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Bhak, Jong
KOrean GenomIcs Center
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dc.citation.endPage 938 -
dc.citation.number 3 -
dc.citation.startPage 929 -
dc.citation.title JOURNAL OF MOLECULAR BIOLOGY -
dc.citation.volume 307 -
dc.contributor.author Bhak, Jong Hwa -
dc.contributor.author Lappe, Michael -
dc.contributor.author Teichmann, Sarah A. -
dc.date.accessioned 2023-12-22T11:45:15Z -
dc.date.available 2023-12-22T11:45:15Z -
dc.date.created 2015-08-03 -
dc.date.issued 2001-03 -
dc.description.abstract In the postgenomic era, one of the most interesting and important challenges is to understand protein interactions on a large scale. The physical interactions between protein domains are fundamental to the workings of a cell: in multi-domain polypeptide chains, in multi-subunit proteins and in transient complexes between proteins that also exist independently. To study the large-scale patterns and evolution of interactions between protein domains, we view interactions between protein domains in terms of the interactions between structural families of evolutionarily related domains. This allows us to classify 8151 interactions betu een individual domains in the Protein Data Bank and the yeast Saccharromyces cerevisiae in terms of 664 types of interactions, between protein families. At least 51 interactions do not occur in the Protein Data Bank and can only be derived from the yeast data. The map of interactions between protein families has the form of a scale-free network, meaning that most protein families only interact with one or two other families, while a few families are extremely versatile in their interactions and are connected to many families. We observe that almost half of all known families engage in interactions with domains from their own family. We also see that the repertoires of interactions of domains within and between polypeptide chains overlap mostly for two specific types of protein families: enzymes and same-family interactions. This suggests that different types of protein interaction repertoires exist for structural, functional and regulatory reasons. (C) 2001 Academic Press -
dc.identifier.bibliographicCitation JOURNAL OF MOLECULAR BIOLOGY, v.307, no.3, pp.929 - 938 -
dc.identifier.doi 10.1006/jmbi.2001.4526 -
dc.identifier.issn 0022-2836 -
dc.identifier.scopusid 2-s2.0-0035970298 -
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/13249 -
dc.identifier.url http://www.sciencedirect.com/science/article/pii/S0022283601945267 -
dc.identifier.wosid 000167930300015 -
dc.language 영어 -
dc.publisher ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD -
dc.title.alternative Mapping protein family interactions: intramolecular and intermolecular protein family interaction repertoires -
dc.title Mapping protein family interactions: Intramolecular and intermolecular protein family interaction repertoires in the PDB and yeast -
dc.type Article -
dc.description.journalRegisteredClass scopus -

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