Výsledky vyhledávání - "Karl Malakian"

Structural Basis for the Immunogenic Properties of the Meningococcal Vaccine Candidate LP2086

Autor: Elena G. Novikova, Jaison Jacob, Alessandro Mascioni, Karl Malakian, Franklin J. Moy, Yingxia Wen, Mininni Terri L, Pamela Fink, Rosaria Camarda, Susan K. Hoiseth, Deborah A. Dilts, Shuo L. Lin, Ellen Murphy, Scott Sigethy, Gary W. Zlotnick, Breagh E. Bentley, Lisa K. McNeil, Viktoria Gusarova, Désirée H. H. Tsao

Publikováno v: Journal of Biological Chemistry. 284:8738-8746

LP2086 is a family of outer membrane lipoproteins from Neisseria meningitidis, which elicits bactericidal antibodies and are currently undergoing human clinical trials in a bivalent formulation where each antigen represents one of the two known LP208

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8413724cf730643fe45e47ec0e1e0635
https://doi.org/10.1074/jbc.m808831200

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Characterization of Protein Kinase C θ Activation Loop Autophosphorylation and the Kinase Domain Catalytic Mechanism

Autor: Lin Liu, Ron Kriz, Rita Greco, Mark Stahl, Karl Malakian, Divya Chaudhary, Robert M. Czerwinski, Laura Lin, Scott Wolfrom, Ann Aulabaugh, Stephane Olland, Ying Huang

Publikováno v: Biochemistry. 44:9563-9573

Protein kinase C theta (PKCtheta), a member of the Ca(2+)-independent novel subfamily of PKCs, is required for T-cell receptor (TCR) signaling and IL2 production. PKCtheta-deficient mice have impaired Th2 responses in a murine ova-induced asthma mode

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::38970adad106eea6b854349f8f0ae93e
https://doi.org/10.1021/bi050608q

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Structure-Based Design of Estrogen Receptor-β Selective Ligands

Autor: Chu-Lai Hsiao, Ramesh A. Bhat, Rayomand J Unwalla, Zhang B. Xu, Karl Malakian, William S. Somers, Tatos N. Akopian, Wah-Tung Hum, Heather A. Harris, Eric S. Manas, Michael S. Malamas, Juan C. Alvarez, Ashok R. Bapat, Scott Wolfrom, Chris P. Miller, Mark Stahl

Publikováno v: Journal of the American Chemical Society. 126:15106-15119

We present the structure-based optimization of a series of estrogen receptor-beta (ERbeta) selective ligands. X-ray cocrystal structures of these ligands complexed to both ERalpha and ERbeta are described. We also discuss how molecular modeling was u

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e8fb882810df1e98eddbab62daae6f1a
https://doi.org/10.1021/ja047633o

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Catalytic Domain Crystal Structure of Protein Kinase C-θ (PKCθ)

Autor: Christina Benander, William S. Somers, Laura Lin, Mark Stahl, Diane Joseph-McCarthy, Karl Malakian, Rita Greco, Stephane Olland, Lori Fitz, Lidia Mosyak, Robert M. Czerwinski, Zhang-Bao Xu, Scott Wolfrom, Divya Chaudhary

Publikováno v: Journal of Biological Chemistry. 279:50401-50409

A member of the novel protein kinase C (PKC) subfamily, PKCθ, is an essential component of the T cell synapse and is required for optimal T cell activation and interleukin-2 production. Selective involvement of PKCθ in TCR signaling makes this enzy

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ffec59ab2a6376bd6ad4fb5f33aab08b
https://doi.org/10.1074/jbc.m409216200

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Two N-Terminal Domains of Kv4 K+ Channels Regulate Binding to and Modulation by KChIP1

Publikováno v: Neuron. 41:587-598

The family of calcium binding proteins called KChIPs associates with Kv4 family K + channels and modulates their biophysical properties. Here, using mutagenesis and X-ray crystallography, we explore the interaction between Kv4 subunits and KChIP1. Tw

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f50525e0eddc63de4b13bdb0e126666c
https://doi.org/10.1016/s0896-6273(04)00049-2

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Catalytically Active MAP KAP Kinase 2 Structures in Complex with Staurosporine and ADP Reveal Differences with the Autoinhibited Enzyme

Autor: Kristine Svenson, Kevin D. Parris, Robert M. Czerwinski, Elizabeth Federico, Scott Wolfrom, Jasbir Seehra, Jean-Baptiste Telliez, William S. Somers, Michelle Maguire, Karl Malakian, Mark Stahl, Ronald W. Kriz, Kathryn W. Underwood, Chu-Lai Hsiao, Tania Shane, Lih-Ling Lin, Meggin Taylor, Yan Liu, Lidia Mosyak

Publikováno v: Structure. 11(6):627-636

MAP KAP kinase 2 (MK2), a Ser/Thr kinase, plays a crucial role in the inflammatory process. We have determined the crystal structures of a catalytically active C-terminal deletion form of human MK2, residues 41–364, in complex with staurosporine at

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::097acf64f2226a080302c56bfbe63f41

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Solution Structure of N-TRADD and Characterization of the Interaction of N-TRADD and C-TRAF2, a Key Step in the TNFR1 Signaling Pathway

Autor: Thomas McDonagh, Jean-Baptiste Telliez, Karl Malakian, Guang-Yi Xu, Sang Hsu, Lih-Ling Lin, Désirée H. H. Tsao

Publikováno v: Molecular Cell. 5(6):1051-1057

TRADD is a multifunctional signaling adaptor protein that is recruited to TNFR1 upon ligand binding. The C-terminal of TRADD comprises the "death domain" that is responsible for association of TNFR1 and other death domain-containing proteins such as

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::692adb84c7552827940f6904a1921e97

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NMR dynamics and antibody recognition of the meningococcal lipidated outer membrane protein LP2086 in micellar solution

Autor: Desiree H.H. Tsao, Alessandro Mascioni, Franklin J. Moy, Viktoria Gusarova, Shuo Lin, Deborah A. Dilts, Scott Sigethy, Karl Malakian, Lisa K. McNeil, Pamela S. Fink, Ellen Murphy, Gary W. Zlotnick, Susan K. Hoiseth, Elena G. Novikova, Breagh E. Bentley, Mininni Terri L, Rosaria Camarda

Publikováno v: Biochimica et biophysica acta. 1798(2)

Neisseria meningitidis is a major cause of meningitis. Although protective vaccination is available against some pathogenic serogroups, serogroup B meningococci have been a challenge for vaccinologists. A family of outer membrane lipoproteins, LP2086

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::325ba3505abfeafd44bebed1974c3bbe
https://pubmed.ncbi.nlm.nih.gov/19835839

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Solution structure of wild-type human matrix metalloproteinase 12 (MMP-12) in complex with a tight-binding inhibitor

Autor: Brian Dwyer, Michelle A. Markus, Karl Malakian, Scott Wolfrom, Jianchang Li, Wei Li, Désirée H. H. Tsao, James E. Wilhelm

Publikováno v: Journal of biomolecular NMR. 41(1)

MMP-12 (macrophage elastase) is a member of a family of proteases that target proteins of the extracellular matrix. Matrix metalloproteinases (MMPs) influence tissue remodeling both in healthy growth and development and in the progression of patholog

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4ae61de7192e2bf46ec7f558e982ca58
https://pubmed.ncbi.nlm.nih.gov/18425585

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