Institution
Agilent Technologies
Company•Santa Clara, California, United States•
About: Agilent Technologies is a company organization based out in Santa Clara, California, United States. It is known for research contribution in the topics: Signal & Mass spectrometry. The organization has 7398 authors who have published 11518 publications receiving 262410 citations. The organization is also known as: Agilent Technologies, Inc..
Topics: Signal, Mass spectrometry, Laser, Amplifier, Analog signal
Papers published on a yearly basis
Papers
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TL;DR: In this article, the removal of sulfachloropyridazine (4-amino-N -(6- Cl -3-pyridazinyl)benzene sulfonamide) antibiotic from water by adsorption on a high silica mordenite with channel window dimension comparable to that of the antibiotic, and with a significant concentration of internal silanol groups due to the dealumination process was investigated.
59 citations
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TL;DR: This SPE-IMS-MS platform overcomes many of the current challenges of large-scale metabolomic and exposomic analyses and offers a viable option for population and patient cohort screening in an effort to gain insights into disease processes and human environmental chemical exposure.
59 citations
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TL;DR: The use of more extended competition experiments appear promising and suggest that it may be possible to determine dissociation rate constants for high affinity afucosylated antibodies without the need to purify or express such variants.
Abstract: FcγRs play a critical role in the immune response following recognition of invading particles and tumor associated antigens by circulating antibodies. In the present study we investigated the role of FcγR glycosylation in the IgG interaction and observed a stabilizing role for receptor N-glycans. We performed a complete glycan analysis of the recombinant FcγRs (FcγRIa, FcγRIIa, FcγRIIb, FcγRIIIaPhe158/Val158, and FcγRIIIb) expressed in human cells and demonstrate that receptor glycosylation is complex and varied between receptors. We used surface plasmon resonance to establish binding patterns between rituximab and all receptors. Complex binding was observed for FcγRIa and FcγRIIIa. The IgG–FcγR interaction was further investigated using a combination of kinetic experiments and enzymatically deglycosylated FcγRIa and FcγRIIIaPhe158/Val158 receptors in an attempt to determine the underlying binding mechanism. We observed that antibody binding levels decreased for deglycosylated receptors, and at the same t...
59 citations
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15 May 2013TL;DR: In this paper, a method of processing a target RNA is provided, which comprises contacting the products of an RNA ligase-mediated ligation reaction with an CAS6 protein, wherein: (i) the target RNA, an RNA-ligase, and first and second adaptors that can ligate together to produce an adaptor dimer that contains a CRISPR stem loop; and (ii) the CAS-6 protein recognizes the CRisPR RNA stem-loop.
Abstract: A method of processing a target RNA is provided. In certain embodiments, this method comprises: contacting the products of an RNA ligase-mediated ligation reaction with an CAS6 protein, wherein: (i) the RNA ligase-mediated ligation reaction comprises: a target RNA, an RNA ligase, and first and second adaptors that can ligate together to produce an adaptor dimer that contains a CRISPR stem loop; and (ii) the CAS6 protein recognizes the CRISPR RNA stem-loop; thereby preventing the adaptor dimer from being reverse transcribed.
59 citations
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TL;DR: It is shown that serum withdrawal inhibits mTORC1 signaling, causes disassembly of translation initiation complexes, and causes mRNA redistribution from polysomes to subpolysomes in wild-type mouse embryo fibroblasts (MEFs), and implicates a discrete profile of deregulated mRNA translation in tuberous sclerosis pathology.
Abstract: The tuberous sclerosis complex (TSC) proteins TSC1 and TSC2 regulate protein translation by inhibiting the serine/threonine kinase mTORC1 (for mammalian target of rapamycin complex 1). However, how TSC1 and TSC2 control overall protein synthesis and the translation of specific mRNAs in response to different mitogenic and nutritional stimuli is largely unknown. We show here that serum withdrawal inhibits mTORC1 signaling, causes disassembly of translation initiation complexes, and causes mRNA redistribution from polysomes to subpolysomes in wild-type mouse embryo fibroblasts (MEFs). In contrast, these responses are defective in Tsc1(-/-) or Tsc2(-/-) MEFs. Microarray analysis of polysome- and subpolysome-associated mRNAs uncovered specific mRNAs that are translationally regulated by serum, 90% of which are TSC1 and TSC2 dependent. Surprisingly, the mTORC1 inhibitor, rapamycin, abolished mTORC1 activity but only affected approximately 40% of the serum-regulated mRNAs. Serum-dependent signaling through mTORC1 and polysome redistribution of global and individual mRNAs were restored upon re-expression of TSC1 and TSC2. Serum-responsive mRNAs that are sensitive to inhibition by rapamycin are highly enriched for terminal oligopyrimidine and for very short 5' and 3' untranslated regions. These data demonstrate that the TSC1/TSC2 complex regulates protein translation through mainly mTORC1-dependent mechanisms and implicates a discrete profile of deregulated mRNA translation in tuberous sclerosis pathology.
59 citations
Authors
Showing all 7402 results
Name | H-index | Papers | Citations |
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Hongjie Dai | 197 | 570 | 182579 |
Zhuang Liu | 149 | 535 | 87662 |
Jie Liu | 131 | 1531 | 68891 |
Thomas Quertermous | 103 | 405 | 52437 |
John E. Bowers | 102 | 1767 | 49290 |
Roy G. Gordon | 89 | 449 | 31058 |
Masaru Tomita | 76 | 677 | 40415 |
Stuart Lindsay | 74 | 347 | 22224 |
Ron Shamir | 74 | 319 | 23670 |
W. Richard McCombie | 71 | 144 | 64155 |
Tomoyoshi Soga | 71 | 392 | 21209 |
Michael R. Krames | 65 | 321 | 18448 |
Shabaz Mohammed | 64 | 188 | 17254 |
Geert Leus | 62 | 609 | 19492 |
Giuseppe Gigli | 61 | 541 | 15159 |