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971.
Klaus F. Wagenbauer Floris A. S. Engelhardt Dr. Evi Stahl Vera K. Hechtl Pierre Stömmer Fabian Seebacher Letizia Meregalli Philip Ketterer Dr. Thomas Gerling Prof. Dr. Hendrik Dietz 《Chembiochem : a European journal of chemical biology》2017,18(19):1873-1885
DNA origami has attracted substantial attention since its invention ten years ago, due to the seemingly infinite possibilities that it affords for creating customized nanoscale objects. Although the basic concept of DNA origami is easy to understand, using custom DNA origami in practical applications requires detailed know‐how for designing and producing the particles with sufficient quality and for preparing them at appropriate concentrations with the necessary degree of purity in custom environments. Such know‐how is not readily available for newcomers to the field, thus slowing down the rate at which new applications outside the field of DNA nanotechnology may emerge. To foster faster progress, we share in this article the experience in making and preparing DNA origami that we have accumulated over recent years. We discuss design solutions for creating advanced structural motifs including corners and various types of hinges that expand the design space for the more rigid multilayer DNA origami and provide guidelines for preventing undesired aggregation and on how to induce specific oligomerization of multiple DNA origami building blocks. In addition, we provide detailed protocols and discuss the expected results for five key methods that allow efficient and damage‐free preparation of DNA origami. These methods are agarose‐gel purification, filtration through molecular cut‐off membranes, PEG precipitation, size‐exclusion chromatography, and ultracentrifugation‐based sedimentation. The guide for creating advanced design motifs and the detailed protocols with their experimental characterization that we describe here should lower the barrier for researchers to accomplish the full DNA origami production workflow. 相似文献
972.
973.
Inside Cover: Traceless Cleavage of Protein–Biotin Conjugates under Biologically Compatible Conditions (ChemBioChem 17/2017) 下载免费PDF全文
974.
Chethana Rao Syamantak Khan Navneet C. Verma Dr. Chayan Kanti Nandi 《Chembiochem : a European journal of chemical biology》2017,18(24):2385-2389
We present efficient labelling of several proteins with orange‐emissive carbon dots. N‐Hydroxysuccinimide was used to activate the carboxyl groups of carbon dots, which subsequently reacted with the lysine groups present on the protein. Labelling was confirmed by UV absorption spectroscopy, PAGE and fluorescence correlation spectroscopy. Protein‐conjugated carbon dots showed an enhancement in fluorescence lifetime and intensity owing to reduced intramolecular dynamic fluctuations. Single‐molecule fluorescence measurements showed reduced fluorescence fluctuations and higher photon budget after protein tagging. Our study opens up opportunities to use carbon dots as highly precise biolabelling probes. 相似文献
975.
A Conjugate of an Anti‐Epidermal Growth Factor Receptor (EGFR) VHH and a Cell‐Penetrating Peptide Drives Receptor Internalization and Blocks EGFR Activation 下载免费PDF全文
Sanne A. M. van Lith Dr. Dirk van den Brand Dr. Rike Wallbrecher Dr. Sander M. J. van Duijnhoven Dr. Roland Brock Dr. William P. J. Leenders 《Chembiochem : a European journal of chemical biology》2017,18(24):2390-2394
Overexpression of (mutated) receptor tyrosine kinases is a characteristic of many aggressive tumors, and induction of receptor uptake has long been recognized as a therapeutic modality. A conjugate of a synthetically produced cell‐penetrating peptide (CPP), corresponding to amino acids 38–59 of human lactoferrin, and the recombinant llama single‐domain antibody (VHH) 7D12, which binds the human epidermal growth factor receptor (EGFR), was generated by sortase A mediated transpeptidation. The conjugate blocks EGF‐mediated EGFR activation with higher efficacy than that of both modalities alone; a phenomenon that is caused by both effective receptor blockade and internalization. Thus, the VHH–CPP conjugate shows a combination of activities that implement a highly powerful new design principle to block receptor activation by its clearance from the cell surface. 相似文献
976.
Dr. Matthias Hauf Dr. Florian Richter Tobias Schneider Thomas Faidt Dr. Berta M. Martins Dr. Tobias Baumann Dr. Patrick Durkin Prof. Dr. Holger Dobbek Prof. Dr. Karin Jacobs Prof. Dr. Andreas Möglich Prof. Dr. Nediljko Budisa 《Chembiochem : a European journal of chemical biology》2017,18(18):1771-1771
977.
Dr. Stephen Middel Dr. Cornelia H. Panse Swantje Nawratil Prof. Dr. Ulf Diederichsen 《Chembiochem : a European journal of chemical biology》2017,18(23):2328-2332
A novel peptide–peptide ligation strategy is introduced that has the potential to provide peptide libraries of linearly or branched coupled fragments and will be suited to introduce simultaneous protein modifications at different ligation sites. Ligation is assisted by templating peptide nucleic acid (PNA) strands, and therefore, ligation specificity is solely encoded by the PNA sequence. PNA templating, in general, allows for various kinds of covalent ligation reactions. As a proof of principle, a native chemical ligation strategy was elaborated. This PNA‐templated ligation includes easy on‐resin procedures to couple linkers and PNA to the respective peptides, and a traceless photocleavage of the linker/PNA oligomer after the ligation step. A 4,5‐dimethoxy‐2‐nitrobenzaldehyde‐based linker that allowed the photocleavable linkage of two bio‐oligomers was developed. 相似文献
978.
Dr. Aime Lopez Aguilar Xiaomeng Hou Dr. Liuqing Wen Prof. Peng G. Wang Prof. Peng Wu 《Chembiochem : a European journal of chemical biology》2017,18(24):2416-2421
Modification of nuclear and cytoplasmic proteins by the addition or removal of O‐GlcNAc dynamically impacts multiple biological processes. Here, we present the development of a chemoenzymatic histology method for the detection of O‐GlcNAc in tissue specimens. We applied this method to screen murine organs, uncovering specific O‐GlcNAc distribution patterns in different tissue structures. We then utilized our histology method for O‐GlcNAc detection in human brain specimens from healthy donors and donors with Alzheimer's disease and found higher levels of O‐GlcNAc in specimens from healthy donors. We also performed an analysis using a multiple cancer tissue array, uncovering different O‐GlcNAc levels between healthy and cancerous tissues, as well as different O‐GlcNAc cellular distributions within certain tissue specimens. This chemoenzymatic histology method therefore holds great potential for revealing the biology of O‐GlcNAc in physiopathological processes. 相似文献
979.
980.
The Oxidation of Hydrophobic Aromatic Substrates by Using a Variant of the P450 Monooxygenase CYP101B1 下载免费PDF全文
Md. Raihan Sarkar Joel H. Z. Lee Dr. Stephen G. Bell 《Chembiochem : a European journal of chemical biology》2017,18(21):2119-2128
The cytochrome P450 monooxygenase CYP101B1, from a Novosphingobium bacterium is able to bind and oxidise aromatic substrates but at a lower activity and efficiency than norisoprenoids and monoterpenoid esters. Histidine 85 of CYP101B1 aligns with tyrosine 96 of CYP101A1, which, in the latter enzyme forms the only hydrophilic interaction with its substrate, camphor. The histidine residue of CYP101B1 was mutated to phenylalanine with the aim of improving the activity of the enzyme for hydrophobic substrates. The H85F mutant lowered the binding affinity and activity of the enzyme for β-ionone and altered the oxidation selectivity. This variant also showed enhanced affinity and activity towards alkylbenzenes, styrenes and methylnaphthalenes. For example the rate of product formation for acenaphthene oxidation was improved sixfold to 245 nmol per nmol CYP per min. Certain disubstituted naphthalenes and substrates, such as phenylcyclohexane and biphenyls, were oxidised with lower activity by the H85F variant. Variants at H85 (A and G) designed to introduce additional space into the active site so as to accommodate these larger substrates did not improve the oxidation activity. As the H85F mutant of CYP101B1 improved the oxidation of hydrophobic substrates, this residue is likely to be in the substrate binding pocket or the access channel of the enzyme. The side chain of the histidine might interact with the carbonyl groups of the favoured norisoprenoid substrates of CYP101B1. 相似文献