http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
- 中文 을 입력하시려면 zhongwen을 입력하시고 space를누르시면됩니다.
- 北京 을 입력하시려면 beijing을 입력하시고 space를 누르시면 됩니다.
RISS 인기검색어
- 검색키워드
- 저자 : Caffrey, Michael S. (검색결과 3 건)
- 무료
- 기관 내 무료
- 유료
-
Kevin Caffrey 고려대학교 민족문화연구원 2014 Cross-Currents Vol.- No.12
This article takes the example of a disappeared altar in a Himalayan valley as revelatory of contradictions within the mechanics of a Hui Muslim revitalization project. The community example—a group of historically identifiable Muslims in China—centers on the disappearance of a gifted propitiation altar that once stood as an instantiation of community cohesion among ethnically varied populations in the valley. The investigation examines transformations of modernity and the erosion of the “social glue” that held valley communities together as the disappearance of this gift is revealed to be a telling instance of the large-scale productivities and corrosions effected by China’s contemporary renaissance of reemerging religious movements and community identifications, processes in which Chinese Muslims serve as a potential indicator for a long view of reform contemporary social transformation.
-
Conformational change of erythroid α-spectrin at the tetramerization site upon binding β-spectrin
Long, Fei,McElheny, Dan,Jiang, Shaokai,Park, Sunghyouk,Caffrey, Michael S.,Fung, Leslie W.-M. Wiley-Blackwell Publishing, Inc. 2007 Protein science Vol. No.
<P>We previously determined the solution structures of the first 156 residues of human erythroid alpha-spectrin (SpalphaI-1-156, or simply Spalpha). Spalpha consists of the tetramerization site of alpha-spectrin and associates with a model beta-spectrin protein (Spbeta) with an affinity similar to that of native alpha- and beta-spectrin. Upon alphabeta-complex formation, our previous results indicate that there is an increase in helicity in the complex, suggesting conformational change in either Spalpha or Spbeta or in both. We have now used isothermal titration calorimetry, circular dichroism, static and dynamic light scattering, and solution NMR methods to investigate properties of the complex as well as the conformation of Spalpha in the complex. The results reveal a highly asymmetric complex, with a Perrin shape parameter of 1.23, which could correspond to a prolate ellipsoid with a major axis of about five and a minor axis of about one. We identified 12 residues, five prior to and seven following the partial domain helix in Spalpha that moved freely relative to the structural domain in the absence of Spbeta but when in the complex moved with a mobility similar to that of the structural domain. Thus, it appears that the association with Spbeta induced an unstructured-to-helical conformational transition in these residues to produce a rigid and asymmetric complex. Our findings may provide insight toward understanding different association affinities of alphabeta-spectrin at the tetramerization site for erythroid and non-erythroid spectrin and a possible mechanism to understand some of the clinical mutations, such as L49F of alpha-spectrin, which occur outside the functional partial domain region.</P>
-
Melé,ndez-Ló,pez, Samuel G.,Herdman, Scott,Hirata, Ken,Choi, Min-Ho,Choe, Youngchool,Craik, Charles,Caffrey, Conor R.,Hansell, Elisabeth,Chá,vez-Munguí,a, Bibiana,Chen, Yen Tin American Society for Microbiology 2007 EUKARYOTIC CELL Vol.6 No.7
<B>ABSTRACT</B><P>Cysteine proteinases are key virulence factors of the protozoan parasite <I>Entamoeba histolytica</I>. We have shown that cysteine proteinases play a central role in tissue invasion and disruption of host defenses by digesting components of the extracellular matrix, immunoglobulins, complement, and cytokines. Analysis of the <I>E. histolytica</I> genome project has revealed more than 40 genes encoding cysteine proteinases. We have focused on <I>E. histolytica</I> cysteine proteinase 1 (EhCP1) because it is one of two cysteine proteinases unique to invasive <I>E. histolytica</I> and is highly expressed and released. Recombinant EhCP1 was expressed in <I>Escherichia coli</I> and refolded to an active enzyme with a pH optimum of 6.0. We used positional-scanning synthetic tetrapeptide combinatorial libraries to map the specificity of the P1 to P4 subsites of the active site cleft. Arginine was strongly preferred at P2, an unusual specificity among clan CA proteinases. A new vinyl sulfone inhibitor, WRR483, was synthesized based on this specificity to target EhCP1. Recombinant EhCP1 cleaved key components of the host immune system, C3, immunoglobulin G, and pro-interleukin-18, in a time- and dose-dependent manner. EhCP1 localized to large cytoplasmic vesicles, distinct from the sites of other proteinases. To gain insight into the role of secreted cysteine proteinases in amebic invasion, we tested the effect of the vinyl sulfone cysteine proteinase inhibitors K11777 and WRR483 on invasion of human colonic xenografts. The resultant dramatic inhibition of invasion by both inhibitors in this human colonic model of amebiasis strongly suggests a significant role of secreted amebic proteinases, such as EhCP1, in the pathogenesis of amebiasis.</P>
연관 검색어 추천
이 검색어로 많이 본 자료
활용도 높은 자료
