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1.
Nat Commun ; 12(1): 457, 2021 01 19.
Article in English | MEDLINE | ID: mdl-33469031

ABSTRACT

Complex-valued neural networks have many advantages over their real-valued counterparts. Conventional digital electronic computing platforms are incapable of executing truly complex-valued representations and operations. In contrast, optical computing platforms that encode information in both phase and magnitude can execute complex arithmetic by optical interference, offering significantly enhanced computational speed and energy efficiency. However, to date, most demonstrations of optical neural networks still only utilize conventional real-valued frameworks that are designed for digital computers, forfeiting many of the advantages of optical computing such as efficient complex-valued operations. In this article, we highlight an optical neural chip (ONC) that implements truly complex-valued neural networks. We benchmark the performance of our complex-valued ONC in four settings: simple Boolean tasks, species classification of an Iris dataset, classifying nonlinear datasets (Circle and Spiral), and handwriting recognition. Strong learning capabilities (i.e., high accuracy, fast convergence and the capability to construct nonlinear decision boundaries) are achieved by our complex-valued ONC compared to its real-valued counterpart.

2.
Sci Rep ; 4: 3589, 2014 Jan 07.
Article in English | MEDLINE | ID: mdl-24395054

ABSTRACT

Over the last few decades, quantum chemistry has progressed through the development of computational methods based on modern digital computers. However, these methods can hardly fulfill the exponentially-growing resource requirements when applied to large quantum systems. As pointed out by Feynman, this restriction is intrinsic to all computational models based on classical physics. Recently, the rapid advancement of trapped-ion technologies has opened new possibilities for quantum control and quantum simulations. Here, we present an efficient toolkit that exploits both the internal and motional degrees of freedom of trapped ions for solving problems in quantum chemistry, including molecular electronic structure, molecular dynamics, and vibronic coupling. We focus on applications that go beyond the capacity of classical computers, but may be realizable on state-of-the-art trapped-ion systems. These results allow us to envision a new paradigm of quantum chemistry that shifts from the current transistor to a near-future trapped-ion-based technology.

3.
Plant Mol Biol ; 44(6): 711-21, 2000 Dec.
Article in English | MEDLINE | ID: mdl-11202434

ABSTRACT

Cytosolic acyl-CoA-binding proteins (ACBPs) are small proteins (ca. 10 kDa) that bind long-chain acyl-CoAs and are involved in the storage and intracellular transport of acyl-CoAs. Previously, we have characterized an Arabidopsis thaliana cDNA encoding a novel membrane-associated ACBP, designated ACBP1, demonstrating the existence of a new form of ACBP in plants (M.-L. Chye, Plant Mol. Biol. 38 (1998) 827-838). ACBP1 likely participates in intermembrane lipid transport from the ER to the plasma membrane, where it could maintain a membrane-associated acyl pool (Chye et al., Plant J. 18 (1999) 205-214). Here we report the isolation of cDNAs encoding ACBP2 (Mr 38,479) that shows conservation in the acyl-CoA-binding domain to previously reported ACBPs, and contains ankyrin repeats at its carboxy terminus. These repeats, which likely mediate protein-protein interactions, could constitute a potential docking site in ACBP2 for an enzyme that uses acyl-CoAs as substrate, in vitro binding assays on recombinant (His)6-ACBP2 expressed in Escherichia coli show that it binds 14[C]palmitoyl-CoA preferentially to 14[C]oleoyl-CoA. Analysis of the acyl-CoA-binding domain in ACBP2 was carried out by in vitro mutagenesis. Mutant forms of recombinant (His)6-ACBP2 with single amino acid substitutions at conserved residues within the acyl-CoA-binding domain were less effective in binding 14[C]palmitoyl-CoA. Northern blot analysis showed that the 1.6 kb ACBP2 mRNA, like that of ACBP1, is expressed in all plant organs. Analysis of the ACBP2 promoter revealed that, like the ACBP1 promoter, it lacks a TATA box suggesting the possibility of a housekeeping function for ACBP2 in plant lipid metabolism.


Subject(s)
Ankyrins/genetics , Arabidopsis Proteins , Arabidopsis/genetics , Carrier Proteins/genetics , Neoplasm Proteins , Palmitoyl Coenzyme A/metabolism , Plant Proteins , Repetitive Sequences, Nucleic Acid , Acyl Coenzyme A/metabolism , Amino Acid Sequence , Amino Acid Substitution , Binding Sites/genetics , Binding, Competitive , Blotting, Northern , Carbon Radioisotopes , Carrier Proteins/metabolism , DNA, Complementary/chemistry , DNA, Complementary/genetics , DNA, Complementary/isolation & purification , DNA, Plant/chemistry , DNA, Plant/genetics , Fatty Acid-Binding Proteins , Histidine/genetics , Molecular Sequence Data , Protein Binding , RNA, Messenger/genetics , RNA, Messenger/metabolism , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/metabolism , Sequence Alignment , Sequence Analysis, DNA , Sequence Homology, Amino Acid , Tissue Distribution
4.
Plant J ; 17(2): 203-8, 1999 Jan.
Article in English | MEDLINE | ID: mdl-10074717

ABSTRACT

The floral homeotic gene AGAMOUS (AG) imparts carpel identity on the fourth whorl of floral organs in wild-type Arabidopsis flowers. Less is known about the genes that regulate carpel patterning and differentiation. To identify cndidate regulators, we screened for genes expressed in developing carpels. Since Arabidopsis carpels are difficult to isolate, we used whole inflorescence apices of two floral homeotic mutants (pi and pi ag) and mRNA differential display, to identify carpel transcripts. Two of the resulting cDNA clones were shown to be expressed predominantly in flowers. They encoded AGL11, a MADS box transcription factor known to be expressed in the carpel and ovules, and a novel Arabidopsis endo-1,4-beta-D-glucanase (ATCEL2). In situ hybridisation localised the ATCEL2 transcript to the developing septum and ovule primordia of young carpels.


Subject(s)
Arabidopsis/genetics , Cellulase/genetics , Gene Expression Regulation, Developmental , Gene Expression Regulation, Plant , RNA, Messenger/genetics , Amino Acid Sequence , Arabidopsis/growth & development , Cellulase/chemistry , Cloning, Molecular , DNA, Complementary , In Situ Hybridization , Molecular Sequence Data , Sequence Homology, Amino Acid
5.
Plant J ; 7(6): 859-76, 1995 Jun.
Article in English | MEDLINE | ID: mdl-7599647

ABSTRACT

Genes encoding phenylalanine ammonia-lyase (PAL) are expressed in a complex pattern during plant development and in response to light, pathogen ingress, mechanical damage and other stresses. Analysis of the promoter of the bean PAL2 gene in transgenic tobacco has shown that some regions responsible for developmental expression are functionally compensatory. The minimum sequence containing all cis sequences necessary for developmental patterns of expression is within -254 bp of the transcription start site. Footprinting and electrophoretic mobility shift assay studies of this region revealed potential cis sequences which coincided with the functional domains defined by small deletions and promoter fusions. Mutations in these potential cis sequences in the context of the minimal -254 bp promoter altered tissue-specific expression patterns, confirming the importance of these sequences for expression in vivo. A functional model for the promoter is presented which predicts that three AC-elements, which are possible Myb protein binding sites, together with a G-box, interact to direct the complex patterns of tissue-specific expression observed.


Subject(s)
Nicotiana/genetics , Phenylalanine Ammonia-Lyase/genetics , Plants, Toxic , Promoter Regions, Genetic , Base Sequence , DNA, Plant/metabolism , DNA-Binding Proteins/genetics , DNA-Binding Proteins/metabolism , Genes, Plant , Molecular Sequence Data , Plants, Genetically Modified , Recombinant Fusion Proteins/genetics , Sequence Deletion
8.
Biochem Pharmacol ; 42(9): 1721-8, 1991 Oct 09.
Article in English | MEDLINE | ID: mdl-1718284

ABSTRACT

Trichosanthin (TCS) is a plant protein which has a wide spectrum of pharmacological activities. It was demonstrated recently that this compound suppressed the replication of human immunodeficiency virus (HIV-1) in vitro. The mechanism of action is believed to be inhibition of protein synthesis. Trichosanthin is a low molecular weight protein which is expected to be easily filtered and eliminated through the kidney. To minimize renal loss, the molecular size of trichosanthin can be increased by coupling to dextran. The larger complex will not undergo glomerular filtration and therefore renal loss can be prevented. This study investigates the kidney's role in trichosanthin elimination and the beneficial effect afforded by coupling to dextran in prolonging plasma half-life. For this purpose, a radioimmunoassay has been developed to determine the concentration of TCS in plasma and urine. The sensitivity of this assay is in the nanogram range. Trichosanthin was coupled to dextran T40 by a dialdehyde method and successful coupling was confirmed by gel filtration chromatography. The complex retained specific binding to trichosanthin antibodies with decreased affinity which can be partially reversed after incubation with dextranase; an enzyme that digested dextran. The pharmacokinetics of intravenously administered trichosanthin (0.75 mg/kg) was compared between two groups of rats with normal and impaired renal function (bilateral renal arterial ligation). Rats with ligation showed a decrease in plasma clearance from 4780 +/- 570 to 220 +/- 20 microL/min and an increase in the mean residence time from 9 +/- 1 to 145 +/- 16 min. Despite the several-fold difference in these parameters, recovery of trichosanthin from normal rat urine was only 0.38 +/- 0.05%. This value can be increased by using higher injection doses. The data indicate that the kidney is an important organ for the elimination of trichosanthin. When the dextran-trichosanthin complex was injected into normal rats trichosanthin activity was not detected in the urine. All the pharmacokinetic parameters suggest that the dextran-trichosanthin complex stayed longer in the body and maintained a much higher plasma concentration than trichosanthin.


Subject(s)
Dextrans/pharmacokinetics , Kidney/metabolism , Trichosanthin/pharmacokinetics , Animals , Binding, Competitive/drug effects , Dextranase/pharmacology , Dextrans/blood , Dextrans/urine , Half-Life , Radioimmunoassay , Rats , Trichosanthin/blood , Trichosanthin/urine
9.
Gene ; 97(2): 267-72, 1991 Jan 15.
Article in English | MEDLINE | ID: mdl-1999291

ABSTRACT

Several cDNA clones coding for trichosanthin (TCS) have been isolated from a cDNA library prepared from the poly(A)+RNA of the root tuber of Trichosanthes kirilowii Maximowicz. The nucleotide sequence codes for a protein of 289 amino acids (aa) including a putative signal peptide of 23 aa and an extra 19 aa at the C terminus; the latter two have not been found in TCS obtained from the natural product [Collins et al., J. Biol. Chem. 265 (1990) 8665-8669]. Recombinant TCS (reTCS) was synthesized in Escherichia coli, in which the cDNA without the signal sequence was expressed under the control of the trc promoter; reTCS was detected by a rabbit anti-TCS antiserum.


Subject(s)
Escherichia coli/genetics , Gene Expression , Plants/genetics , Trichosanthin/genetics , Amino Acid Sequence , Base Sequence , Cloning, Molecular , DNA/genetics , Molecular Sequence Data , Recombinant Proteins/biosynthesis , Recombinant Proteins/genetics , Regulatory Sequences, Nucleic Acid , Restriction Mapping , Trichosanthin/biosynthesis
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