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Nicoleta Joo Séverine Renaudineau Guillaume Delapierre Dr. Gérard Bidan Dr. Lise‐Marie Chamoreau René Thouvenot Dr. Pierre Gouzerh Prof. Dr. Anna Proust Prof. Dr. 《Chemistry (Weinheim an der Bergstrasse, Germany)》2010,16(17):5043-5051
Organosilyl/‐germyl polyoxotungstate hybrids [PW9O34(tBuSiO)3Ge(CH2)2CO2H]3? ( 1 a ), [PW9O34(tBuSiO)3Ge(CH2)2CONHCH2C?CH]3? ( 2 a ), [PW11O39Ge(CH2)2CO2H]4? ( 3 a ), and [PW11O39Ge(CH2)2CONHCH2C≡CH]4? ( 4 a ) have been prepared as tetrabutylammonium salts and characterized in solution by multinuclear NMR spectroscopy. The crystal structure of (NBu4)3 1 a? H2O has been determined and the electrochemical behavior of 1 a and 2 a has been investigated by cyclic voltammetry. Covalent grafting of 2 a onto an n‐type silicon wafer has been achieved and the electrochemical behavior of the grafted clusters has been investigated. This represents the first example of covalent grafting of Keggin‐type clusters onto a Si surface and a step towards the realization of POM‐based multilevel memory devices. 相似文献
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A Simple Colorimetric Enzymatic-Assay for Okadaic Acid Detection Based on the Immobilization of Protein Phosphatase 2A in Sol-Gel 总被引:2,自引:0,他引:2
Okadaic acid (OA), a lipophilic toxin, is produced by Dinophysis and Prorocentrum, and causes diarrheic shellfish poisoning to humans. The mechanism of OA action is based on the reversible inhibition of
protein phosphatase type 2A (PP2A) by the toxin. Therefore, this inhibition could be used to develop assay for OA detection.
In this work, a colorimetric test based on the PP2A inhibition was developed for OA detection. PP2A from GTP and Millipore
was immobilized on silica sol-gel, and the detection was performed. A limit of detection of 0.29 and 1.14 μg/L was respectively
observed for enzyme from GTP and Millipore. The immobilization technique provided a tool to preserve the enzymatic activity,
which is very unstable in solution. The PP2A immobilized sol-gel exhibited a storage stability of near 5 months, when microtiter
plate with enzyme-immobilized polymer was kept at −18C°. The combination of the simplicity of the colorimetric method, along
with long storage stability achieved by sol-gel immobilization, demonstrated the potentiality of this technique to be used
for commercial purpose. 相似文献
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Malik L Nygaard J Hoiberg-Nielsen R Arleth L Hoeg-Jensen T Jensen KJ 《Langmuir : the ACS journal of surfaces and colloids》2012,28(1):593-603
The self-assembly of biopharmaceutical peptides into multimeric, nanoscale objects, as well as their disassembly to monomers, is central for their mode of action. Here, we describe a bioorthogonal strategy, using a non-native recognition principle, for control of protein self-assembly based on intermolecular fluorous interactions and demonstrate it for the small protein insulin. Perfluorinated alkyl chains of varying length were attached to desB30 human insulin by acylation of the ε-amine of the side-chain of LysB29. The insulin analogues were formulated with Zn(II) and phenol to form hexamers. The self-segregation of fluorous groups directed the insulin hexamers to self-assemble. The structures of the systems were investigated by circular dichroism (CD) spectroscopy and synchrotron small-angle X-ray scattering. Also, the binding affinity to the insulin receptor was measured. Interestingly, varying the length of the perfluoroalkyl chain provided three different scenarios for self-assembly; the short chains hardly affected the native hexameric structure, the medium-length chains induced fractal-like structures with the insulin hexamer as the fundamental building block, while the longest chains lead to the formation of structures with local cylindrical geometry. This hierarchical self-assembly system, which combines Zn(II) mediated hexamer formation with fluorous interactions, is a promising tool to control the formation of high molecular weight complexes of insulin and potentially other proteins. 相似文献
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Ellen Verheyen Lise Delain‐Bioton Steffen van der Wal Najim el Morabit Arjan Barendregt Wim E. Hennink Cornelus F. van Nostrum 《Macromolecular bioscience》2010,10(12):1517-1526
An efficient strategy is reported to introduce methacrylamide groups on the lysine residues of a model protein (lysozyme) for immobilization and triggered release from a hydrogel network. A novel spacer unit was designed, containing a disulfide bond, such that the release of the protein can be triggered by reduction. The modified proteins were characterized by MALDI‐TOF MS, titration of free NH2 residues and spectral analysis. The modification reaction is well controlled, and the number of introduced functions can be tailored by changing the reaction conditions. Gel electrophoresis experiments showed that the methacrylamide modified protein can be immobilized in a polyacrylamide hydrogel and subsequently released by reduction of the spacer by which the protein was grafted to the polymeric network.
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Danila I Pop F Escudero C Feldborg LN Puigmartí-Luis J Riobé F Avarvari N Amabilino DB 《Chemical communications (Cambridge, England)》2012,48(38):4552-4554
The formation of helical self-assembled fibres by a C(3) symmetric molecule incorporating three tetrathiafulvalene units is shown to be influenced dramatically by the processing conditions, leading to a variety of different chiral forms, including unprecedented croissants. 相似文献
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