Institution
Torrey Pines Institute for Molecular Studies
Nonprofit•San Diego, California, United States•
About: Torrey Pines Institute for Molecular Studies is a nonprofit organization based out in San Diego, California, United States. It is known for research contribution in the topics: T cell & Antigen. The organization has 2323 authors who have published 2217 publications receiving 112618 citations.
Topics: T cell, Antigen, Solid-phase synthesis, Cytotoxic T cell, Peptide
Papers published on a yearly basis
Papers
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National and Kapodistrian University of Athens1, Harvard University2, Rice University3, University of British Columbia4, University of Peloponnese5, Torrey Pines Institute for Molecular Studies6, University of Cyprus7, University of New Mexico8, University of Chicago9, Purdue University10, University of Pennsylvania11, City College of New York12, City University of New York13, Reading Hospital14
TL;DR: The benefits, challenges, and opportunities of using antimicrobial peptides against multidrug-resistant pathogens are identified, advances in the deployment of novel promising antimacterial peptides are highlighted, and the needs and priorities in designing focused development strategies taking into account the most advanced tools available are underlined.
Abstract: Accelerating growth and global expansion of antimicrobial resistance has deepened the need for discovery of novel antimicrobial agents. Antimicrobial peptides have clear advantages over conventional antibiotics which include slower emergence of resistance, broad-spectrum antibiofilm activity, and the ability to favourably modulate the host immune response. Broad bacterial susceptibility to antimicrobial peptides offers an additional tool to expand knowledge about the evolution of antimicrobial resistance. Structural and functional limitations, combined with a stricter regulatory environment, have hampered the clinical translation of antimicrobial peptides as potential therapeutic agents. Existing computational and experimental tools attempt to ease the preclinical and clinical development of antimicrobial peptides as novel therapeutics. This Review identifies the benefits, challenges, and opportunities of using antimicrobial peptides against multidrug-resistant pathogens, highlights advances in the deployment of novel promising antimicrobial peptides, and underlines the needs and priorities in designing focused development strategies taking into account the most advanced tools available.
432 citations
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TL;DR: An enzyme derepression assay is developed, based on overcoming XIAP-mediated suppression of Caspase-3, and mixture-based combinatorial chemical libraries are screened for compounds that reversed XI AP-mediated inhibition of Cazase- 3, identifying a class of polyphenylureas with XIAP -inhibitory activity.
427 citations
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Ludwig Institute for Cancer Research1, University of California, San Diego2, Mayo Clinic3, National University of Singapore4, Torrey Pines Institute for Molecular Studies5, Slovak Academy of Sciences6, Katholieke Universiteit Leuven7, National Institutes of Health8, Children's Hospital Oakland Research Institute9, German Center for Neurodegenerative Diseases10, King's College London11
TL;DR: Single-dose injection of antisense oligonucleotides (ASOs) that target repeat-containing RNAs but preserve levels of mRNAs encoding C9ORF72 produced sustained reductions in RNA foci and dipeptide-repeat proteins, and ameliorated behavioral deficits.
421 citations
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TL;DR: Mutation of putative CDK phosphorylation sites, at least five of which are phosphorylated in vivo, strongly reduces SBF-dependent transcription and delays cell cycle initiation and, like mammalian Rb, Whi5 is a G1-specific transcriptional repressor antagonized by CDK.
421 citations
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TL;DR: A method for identifying and quantifying protein kinases in any biological sample or tissue from any species using acyl phosphate-containing nucleotides and direct competition between probes and inhibitors can be assessed to determine inhibitor potency and selectivity against nativeprotein kinases, as well as hundreds of other ATPases.
Abstract: The central role of protein kinases in signal transduction pathways has generated intense interest in targeting these enzymes for a wide range of therapeutic indications. Here we report a method for identifying and quantifying protein kinases in any biological sample or tissue from any species. The procedure relies on acyl phosphate-containing nucleotides, prepared from a biotin derivative and ATP or ADP. The acyl phosphate probes react selectively and covalently at the ATP binding sites of at least 75% of the known human protein kinases. Biotinylated peptide fragments from labeled proteomes are captured and then sequenced and identified using a mass spectrometry-based analysis platform to determine the kinases present and their relative levels. Further, direct competition between the probes and inhibitors can be assessed to determine inhibitor potency and selectivity against native protein kinases, as well as hundreds of other ATPases. The ability to broadly profile kinase activities in native proteomes offers an exciting prospect for both target discovery and inhibitor selectivity profiling.
411 citations
Authors
Showing all 2327 results
Name | H-index | Papers | Citations |
---|---|---|---|
Eric J. Topol | 193 | 1373 | 151025 |
John R. Yates | 177 | 1036 | 129029 |
George F. Koob | 171 | 935 | 112521 |
Ian A. Wilson | 158 | 971 | 98221 |
Peter G. Schultz | 156 | 893 | 89716 |
Gerald M. Edelman | 147 | 545 | 69091 |
Floyd E. Bloom | 139 | 616 | 72641 |
Stuart A. Lipton | 134 | 488 | 71297 |
Benjamin F. Cravatt | 131 | 666 | 61932 |
Chi-Huey Wong | 129 | 1220 | 66349 |
Klaus Ley | 129 | 495 | 57964 |
Nicholas J. Schork | 125 | 587 | 62131 |
Michael Andreeff | 117 | 959 | 54734 |
Susan L. McElroy | 117 | 570 | 44992 |
Peter E. Wright | 115 | 444 | 55388 |