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7篇 您的检索式:作者名="Markussen Jan"
    题名 作者 年代 出处 被引量
1胰岛素类似物的结构设计与药代动力学显示文摘Jan Markussen 2004国外医学:内分泌学分册2004,24,4:2
2Prepro-Leaders Lacking N-Linked Glycosylation for Secretory Expression in the Yeast Saccharomyces cerevisiae显示文摘Thomas Kjeldsen Morten Hach Per Balschmidt Svend Havelund Annette Frost Pettersson Jan Markussen 1998Protein Expression and Purification1998,,3:1
3Crystallization and preliminary crystallographic analysis of [A21Ser-B27Arg-B30Thr-NH_2]-human insulin显示文摘Some experiments have shown that the properties of single mutation can be synthesizedin a mutant with multiple mutations. Following this idea, SRN-HI was prepared.Markussen et al.reported that a high stability and a prolonged action could be createdfrom mutations AsnA21Ser and ThrB27Arg respectively. Therefore, a double property wasexpected to appear in SRN-HI, which has been proved to be true by biological test.金雷 张林 王大成 Jan Markussen 1995Chinese Science Bulletin1995,40,11:0
4Crystallization and preliminary crystallographic studies of insulin T_3R_3 states created in different conditions显示文摘In the presence of a series of small organic molecules including 1, 4 dioxane, DMF, isopropanol, rDNA human insulin, mutants A21 Asn→Ser and (A21 Asn→Ser, B27 Thr→Arg) human insulin have been crystallized in both Zn 2+ containing and Zn 2+ free system. Preliminary crystallographic analyses show that they all belong to T 3R 3 structural type. The results indicate that, except phenolic derivatives and lyotropic anions reported before, some other appropriate organic molecules can also induce the T 3R 3 conformation transition of insulin.AI Xi 1, 2 , ZENG Zonghao 1, HUANG Peitang 2, Jan Markussen 3 and WANG Dacheng 1 * 1. Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China 2. Institute of Biotechnology, Academy of Military Medical Sciences, Beijing 1 1998Chinese Science Bulletin1998,43,1:0
5B9(Ser→Asp)人胰岛素突变体0.20nm分辨率晶体结构研究——一种速效胰岛素的结构特征显示文摘报道了运用X射线分析技术,在0.20nm分辨率测定了B9(Ser→Asp)的正交晶型的晶体结构。精化后的模型显示,B9(Ser→Asp)二聚体的分子骨架与天然胰岛素基本相同,但局部构象有差别,特别在B9Asp突变位点附近的侧链构象有较大变化,残基B9,B13,D9,D13的4个羧基互相排斥,使二聚体内分子间界面上的空间和电荷互补性都遭到严重破坏,从而造成在生理条件下胰岛素二聚体的不稳定,及其在生理条件下的强烈单体化趋向。这些变化构成了B9(Ser→Asp)的速效性的主要结构基础。外,B链N端肽段呈开放状态,可能代表低聚或单体状态下胰岛素的一种新构象状态。刘新奇 曾宗浩 张英 Jan Markussen 王大成 2000自然科学进展(国家重点实验室通讯)2000,10,2:0
6Crystallization and preliminary crystallographic analyses of human insulin mutant B9(Ser→Asp)in different aggregation forms显示文摘B9(Ser→Asp) insulin, one of the fast-acting insulin mutants produced by protein engineering, has been crystallized. Three crystal forms have been obtained, which belong to orthorhombic, tetragonal and rhombohedral system, respectively. Each crystal form contains different aggregation units of the mutant, i.e. dimer or hexamer. The diffraction data of the former two have been collected beyond 0.2 nm resolution. The structural analyses and comparisons will provide some information about insulin’s self-association and the structural basis of the fast absorption produced from the mutation.Xinqi Liu Lei Jin Ying Zhang Markussen Jan Dacheng Wang 1999Chinese Science Bulletin1999,44,9:0
7Orthorhombic crystal structure of an insulin mutant B9Asp at 0.20 nm resolution刘新奇 金雷 张英 Jan Markussen 王大成 2000Progress in Natural Science:Materials International2000,10,6:0
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