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  • Proceedings of the National Academy of Sciences  (4)
  • Zhang, Wei  (4)
  • Linguistics  (4)
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  • Proceedings of the National Academy of Sciences  (4)
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  • 1
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 117, No. 5 ( 2020-02-04), p. 2560-2569
    Abstract: De novo mutations (DNMs), or mutations that appear in an individual despite not being seen in their parents, are an important source of genetic variation whose impact is relevant to studies of human evolution, genetics, and disease. Utilizing high-coverage whole-genome sequencing data as part of the Trans-Omics for Precision Medicine (TOPMed) Program, we called 93,325 single-nucleotide DNMs across 1,465 trios from an array of diverse human populations, and used them to directly estimate and analyze DNM counts, rates, and spectra. We find a significant positive correlation between local recombination rate and local DNM rate, and that DNM rate explains a substantial portion (8.98 to 34.92%, depending on the model) of the genome-wide variation in population-level genetic variation from 41K unrelated TOPMed samples. Genome-wide heterozygosity does correlate with DNM rate, but only explains 〈 1% of variation. While we are underpowered to see small differences, we do not find significant differences in DNM rate between individuals of European, African, and Latino ancestry, nor across ancestrally distinct segments within admixed individuals. However, we did find significantly fewer DNMs in Amish individuals, even when compared with other Europeans, and even after accounting for parental age and sequencing center. Specifically, we found significant reductions in the number of C→A and T→C mutations in the Amish, which seem to underpin their overall reduction in DNMs. Finally, we calculated near-zero estimates of narrow sense heritability ( h 2 ), which suggest that variation in DNM rate is significantly shaped by nonadditive genetic effects and the environment.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    RVK:
    RVK:
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 2020
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
    Location Call Number Limitation Availability
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  • 2
    Online Resource
    Online Resource
    Proceedings of the National Academy of Sciences ; 2022
    In:  Proceedings of the National Academy of Sciences Vol. 119, No. 14 ( 2022-04-05)
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 119, No. 14 ( 2022-04-05)
    Abstract: Due to the importance of single-atom catalysts (SAC), here, the catalysis of Pt SAC was studied at the single-molecule single-atom level. Both static and dynamic activity heterogeneity are observed in Pt SAC. It reveals that the intrinsic catalytic activity of Pt SAC is higher than that of Pt nanoparticles (NPs), although they follow the same bimolecular competition mechanism. Significantly, Pt SAC presents no catalysis-induced surface restructuring, meaning that the dynamic activity fluctuation of Pt SAC can only be attributed to the spontaneous surface restructuring, and the catalysis process does not affect much of the structure of Pt 1 -based active sites, all different from Pt NP catalysis, in which the surface restructuring and the catalysis can affect each other. Further, density functional theory (DFT) calculation indicates that the unique catalytic properties of Pt SAC or the different catalytic properties between Pt SAC and NPs could be attributed to the strong adsorptions of both reactant and product on Pt SAC, large surface energy of Pt SAC, and strong binding of Pt 1 on support. Knowledge revealed here provides fundamental insights into the catalysis of atomically dispersed catalyst.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    RVK:
    RVK:
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 2022
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
    Location Call Number Limitation Availability
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  • 3
    Online Resource
    Online Resource
    Proceedings of the National Academy of Sciences ; 2023
    In:  Proceedings of the National Academy of Sciences Vol. 120, No. 25 ( 2023-06-20)
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 120, No. 25 ( 2023-06-20)
    Abstract: As a sustainable approach for N 2 fixation, electrocatalytic N 2 reduction reaction (N 2 RR) to produce ammonia (NH 3 ) is highly desirable with a precise understanding to the structure-activity relationship of electrocatalysts. Here, firstly, we obtain a novel carbon-supported oxygen-coordinated single-Fe-atom catalyst for highly efficient production of ammonia from electrocatalytic N 2 RR. Based on such new type of N 2 RR electrocatalyst, by combining operando X-ray absorption spectra (XAS) with density function theory calculation, we reveal significantly that the as-prepared active coordination structure undergoes a potential-driven two-step restructuring, firstly from Fe SA O 4 (OH) 1a to Fe SA O 4 (OH) 1a′ (OH) 1b with the adsorption of another –OH on Fe SA at open-circuit potential (OCP) of 0.58 V RHE , and subsequently restructuring from Fe SA O 4 (OH) 1a′ (OH) 1b to Fe SA O 3 (OH) 1a″ due to the breaking of one Fe-O bond and the dissociation of one –OH at working potentials for final electrocatalytic process of N 2 RR, thus revealing the first potential-induced in situ formation of the real electrocatalytic active sites to boost the conversion of N 2 to NH 3 . Moreover, the key intermediate of Fe-NNH x was detected experimentally by both operando XAS and in situ attenuated total reflection–surface-enhanced infrared absorption spectra (ATR-SEIRAS), indicating the alternating mechanism followed by N 2 RR on such catalyst. The results indicate the necessity of considering the potential-induced restructuring of the active sites on all kinds of electrocatalysts for such as highly efficient ammonia production from N 2 RR. It also paves a new way for a precise understanding to the structure-activity relationship of a catalyst and helps the design of highly efficient catalysts.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    RVK:
    RVK:
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 2023
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
    Location Call Number Limitation Availability
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  • 4
    Online Resource
    Online Resource
    Proceedings of the National Academy of Sciences ; 2019
    In:  Proceedings of the National Academy of Sciences Vol. 116, No. 27 ( 2019-07-02), p. 13305-13310
    In: Proceedings of the National Academy of Sciences, Proceedings of the National Academy of Sciences, Vol. 116, No. 27 ( 2019-07-02), p. 13305-13310
    Abstract: Mycophenolic acid (MPA) from filamentous fungi is the first natural product antibiotic to be isolated and crystallized, and a first-line immunosuppressive drug for organ transplantations and autoimmune diseases. However, some key biosynthetic mechanisms of such an old and important molecule have remained unclear. Here, we elucidate the MPA biosynthetic pathway that features both compartmentalized enzymatic steps and unique cooperation between biosynthetic and β-oxidation catabolism machineries based on targeted gene inactivation, feeding experiments in heterologous expression hosts, enzyme functional characterization and kinetic analysis, and microscopic observation of protein subcellular localization. Besides identification of the oxygenase MpaB′ as the long-sought key enzyme responsible for the oxidative cleavage of the farnesyl side chain, we reveal the intriguing pattern of compartmentalization for the MPA biosynthetic enzymes, including the cytosolic polyketide synthase MpaC′ and O -methyltransferase MpaG′, the Golgi apparatus-associated prenyltransferase MpaA′, the endoplasmic reticulum-bound oxygenase MpaB′ and P450-hydrolase fusion enzyme MpaDE′, and the peroxisomal acyl-coenzyme A (CoA) hydrolase MpaH′. The whole pathway is elegantly comediated by these compartmentalized enzymes, together with the peroxisomal β-oxidation machinery. Beyond characterizing the remaining outstanding steps of the MPA biosynthetic steps, our study highlights the importance of considering subcellular contexts and the broader cellular metabolism in natural product biosynthesis.
    Type of Medium: Online Resource
    ISSN: 0027-8424 , 1091-6490
    RVK:
    RVK:
    Language: English
    Publisher: Proceedings of the National Academy of Sciences
    Publication Date: 2019
    detail.hit.zdb_id: 209104-5
    detail.hit.zdb_id: 1461794-8
    SSG: 11
    SSG: 12
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
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