检索结果-南通市图书馆

Evolution of a protein domain interaction network

Chinese Physics B 2010年第1期19卷 204-211页

作者：高丽锋石建军官山 Institute of Crop Sciences Chinese Academy of Agricultural Sciences College of Physics Science and Technology Yangzhou University

In this paper, we attempt to understand complex network evolution from the underlying evolutionary relationship between biological organisms. Firstly, we construct a Pfam domain interaction network for each of the 470 completely sequenced organisms, and therefore each organism is correlated with a specific Pfam domain interaction network; secondly, we infer the evolutionary relationship of these organisms with the nearest neighbour joining method; thirdly, we use the evolutionary relationship between organisms constructed in the second step as the evolutionary course of the Pfam domain interaction network constructed in the first step. This analysis of the evolutionary course shows：（i） there is a conserved sub-network structure in network evolution; in this sub-network, nodes with lower degree prefer to maintain their connectivity invariant, and hubs tend to maintain their role as a hub is attached preferentially to new added nodes; （ii） few nodes are conserved as hubs; most of the other nodes are conserved as one with very low degree; （iii） in the course of network evolution, new nodes are added to the network either individually in most cases or as clusters with relative high clustering coefficients in a very few cases.

关键词： complex network protein domain network evolution

来源：

维普期刊数据库

同方期刊数据库评论

在线全文

学校读者我要写书评

暂无评论

A single-domain protein catenane of dihydrofolate reductase

引用

National Science Review 2023年第11期10卷 128-137页

作者： Jing Fang Tianzuo Li Jiyeon Lee Dahye Im Lianjie Xu Yajie Liu Jongcheol Seo Wen-Bin Zhang Beijing National Laboratory for Molecular Sciences Key Laboratory of Polymer Chemistry & Physics of Ministry of EducationCenter for Soft Matter Science and EngineeringCollege of Chemistry and Molecular EngineeringPeking University Department of Chemistry Pohang University of Science and Technology (POSTECH) Beijing Academy of Artificial Intelligence

A single-domain protein catenane refers to two mechanically interlocked polypeptide rings that fold synergistically into a compact and integrated structure, which is extremely rare in nature. Here, we report a single-domain protein catenane of dihydrofolate reductase(cat-DHFR). This design was achieved by rewiring the connectivity between secondary motifs to introduce artificial entanglement and synthesis was readily accomplished through a series of programmed and streamlined post-translational processing events in cells without any additional in vitro reactions. The target molecule contained few exogenous motifs and was thoroughly characterized using a combination of ultra-performance liquid chromatography–mass spectrometry, sodium dodecyl sulfate–polyacrylamide gel electrophoresis, protease cleavage experiments and ion mobility spectrometry–mass spectrometry. Compared with the linear control, cat-DHFR retained its catalytic capability and exhibited enhanced stability against thermal or chemical denaturation due to conformational restriction. These results suggest that linear proteins may be converted into their concatenated single-domain counterparts with almost identical chemical compositions, well-preserved functions and elevated stabilities, representing an entirely new horizon in protein science.

关键词： cellular synthesis catenane protein domain chemical topology DHFR

来源：

同方期刊数据库评论

在线全文

同方期刊数据库

学校读者我要写书评

暂无评论

The Evolutionary Relationship of the domain Architectures in the RhoGEF-containing proteins

引用

Genomics, Proteomics & Bioinformatics 2005年第2期3卷 94-106页

作者： Qing-Lan Sun Hong-Jun Zhou Kui Lin The Key Laboratory of the Ministry of Education for Biodiversity Science and Ecological Engineering College of Life Sciences Beijing Normal University Beijing 100875 China.

domain insertions and deletions lead to variations in the domain architectures of the proteins from their common ancestor. In this work, we investigated four groups of the RhoGEF-containing proteins from different organisms with domain architectures RhoGEF-PH-SH3, SH3-RhoGEF-PH, RhoGEF-PH, and SH3-RhoGEF defined in the Pfam database. The phylogenetic trees were constructed using each individual domain and/or the combinations of all the domains. The phylogenetic analysis suggests that RhoGEF-PH-SH3 and SH3-RhoGEF-PH might have evolved from RhoGEF-PH through the insertion of SH3 independently, while SH3- RhoGEF of proteins in fruit fly might have evolved from SH3-RhoGEF-PH by the degeneration of PH domain.

关键词： protein domain domain architecture phylogenetic analysis domain loss RhoGEF-containing proteins

来源：

维普期刊数据库

同方期刊数据库评论

在线全文

学校读者我要写书评

暂无评论

The Catalytic Triad are Essential for TSP50 to Perform Its Function in Cell Proliferation

The Catalytic Triad are Essential for TSP50 to Perform Its F...

引用

“细胞活动生命活力”——中国细胞生物学学会全体会员代表大会暨第十二次学术大会

作者： Yu-Yin Li~(1,2),Yong-Li Bao~1,Zhen-Bo Song~1,Lu-Guo Sun~(1,3),Ping Wu~1,Yu Zhang~2,Cong Fan~2,Yin Wu~2,Chun-Lei Yu~(1,2), Yan-Xin Huang~1,Ying Sun~3,Li-Hua Zheng~3,Guan-Nan Wang~3,and Yu-Xin Li~(2,3) 1.National Engineering Laboratory for Druggable Gene and protein Screening,Northeast Normal University,Changchun 130024,China 2.Research Center of Agriculture and Medicine Gene Engineering of Ministry of Education,Northeast Normal University,Changchun 130024,China 3.Institute of Genetics and Cytology,Northeast Normal University,Changchun 130024,China

Testes-specific protease 50(TSP50),a new threonine enzyme,shares similar aa sequence and enzymatic structure with many serine proteases and is proposed to be a potential ***50 is up-regulated in breast cancer epithelial cells,and ectopic expression of TSP50 in TSP50-deficient Chinese hamster ovary(CHO) cells markedly promoted cell ***,the mechanism(s) by which TSP50 exerts its growth promotion effects are not yet fully *** delineate whether the threonine protease catalytic triad of TSP50 are essential for its function in cell proliferation,we constructed and characterized three mutant TSP50s in which point mutations were introduced in the protease catalytic triad *** a series of the proliferation,colony formation and tumorigenicity assay,we showed that TSP50 T310A and TSP50 H153A can significantly depress TSP50-induced cell proliferation and tumor *** investigation revealed that TSP50 T310A and TSP50 H153A can destroy the interaction between TSP50 and NF-kB:IκBαcomplex which is necessary for TSP50 to perform its function in cell *** together,our data highlight the importance of the catalytic triad,especially threonine, the most critical protease catalytic site,for TSP50-induced cell proliferation and tumor formation,and the catalytic site of TSP50 would be a potential therapeutic target.

关键词： Serine protease TSP50 mechanism cell proliferation NF-κB signaling tumor formation protein domain

来源： cnki会议评论

在线全文

cnki会议

学校读者我要写书评

暂无评论

Degradation of mouse NTE-related esterase by macroautophagy and the proteasome

Degradation of mouse NTE-related esterase by macroautophagy ...

引用

重庆市生物化学与分子生物学学术会议

作者：常平安 Key Laboratory of Molecular Biology College of Bio-informationChongqing University of Posts and Telecommunications

In recent years,a mammalian family of lipid hydrolases,designated"patatin-like phospholipase (PNPLA)"has attracted attention as its members were found to serve critical roles in diverse aspects of lipid metabolism and *** PNPLAs comprise ten members divided into three subgroups and one subgroup contains PNPLA6 and PNPLA7,which were also named neuropathy target esterase

关键词： NTE-related esterase macroautophagy proteasome protein domain

来源： cnki会议评论

在线全文

cnki会议

学校读者我要写书评

暂无评论

General trends of protein expression and localization reveal the rule of bio-complexity realization

General trends of protein expression and localization reveal...

引用

第五届全国生物信息学与系统生物学学术大会暨国际生物信息学前沿研讨会高通量时代的生物信息学与系统生物学

作者：杨冬 Dingchen Li Fan Zhong Dong Li Ying Jiang Fuchu He State Key Laboratory of Proteomics Beijing Proteome Research CenterBeijing Institute of Radiation Medicine Institutes of Biomedical Sciences and Department of Chemistry Fudan University

Background:During evolution,proteins containing newly emerged domains and the increasing proportion of multi-domain proteins in the full Genome-Encoded Proteome(GEP) have substantially contributed to increasing biological ***,it is not known how these two potential structural factors are preferentially utilized at given physiological states,until our most recent study found that multidomain proteins or only older domain- containing proteins are significantly overrepresented in certain-state proteomes(CSPs,i.e., all the proteins expressed at certain physiological states) compared with GEP,which indicates biological complexity under certain conditions is more significantly realized by diverse domain organization than by the emergence of new types of *** further explore the regular utilization pattern in the view of protein spatial distribution at levels ranging from organelles to organs,we investigated the relationships between protein domain characters and protein subcelluar localization width(SLW) or tissue specificity(TS). Methods:To calculate SLW,we collected high confident subcellular location information in Swiss-Prot,GOA,human protein atlas(HPA),MitoP2,Human Liver Organelle Proteome(HLOP) and related references and *** identification is based on RPS-BLAST against Pfam and SMART(Eproteins,including the subcellular locations for different splice isoforms as complete as *** on this atlas,we found that SLW positively correlates with DN value,while it negatively correlates with DA value,that is, multi-domain proteins or only older domain-containing proteins tend to be localized at more subcellular *** addition,SLW negatively correlate with TS,*** with more subcellular location

关键词： Biological complexity protein domain proteome subcellular localization tissue specificity

来源： cnki会议评论

在线全文

cnki会议

学校读者我要写书评

暂无评论

欢迎您,

建议与咨询留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

时间限定

文献类型

馆藏选择

核心期刊

语言

文献类型

帮助

文字说明：

检索规则说明：

检索范例：

分类表

所选分类

限定检索结果

文献类型

馆藏范围

日期分布

学科分类号

主题

机构

作者

语言

在线全文

在线全文

在线全文

在线全文

在线全文

在线全文

请选择保存的检索档案：

请选择收藏分类：

通借通还

欢迎您,

建议与咨询 留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

时间限定

文献类型

馆藏选择

核心期刊

语言

文献类型

帮助

文字说明：

检索规则说明：

检索范例：

分类表

所选分类

限定检索结果

文献类型

馆藏范围

日期分布

学科分类号

主题

机构

作者

语言

在线全文

在线全文

在线全文

在线全文

在线全文

在线全文

请选择保存的检索档案： 新增检索档案 确定 取消

请选择收藏分类： 新增自定义分类 确定 取消

通借通还

建议与咨询留下您的常用邮箱和电话号码，以便我们向您反馈解决方案和替代方法

请选择保存的检索档案：

请选择收藏分类：