Zobrazeno 1 - 10
of 22
pro vyhledávání: '"Alex Smolyar"'
Autor:
Tomoko Hirozane-Kishikawa, Alex Smolyar, Nono Ayivi-Guedehoussou, Irma Lemmens, Fana Gebreab, Sebiha Cevik, Pascal Braun, Jin Sook Ahn, Michael E. Cusick, Haiyuan Yu, Christophe Simon, Huey Ling Kao, Niels Klitgord, Matija Dreze, David Szeto, Amélie Dricot, Marc Vidal, Jean Vandenhaute, Nicolas Simonis, Elizabeth Dann, Jean François Rual, Anne-Ruxandra Carvunis, Kristin C. Gunsalus, Mike Boxem, Chenwei Lin, Murat Tasan, Jan Tavernier, Changyu Fan, Anne Sophie de Smet, Frederick P. Roth, Tong Hao, David E. Hill, Kavitha Venkatesan, Muhammed A. Yildirim, Muneesh Tewari, Ning Li, Julie M. Sahalie, Stuart Milstein, Nicolas Bertin
Publikováno v:
Nature methods, 6 (1
To provide accurate biological hypotheses and elucidate global properties of cellular networks, systematic identification of protein-protein interactions must meet high quality standards.We present an expanded C. elegans protein-protein interaction n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::20e09315f3cc21038cb974affc204ac8
https://doi.org/10.1038/nmeth.1279
https://doi.org/10.1038/nmeth.1279
Autor:
Aurelio Pio Nardozza, Michele Tinti, Arnaud Ceol, Marc Vidal, Andrew Chatr-aryamontri, Daniele Peluso, Luisa Castagnoli, Gianni Cesareni, Alex Smolyar, Michael E. Cusick, Simona Panni, Francesca Sacco
Publikováno v:
Nucleic Acids Research
Understanding the consequences on host physiology induced by viral infection requires complete understanding of the perturbations caused by virus proteins on the cellular protein interaction network. The VirusMINT database (http://mint.bio.uniroma2.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1f87266bd47782b2feaeaac33016d5e4
http://europepmc.org/articles/PMC2686573
http://europepmc.org/articles/PMC2686573
Autor:
Carlene Fraughton, Debra S. Goldberg, Janghoo Lim, Lan V. Zhang, Gabriel F. Berriz, Christophe Simon, Francis D. Gibbons, Camille Bex, Alex Smolyar, Giovanni Franklin, Joanna S. Albala, Michael E. Cusick, Huda Y. Zoghbi, Estelle Llamosas, Amélie Dricot, Marc Vidal, Lynn Doucette-Stamm, Robert S. Sikorski, Philippe Lamesch, Matija Dreze, Mike Boxem, Niels Klitgord, Sharyl L. Wong, David E. Hill, Siming Li, Jean Vandenhaute, Tong Hao, Tomoko Hirozane-Kishikawa, Frederick P. Roth, Nono Ayivi-Guedehoussou, Jean François Rual, Sebiha Cevik, Jennifer Rosenberg, Kavitha Venkatesan, Stephanie Bosak, Reynaldo Sequerra, Ning Li, Stuart Milstein
Publikováno v:
Nature. 437:1173-1178
Systematic mapping of protein-protein interactions, or 'interactome' mapping, was initiated in model organisms, starting with defined biological processes and then expanding to the scale of the proteome. Although far from complete, such maps have rev
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::257d4664b18ddc1c9ca11f4e2fbc3131
https://doi.org/10.1038/nature04209
https://doi.org/10.1038/nature04209
Autor:
Rongguang Zhang, Lei Tang, Gerhard Wagner, Kemin Tan, Andrzej Joachimiak, Jin-huan Liu, Rebecca E. Hussey, Ellis L. Reinherz, Hsiu-Ching Chang, Petra Kern, Brian Hare, Yi Xiong, Alex Smolyar, Jia-huai Wang
Publikováno v:
Science. 286:1913-1921
The crystal structure of a complex involving the D10 T cell receptor (TCR), 16-residue foreign peptide antigen, and the I-Akself major histocompatibility complex (MHC) class II molecule is reported at 3.2 angstrom resolution. The D10 TCR is oriented
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::203dce9021a72859f1bff9daa635c7cc
https://doi.org/10.1126/science.286.5446.1913
https://doi.org/10.1126/science.286.5446.1913
Autor:
Alex Smolyar, Chung F. Wong
Publikováno v:
Journal of Molecular Structure: THEOCHEM. 488:51-67
In order to develop model parameters for simulating the spectroscopic properties of tryptophan and tyrosine in solutions and in proteins, we have carried out Hartree–Fock (HF) and configurational interaction (CI) calculations to study the electroni
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::91e30256a928740cd2dd2fd30cbb428e
https://doi.org/10.1016/s0166-1280(98)00627-7
https://doi.org/10.1016/s0166-1280(98)00627-7
Structure of a Heterophilic Adhesion Complex between the Human CD2 and CD58 (LFA-3) Counterreceptors
Autor:
Zhen-Yu J. Sun, Ellis L. Reinherz, Kemin Tan, Jia-huai Wang, Jin-huan Liu, Alex Smolyar, Mikyung Kim, Gerhard Wagner
Publikováno v:
Cell. 97(6):791-803
Interaction between CD2 and its counterreceptor, CD58 (LFA-3), on opposing cells optimizes immune recognition, facilitating contacts between helper T lymphocytes and antigen-presenting cells as well as between cytolytic effectors and target cells. He
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9dcb9c36e9fe45b25f6482a3d9c1253
Autor:
Hsiu-Ching Chang, Ellis L. Reinherz, Petra Kern, Rebecca E. Hussey, Jia-huai Wang, Mai-kun Teng, Jin-huan Liu, Rebecca Spoerl, Alex Smolyar, Ju Liu
Publikováno v:
Immunity. 9(4):519-530
The crystal structure of the two immunoglobulin variable-like domains of the murine CD8alphaalpha homodimer complexed to the class I MHC H-2Kb molecule at 2.8 A resolution shows that CD8alphaalpha binds to the protruding MHC alpha3 domain loop in an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b97618240f2ad76e59900ba43a289b61
Publikováno v:
The Journal of Experimental Medicine
A recent crystal structure of the N15 alpha/beta-T cell receptor (TCR) in complex with an Fab derived from the H57 Cbeta-specific monoclonal antibody (mAb) shows the mAb fragment interacting with the elongated FG loop of the Cbeta domain. This loop c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::065a4a3f2109c5c6bfe4197a27038f49
https://doi.org/10.1084/jem.187.9.1529
https://doi.org/10.1084/jem.187.9.1529
Publikováno v:
Biophysical Journal. 74:1087-1100
Small ligands generally bind within the seven transmembrane-spanning helices of G-protein-coupled receptors, but their access to the binding pocket through the closely packed loops has not been elucidated. In this work, a model of the extracellular l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::55d1e83efd215a3d8c8de5c7527d1d1b
https://doi.org/10.1016/s0006-3495(98)77827-0
https://doi.org/10.1016/s0006-3495(98)77827-0
Autor:
Stanley G. Nathenson, Jin-huan Liu, Alex Smolyar, Jia-huai Wang, M.-K. Teng, Hsiu-Ching Chang, Rebecca E. Hussey, Ellis L. Reinherz, A G Tse, J.-H. Liu
Publikováno v:
Current Biology. 8:409-414
Whether T-cell receptors (TCRs) recognize antigenic peptides bound to major histocompatability complex (MHC) molecules through common or distinct docking modes is currently uncertain. We report the crystal structure of a complex between the murine N1
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::11fbcf4e8520704ecee68bf9fd23f01e
https://doi.org/10.1016/s0960-9822(98)70160-5
https://doi.org/10.1016/s0960-9822(98)70160-5