenkova, Univ. of Manchester, UK, will present a new type of chemical nuclease, showing very unusual catalytic and structural properties. These novel oligonucleotide-mediated chemical nucleases were constructed by conjugating short, catalytically inactive oligopeptides containing alternating basic and hydrophobic amino acids with an oligonucleotide component. The most remarkable feature of these novel biocatalysts was that the conjugation of peptide and oligonucleotide seems to produce a new hybrid that synergistically combines the individual properties of the two components to yield a new and unusual catalytic ability. Jan Liphardt, UC, Berkeley, will describe his work on how synthesized light powered and controlled forms of the E. coli bacterium help us understand the conversion of light into mechanical work in biological systems. The images on the left shows a single E. coli cell that is stuck to a surface(red) and rotates when illuminated with green light (green). The cell uses the Proteorhodopsin light powered pump to harvest photons, creating a proton-motive-force that, in turn, drives the flagellar motor.
Ned Seeman's DNA Nanotechnology Session
While growing up here at SUNY at Albany, Ned Seeman invented the DNA nanotechnology from the inspiration he derived from the Edward Durrel Stone architecture of the University. Now William Shih, Harvard Univ., is using it to build molecular transporter machines. He will describe how this machine, built by the scaffolded DNA origami method, has the shape of a tripod, consisting of a 30 nm wide hexagonal core with a 6 nm wide central feedthrough and bearing three 400 nm long stiff tubes. The tubes are fastened to the core by hinges that enable uniaxial rotation of the tubes constrained to a 90 degree range. Hanadi Sleiman, McGill Univ., will delineate a new approach that combines the concepts of supramolecular chemistry with the programmability of DNA, to direct the organization of functional components, one by one, into 2 & 3D structures. Thus, 2D dynamic scaffolds, 3D DNA cages with full modularity of geometry and ready switching of the cavity size, DNA nanotubes, metal-DNA 3D frameworks, and DNA extended fibers have been constructed. In addition, Hanadi, shows how the addition of an external small molecule guest can be used to dramatically modify the outcome of DNA self-assembly, in some cases altering the conventional Watson-Crick code of DNA association, into new structures of higher molecularity than the DNA double helix. Yamuna Krishnan, NCBS, Bangalore, India, will describe how unusual non-B-DNA motifs can be used to build rigid scaffolds and molecular switches, and how these DNA scaffolds may be used as powerful probes to interrogate living cells and whole organisms.
Macromolecular complexes: cryo-electron microscopy & tomography
Wah Chiu, Baylor College of Medicine, will discuss how single particle cryo-EM and novel modeling methods are employed to yield C-alpha backbone traces of molecular components in an assembly in different functional states. Martin Beck, ETH, Switzerland, will describe a hybrid approach of quantitative mass spectrometry and cryo-electron tomography to determine the molecular anatomy of the human pathogen Leptospira interrogans. The cellular concentration of proteins covering 62% of the open reading frames was determined by selected reaction monitoring and MS1 feature extraction. These data have been used to interpret cryo-electron tomograms at the molecular level with a focus on bacterial stress response and the motility system. Ohad Medalia, Ben Gurion Univ., Israel, will show the 3D molecular organization of integrin-mediated cell adhesion as revealed by cryo-electron tomography of intact mammalian cells. By means of correlating fluorescent and cryo-EM, he identifies Fas(?) and acquires 25 tomograms that are analyzed in 3D.



The positioning of nucleosomes on DNA controls the ability of the cellular machinery to access genetic messages. Generally, the messages become silent when and where the DNA wraps around the histones to form stable nucleosomes, and active when nucleosomes reposition by dynamically and reversibly sliding over the DNA. It is thought that enzymes and cofactors are recruited to regulate gene expression by modifying the DNA and histones via nucleosome repositioning. Correctly predicting the positioning of the nucleosome is accordingly linked to the 'activity' of the cell. Nucleosome positioning is driven primarily by sequence-dependent physicochemical properties of DNA (deformable versus 'rigid' sequences) and electrostatic interactions between the negatively charged DNA and the positively charged histone proteins (differences in charge build-up on AT-rich versus GC-rich sequences). The details of this sequence dependence are still to be clarified.

Given the increased interest in the subject, we are organizing a satellite workshop to be held immediately following the Conversation, at 2:00 pm on Saturday, June 20th 2009.

The discussion will focus on several issues: DNA sequence patterns responsible for nucleosome positioning (NP); comparisons between NP sequence patterns observed in vivo and in vitro; deformational characteristics of DNA sequences that attract and repel nucleosomes; NP predictions with single nucleotide precision, and; the possible role of linker histones and higher-order chromatin structure on NP. The format of the Workshop will be a round-table discussion with 10-15 min presentations followed by informal discussions. The following investigators have agreed to participate in the workshop: Tom Bishop, Tulane Univ., David Clark, NIH, Feng Cui, NIH, Pasquale De Santis, Univ. of Rome, Italy, Steve Johnson, Stanford Univ., Wilma Olson, Rutgers Univ., Frank Pugh, Pennsylvania State Univ., Eran Segal, Weizmann, Rehovot, Israel, and Edward Trifonov, Univ. of Haifa, Israel. Victor Zhurkin, NIH, will act as a chair and provide the necessary navigation for the workshop. All participants are encouraged to present posters during the poster session, which will be held 1-2 days prior to the Workshop. If you are working in this area, we encourage you to share your research results and thoughts with us. You may do so by presenting a poster; in addition, you can request time to present your results orally.

Speakers, Chairs & Guests asof August 6 2008

Abgaryan, Lucy, Yeravan State Univ., Armenia
Adams, Claire, Univ. of Kentucky
Aravind, L., NCBI, NIH
Artamonova, Irena, Vavilov Insti., Moscow, Russia
Arya, Gaurav, UCSD
Atkinson, Gemma, Uppsala University
Avihoo, Assaf, Ben-Gurion Univ., Beer-Sheva, Israel
Bairagya, Hridoy, NIT-Durgapur, India
Balasubramanian, Harish, Princeton, Univ.
Baldwin, Geoff, Imperial College, London UK
Banas, Pavel, IBP, Brno, CZ
Barvik Jr, Ivan, Charles Univ., Czech Republic
Bass, Brenda, Univ. of Utah
Baylin, Stephen, Johns Hopkins School of Medicine
Beck, Martin, ETH, Switzerland
Besseovs, Ivana, Acad. Sci. Czech Republic
Bichenkova, Elena, Univ. of Manchester, UK
Bishop, Tom, Tulane Univ.,
Bolshoy, Alexander, Haifa, Israel
Borek, Dominika, UTSW Med. Ctr, Dallas TX
Bowman, Gregory, Johns Hopkins
Brahmachari, Samir, CSIR, Delhi, India
Callahan, Brian, Wadsworth Center
Carneiro, Karina, McGill Univ., Montreal Canada
Chattopadhyaya, Rajagopal, Bose Institue,, India
Chaurasiya, Kathy, Northeastern Univ.,
Chen, Huiyi, Harvard
Cheng, Chia-Ho, Univ. of Mass, Lowell
Chiu,Wah, Baylor College of Medicine
Ciengshin, Tanashaya, NYU
Cingolani, Gino, Upstate SUNY
Clark, David, NIH,
Clore, Marius, NIH
Cohanim, Amir, Technion, Israel,
Coller, Jeff, Case Western Reserv Univ.
Corey, David, Univ. of Texas,SW Medical Center, Dallas
Cowsik, Sudha, JNU, New Delhi, India
Cui, Feng, NIH.,
Dalyan, Yeva, Yerevan State Univ., Armenia
Das, Subha, Carnegie Mellon Univ.
De Santis, Pasquale, Univ. of Rome, Italy,
Del Sol, Antonio, Fujirebio, Tokyo, Japan
Delaney, Sarah, Brown Univ.
Di Mauro, Ernesto, Univ. of Rome, Italy
Dror, Oranit, Tel Aviv Univ., Israel
Dunker, Keith, IUPUI,
Egorova, Vera, Tufts University
Engelhart, Aaron E, Georgia Tech
Esguerra, Mauricio, Rutgers Univ.
Fedorova, Olga, ICB, Novosibirsk, Russia
Field, Yair, Weizmann, Israel
Filippova,, Galina, Fred Hutchinson Cancer Center
Fire, Andrew, Stanford Univ. , Nobel Laureate
Frank, Joachim, Columbia Univ.
Frank-Kamenestskii, Maxim, Boston Univ.
Friedman, Simon, Univ. of Missouri, Kansas City
Fu, Jie, Columbia
Gabdank, Idan, Ben Gurion University, Israel
Gelfand, Mikhail, IITP, Moscow, Russia
Gevorgyan, Hayk, Yerevan State Univ. Armenia
Gojobori, Takashii, NIG, Mishima, Japan
Grigoryev, Sergei, Pennsylvania State Univ., Hershey
Gu, Hongzhou, NYU
Guéroult, Marc, Univ. Paris Diderot-Paris, France
Gunasekera, Kenneth, Princeton
Gupta, Goutam, Los Alamos Natl laboratory
Gursky, Georgy, Engelhardt Institute, Moscow, Russia
Ha, Taekjip Univ. of Illinois, Urbana-Champaign
Hansen, Jeffrey, Colorado State Univ.
Haran, Tali, Technion, Israel
Harding, Stephanie, Univ. of Rochester
Hashem, Yaser, Univ. Louis Pateur, Paris, France
Hauryliuk, Vasili, Univ. of Tartu, Estonia
Heinemann, Udo, M D C for Molecular Medicine, Berlin, Germany
Hellman, Lance, Univ. of Kentucky
Herschlag, Dan, Stanford Univ.
Hickman, Alison NIH
Honig, Barry, Columbia Univ.
Hsu, Danny, Univ. of Cambridge, UK
Huang, Yuegao, Wesleyan Univ.
Hud, Nick, Georgia Tech
Islam, Maidul Md., IICB, Kolkata, India
Jain, Kumkum, IIT Delhi, India
Jernigan, Robert, University of Iowa
Ji, Liang-nian, Sun Yatsen Univ., China
Jiang, Cizhong, Pennsylvania State Univ.
Johansson, Magnus, Univ. of Uppsala, Sweden
Johnson, Steve, Stanford Univ.
Kallenbach, Neville, NYU
Kasprzak, Wojciech, NIH
Kim, Taejin, NIH
Krishnan, Yamuna, NCBS, Bangalore, India
Krzyzosiak, Wlodzimierz, Polish Academy of Science, Poznan, Poland
Kuhlman, Brian, Univ. of North Carolina, Chapel Hill
Laederach, Alain, Wadsworth Center
Lando, Dmitri, Natl. Acad. Sci., Minsk, Belarus
Lee, Andrew, Univ. of North Carolina, Chapel Hill
Leith, Jason, Harvard
Leontis, Neocles, Bowling Green State Univ.
Li, Dadong, NYU
Li, Hong, Florida State Univ, Tallahasse
Li, Wen, Columbia Univ.
Li, Yuhang, NYU
Liphardt, Jan, UC Berkeley
Liu, Peng, Columbia Univ.,
Liu, Wenyan, NYU
Lilley, David, University of Dundee, UK
Lo, Pik Kwan Peggy, McGill Univ., Montreal Canada
Lobachev, Kirill, Georgia Tech
Lukin, Mark, SUNY Stony Brook
Ly, Danith., Carnegie Mellon
Madhusudhan, M S, Bioinformatics Institute, Singapore
Mankin, Alexander, Univ. of Illlinois, Chicago
Marky, Luis, Univ. of Nebraska Medical Center
Marx, Kenneth, Univ. Mass., Lowell
McCauley, Micah, Northeastern Univ.,
McKnight, Jeffrey, Johns Hopkins Univ.
Medalia, Ohad, Ben Gurion Univ., Beer-Sheva , Israel
Meister, Vesely, FloraMera Halle a.d. Saale, Germany
Melikishvili, Manana, Univ. of Kentucky
Mirkin, Sergei, Tufts Univ.
Moreno, Andrew, Wesleyan Univ.
Morgunov, Igor, RAS, Pushchino, Russia
Morii, Takashi, Kyoto Univ., Kyoto, Japan
Morozov, Alexandre, Rutgers
Movileanu , Liviu , Syracuse Univ
Mozziconacci, Julien, Univ. Pierre et Marie Curie, Paris, France
Mukerji, Ishita, Wesleyan Univ
Neira, Mauricio Esguerra, Rutgers
Niazi, Farshad, Case Western Reserve Univ.
Nowacki, Mariusz, Princeton
Nussinov , Ruth, Tel Aviv Univ., Tel Aviv, Israel
Ogura, Atsushi, Ochanomizu Univ., Tokyo, Japan
Oldfield, Chris, IUPUI
Olson, Wilma, Rutgers Univ.,
Otwinowski, Zbyszek, UTSW Med. Ctr, Dallas TX
Padmavathi, P., Univ. of Hyderabad, India
Paramanathan, Thayaparan, Northeastern Univ.,
Pieniazek, Susan, Wesleyan
Petrov, Valey V., IBPM, RAS, Pushchino, Moscow, Russia,
Pradhan, S. Kalyan, Saha Institute of Nuclear Physics, Kolkata, India,
Pugh, Frank, Pennsylvania State Univ.,
Puranik, Mrinalini, NCBS, Bangalore, India
Pyle, Anna Marie, Yale Univ.
Rajeswari, Moganty, AIIMS, New Delhi, India
Reblova, Kamila, IBP, Brno, Czech Republic
Reddy, Vijay, Queens College, CUNY,
Regan, Lynne, Yale Univ.
Reuter, Jessica, Univ. of Rochester
Reyes, Vincente, Rochester Insti. of Tech.
Rhodes, Daniela , MRC, LMB,, Cambridge UK
Rice, Phoebe, Univ. of Chicago
Rich, Alex, MIT,
Rodnina, Marina, MPI Goettingen, Germany
Rohs, Remo, Columbia Univ.
Ruben, George, Univ. of New Hampshire
Rueda, David, Wayne State Univ.
Saenger, Wolfram, Univ. of Berlin, Berlin, Germany
Safro, Mark, Weizmann, Israel
Samori, Bruno, Univ. of Bologna, Italy
Sanyal, Suparna, Univ. of Uppsala, Sweden
Sarai, Akinori, Kyushu Institute of Technology, Iizuka, Japan
Satyanarayanajois, Seetharama, Univ. of Louisiana
Scipioni, Anita, University of Rome, Italy
Seeman, Ned, NYU
Segal, Eran, Weizmann, Rehovot, Israel,
Severinov, Konstantin , Rutgers Univ.
Sgourakis, Nikolaos, RPI
Sha, Ruojie, NYU
Shah, Kartik, Tufts Univ.
Shakked, Zippi, Weizmann, Israel
Shapiro, Bruce, NIH, NCI,
Sheetin, Matthew, Univ. of Rochester
Shih, William, Harvard Univ
Shishkin, Alexander, Tufts Univ.
Sidorova, Nina, NIH
Singh, Poonam, CDRI, Lucknow, India
Singh, Sanjeev Kumar, Madurai Kamraj Univ., India
Sleiman, Hanadi, McGill Univ
Soler, Montserrat, , IRB, Barcelona, Spain
Sorokin, A. A., Univ. of Edinburg, UK
Sponer, Jiri, IBP, Brno, CZ
Stanov, Dontcho, Imperial College, London UK
Stellwagen, Nancy, Univ. of Iowa
Strawn, Rebecca, Princeton
Stumph, William, San Diego State Univ.,
Subramanian, Harikrishnan Krishnaswamy, NYU
Sugiyama, Hiroshi, Kyoto Univ., Japan
Suzuki, Ikuo, NIG, Mishima, Japan,
Tajmir Riahi, H. A., UQTR, Canada
Thomson, James Univ. of Wisconsin, School of Medicine
Timsit, Youri, IBPC, Paris, France
Tolstorukov, Michael Y., Harvard Univ.,
Tomita, Masaru, Keio Univ., Fujisawa, Japan
Travers, Andrew, MRC, LMB, Cambridge, UK
Trifonov, Edward, Univ. of Haifa, Israel.
Tullius, Tom, Boston University
Udomprasert, Anuttara, NYU
Ulyanov, Nikolai, UCSF
Uversky, Vladimir, IUPUI,
Valadkhan, Saba, Case Western Reserve Univ.
Van Ingen, Hugo, Univ. of Toronto, Canada
Van Nostrand, Keith, Univ. of Rochester
Vasquez, Karen, Univ. of Texas, M D Anderson Cancer Center
Vijayalakshmi, M., NCBS, Bangalore, India
Vishveshwara, Saraswathi, IISc, Bangalore, India
Vologodskii, Alexander, NYU
Vorobjev, Yuri, ICB, Novosibirsk, Russia
Wagner, Gerhart, Univ. of Uppsala, Sweden
Wang. Tong, NYU
Waring, Michael, Univ. of Cambridge, UK
West, Sean, Columbia Univ.
Westhof, Eric, Univ. of Strasbourg, France
Wijmenga, Sybren, Radboud University Nijmegen, The Netherlands
Williams, Mark, Northeastern Univ.
Wolberger, Cynthia, Johns Hopkins School of Medicine
Xia, Ke, RPI
Xie, Sunney, Harvard Univ.
Yamana, Kazushige, Univ. of Hyogo, Himeji, Japan
Yang Hui-ying, Sun Yatsen Univ., China
Yeo, Gene, Salk Institute
Yonath, Ada, Weizmann, Israel
Zakrzewska, Krystyna, IBCP, Lyon, France
Zhai, Jie, Wesleyan
Zhao, Xinshuai, NYU
Zhang, George Junjie, Baylor College of Med.
Zhang, Songjie, RPI
Zhang, Yu., Georgia Tech
Zheng, Jianping, NYU
Zhurkin, Victor, NIH
Zlatanova, Jordanka Univ. of Wyoming
Zu, Zhenjiang, Univ. of Rochester,
Ramaswamy H. Sarma