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排序方式: 共有259条查询结果,搜索用时 54 毫秒
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Alaullah Sheikh Farhana Khanam Md. Abu Sayeed Taibur Rahman Marcin Pacek Yanhui Hu Andrea Rollins Md. Saruar Bhuiyan Sean Rollins Anuj Kalsy Mohammad Arifuzzaman Daniel T. Leung David A. Sarracino Bryan Krastins Richelle C. Charles Regina C. LaRocque Alejandro Cravioto Stephen B. Calderwood W. Abdullah Brooks Jason B. Harris Joshua LaBaer Firdausi Qadri Edward T. Ryan 《PLoS neglected tropical diseases》2011,5(6)
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Burchat AF Calderwood DJ Hirst GC Holman NJ Johnston DN Munschauer R Rafferty P Tometzki GB 《Bioorganic & medicinal chemistry letters》2000,10(19):2171-2174
Pyrrolo[2,3-d]pyrimidines containing a 5-(4-phenoxyphenyl) substituent are novel, potent and selective inhibitors of lck in vitro. Exploration of C-6 position of the pyrrolo[2,3-d]pyrimidine and the terminal phenyl group structure-activity relationship (SAR) is detailed. Compound 1 is orally active in animal models. 相似文献
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Bouaouina M Goult BT Huet-Calderwood C Bate N Brahme NN Barsukov IL Critchley DR Calderwood DA 《The Journal of biological chemistry》2012,287(10):6979-6990
The activation of heterodimeric integrin adhesion receptors from low to high affinity states occurs in response to intracellular signals that act on the short cytoplasmic tails of integrin β subunits. Binding of the talin FERM (four-point-one, ezrin, radixin, moesin) domain to the integrin β tail provides one key activation signal, but recent data indicate that the kindlin family of FERM domain proteins also play a central role. Kindlins directly bind integrin β subunit cytoplasmic domains at a site distinct from the talin-binding site, and target to focal adhesions in adherent cells. However, the mechanisms by which kindlins impact integrin activation remain largely unknown. A notable feature of kindlins is their similarity to the integrin-binding and activating talin FERM domain. Drawing on this similarity, here we report the identification of an unstructured insert in the kindlin F1 FERM domain, and provide evidence that a highly conserved polylysine motif in this loop supports binding to negatively charged phospholipid head groups. We further show that the F1 loop and its membrane-binding motif are required for kindlin-1 targeting to focal adhesions, and for the cooperation between kindlin-1 and -2 and the talin head in αIIbβ3 integrin activation, but not for kindlin binding to integrin β tails. These studies highlight the structural and functional similarities between kindlins and the talin head and indicate that as for talin, FERM domain interactions with acidic membrane phospholipids as well β-integrin tails contribute to the ability of kindlins to activate integrins. 相似文献
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Amy L. Stiegler Thomas D. Grant Joseph R. Luft David A. Calderwood Edward H. Snell Titus J. Boggon 《PloS one》2013,8(1)
The heterotrimeric protein complex containing the integrin linked kinase (ILK), parvin, and PINCH proteins, termed the IPP complex, is an essential component of focal adhesions, where it interacts with many proteins to mediate signaling from integrin adhesion receptors. Here we conduct a biochemical and structural analysis of the minimal IPP complex, comprising full-length human ILK, the LIM1 domain of PINCH1, and the CH2 domain of α-parvin. We provide a detailed purification protocol for IPP and show that the purified IPP complex is stable and monodisperse in solution. Using small-angle X-ray scattering (SAXS), we also conduct the first structural characterization of IPP, which reveals an elongated shape with dimensions 120×60×40 Å. Flexibility analysis using the ensemble optimization method (EOM) is consistent with an IPP complex structure with limited flexibility, raising the possibility that inter-domain interactions exist. However, our studies suggest that the inter-domain linker in ILK is accessible and we detect no inter-domain contacts by gel filtration analysis. This study provides a structural foundation to understand the conformational restraints that govern the IPP complex. 相似文献