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1.
Raza Syed Arshad Siddiqui Atiq W. Standing Craig 《Systemic Practice and Action Research》2019,32(2):125-153
Systemic Practice and Action Research - Most of the traditional technology acceptance models revolve around information systems (IS)/information technology (IT) adoption at individual user level.... 相似文献
2.
A. E. Yassen H. A. Hassan L. S. Kawashti 《Cellular and molecular life sciences : CMLS》1994,50(11-12):1111-1114
A detailed karyotypic analysis of two Egyptian species of bats,Taphozous perforatus andTaphozous nudiventris, was made on the basis of conventional data and G-band patterns. No detectable karyotypic difference was found between the two species (2n=42, F.N. 64). By comparison of G-band patterns, some differences between the two species were seen in the corresponding autosomal pairs. These results are reported for the first time in Egypt. 相似文献
3.
外加电磁场对火焰结构及燃料燃烧特性的影响 总被引:1,自引:0,他引:1
燃料在电、磁场作用下的燃烧是一个新的跨学科性质的研究课题.它涉及磁流体发电、空间技术中电磁燃烧技术的应用以及能源与动力工程中能量转换与效率.本文从实验和理论两个方面,扼要地报导了碳氢燃料在外加磁场、电场影响下的火焰结构及其燃烧特性.把近年来我研究小组的主要研究结果汇总发表. 相似文献
4.
D. V. Amin R. B. Doctor A. O. Girdhar U. H. Shah 《Cellular and molecular life sciences : CMLS》1980,36(12):1410-1411
Summary Prostaglandin (PG) release was measured from the isolated perfused rabbit heart. The effects of -adrenergic stimulation and blockade suggest that PG synthesis is regulated in part by adrenergic mechanisms. 相似文献
5.
本文记述了伊朗膜翅目Hymenoptera青蜂科Chrysididae和切叶蜂科MegachiLidae的种类,其中青蜂科7属( Chrysis,Chrysura,Cleptes,Pseudomalus,Trichrysis,Parnopes和Spinolia)10种,切叶蜂科10属( Anthidium, Anthidiellum,Chalicodoma,Coelioxys,Heriades,Hoplitis,Megachile,Osmia,Protosmia 和Stelis)17种。 相似文献
6.
Sobia Zaidi Md. Imtaiyaz Hassan Asimul Islam Faizan Ahmad 《Cellular and molecular life sciences : CMLS》2014,71(2):229-255
Cytochrome-c (cyt-c), a multi-functional protein, plays a significant role in the electron transport chain, and thus is indispensable in the energy-production process. Besides being an important component in apoptosis, it detoxifies reactive oxygen species. Two hundred and eighty-five complete amino acid sequences of cyt-c from different species are known. Sequence analysis suggests that the number of amino acid residues in most mitochondrial cyts-c is in the range 104?±?10, and amino acid residues at only few positions are highly conserved throughout evolution. These highly conserved residues are Cys14, Cys17, His18, Gly29, Pro30, Gly41, Asn52, Trp59, Tyr67, Leu68, Pro71, Pro76, Thr78, Met80, and Phe82. These are also known as “key residues”, which contribute significantly to the structure, function, folding, and stability of cyt-c. The three-dimensional structure of cyt-c from ten eukaryotic species have been determined using X-ray diffraction studies. Structure analysis suggests that the tertiary structure of cyt-c is almost preserved along the evolutionary scale. Furthermore, residues of N/C-terminal helices Gly6, Phe10, Leu94, and Tyr97 interact with each other in a specific manner, forming an evolutionary conserved interface. To understand the role of evolutionary conserved residues on structure, stability, and function, numerous studies have been performed in which these residues were substituted with different amino acids. In these studies, structure deals with the effect of mutation on secondary and tertiary structure measured by spectroscopic techniques; stability deals with the effect of mutation on T m (midpoint of heat denaturation), ?G D (Gibbs free energy change on denaturation) and folding; and function deals with the effect of mutation on electron transport, apoptosis, cell growth, and protein expression. In this review, we have compiled all these studies at one place. This compilation will be useful to biochemists and biophysicists interested in understanding the importance of conservation of certain residues throughout the evolution in preserving the structure, function, and stability in proteins. 相似文献
7.
Stark A Lin MF Kheradpour P Pedersen JS Parts L Carlson JW Crosby MA Rasmussen MD Roy S Deoras AN Ruby JG Brennecke J;Harvard FlyBase curators;Berkeley Drosophila Genome Project Hodges E Hinrichs AS Caspi A Paten B Park SW Han MV Maeder ML Polansky BJ Robson BE Aerts S van Helden J Hassan B Gilbert DG Eastman DA Rice M Weir M Hahn MW Park Y Dewey CN Pachter L Kent WJ Haussler D Lai EC Bartel DP Hannon GJ Kaufman TC Eisen MB Clark AG Smith D Celniker SE Gelbart WM Kellis M 《Nature》2007,450(7167):219-232
8.
9.
Rasmussen SG DeVree BT Zou Y Kruse AC Chung KY Kobilka TS Thian FS Chae PS Pardon E Calinski D Mathiesen JM Shah ST Lyons JA Caffrey M Gellman SH Steyaert J Skiniotis G Weis WI Sunahara RK Kobilka BK 《Nature》2011,477(7366):549-555
G protein-coupled receptors (GPCRs) are responsible for the majority of cellular responses to hormones and neurotransmitters as well as the senses of sight, olfaction and taste. The paradigm of GPCR signalling is the activation of a heterotrimeric GTP binding protein (G protein) by an agonist-occupied receptor. The β(2) adrenergic receptor (β(2)AR) activation of Gs, the stimulatory G protein for adenylyl cyclase, has long been a model system for GPCR signalling. Here we present the crystal structure of the active state ternary complex composed of agonist-occupied monomeric β(2)AR and nucleotide-free Gs heterotrimer. The principal interactions between the β(2)AR and Gs involve the amino- and carboxy-terminal α-helices of Gs, with conformational changes propagating to the nucleotide-binding pocket. The largest conformational changes in the β(2)AR include a 14 ? outward movement at the cytoplasmic end of transmembrane segment 6 (TM6) and an α-helical extension of the cytoplasmic end of TM5. The most surprising observation is a major displacement of the α-helical domain of Gαs relative to the Ras-like GTPase domain. This crystal structure represents the first high-resolution view of transmembrane signalling by a GPCR. 相似文献
10.
Miwi catalysis is required for piRNA amplification-independent LINE1 transposon silencing 总被引:1,自引:0,他引:1
Reuter M Berninger P Chuma S Shah H Hosokawa M Funaya C Antony C Sachidanandam R Pillai RS 《Nature》2011,480(7376):264-267