{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2022,4,5]],"date-time":"2022-04-05T04:47:25Z","timestamp":1649134045812},"reference-count":25,"publisher":"Portland Press Ltd.","issue":"5","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2011,10,1]]},"abstract":"<jats:p>Scientific contact lies at the heart of research and that between China and the U.K. is an important example of how it can come about. In 1911, when the Biochemical Society began, U.K. science was developing fast with profound discoveries in physics (the Rutherford atomic model) and biochemistry (the discovery of vitamins). In China, however, there was great social and political instability and a revolution. Since then, the turbulence of two world wars and a variety of deep global political tensions meant that the contacts between China and U.K. did not reflect the prodigious growth of biochemistry. There was, however, one particular and remarkable contact, that made by Joseph Needham, an outstanding biochemist. He visited China between 1943 and 1946, contacting many Chinese universities that were severely dislocated by war. Showing remarkable diplomatic abilities, Needham managed to arrange delivery of research and teaching equipment. His activities helped the universities to carry out their functions under near-impossible conditions and reminded them that they had friends abroad. Most remarkably, Joseph Needham developed an extraordinary grasp of Chinese culture, science and history and he opened the West to the extent and importance of Chinese science. Formal scientific and intellectual contacts between the scientific academic bodies in China and U.K., notably the Chinese Academy of Science and the Royal Society, resumed after British recognition of the Chinese Communist government in 1950. The delegations included outstanding scientists in biochemistry and related disciplines. Research activities, such as that concerning influenza, were soon established, whereas institutions, such as the Royal Society and the Wellcome Trust, acted a little later to support research. The outcomes have been long-term collaborations in such areas as insulin structure and function. There are now numerous joint activities in biochemistry and biomedicine supported by the MRC (Medical Research Council), BBSRC (Biotechnology and Biological Sciences Research Council), NERC (Natural Environment Research Council), EPSRC (Engineering and Physical Sciences Research Council) and UKRC (UK Research Councils). The present contacts and the associated research are very considerable and growing. It is clear that biochemistry in both countries has much to offer each other, and there is every reason to believe that these contacts will continue to expand in the future.<\/jats:p>","DOI":"10.1042\/bst0391313","type":"journal-article","created":{"date-parts":[[2012,5,3]],"date-time":"2012-05-03T12:32:44Z","timestamp":1336048364000},"page":"1313-1322","update-policy":"http:\/\/dx.doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":1,"title":["Biochemical contacts and collaborations between China and the U.K. since 1911"],"prefix":"10.1042","volume":"39","author":[{"given":"Guy\u00a0G.","family":"Dodson","sequence":"first","affiliation":[{"name":"Department of Chemistry, University of York, Heslington, York YO10 5DD, U.K."}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"288","published-online":{"date-parts":[[2011,9,21]]},"reference":[{"issue":"6","key":"2021111900575442500_B1","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1042\/BIO03206046","article-title":"Celebrating 100\u00a0years of The Biochemical Society","volume":"32","author":"Kleanthous","year":"2010","journal-title":"Biochemist"},{"key":"2021111900575442500_B2","volume-title":"Bomb, Book and Compass: Joseph Needham and the Great Secrets of China","author":"Winchester","year":"2008"},{"key":"2021111900575442500_B3","doi-asserted-by":"crossref","first-page":"556","DOI":"10.1042\/bj0600556","article-title":"The structure of pig and sheep insulins","volume":"60","author":"Brown","year":"1955","journal-title":"Biochem. J."},{"key":"2021111900575442500_B4","doi-asserted-by":"crossref","first-page":"549","DOI":"10.1002\/iub.206","article-title":"The development of biochemistry and molecular biology in China","volume":"61","author":"Zhang","year":"2009","journal-title":"IUBMB Life"},{"key":"2021111900575442500_B5","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1038\/224491a0","article-title":"Structure of rhombohedral 2 zinc insulin crystals","volume":"224","author":"Adams","year":"1969","journal-title":"Nature"},{"key":"2021111900575442500_B6","first-page":"752","article-title":"Studies on the insulin crystal structure: the molecule at 1.8 \u00c5 resolution","volume":"17","author":"Peking Insulin Structure Research Group","year":"1974","journal-title":"Sci. Sin."},{"key":"2021111900575442500_B7","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1038\/255103a0","article-title":"Chinese work on insulin","volume":"255","author":"Hodgkin","year":"1975","journal-title":"Nature"},{"key":"2021111900575442500_B8","first-page":"582","article-title":"Hydrogens in rhombohedral 2 zinc insulin crystals by X-ray analysis","volume":"24","author":"Sakabe","year":"1979","journal-title":"Tanpakushitsu Kakusan Koso"},{"key":"2021111900575442500_B9","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1042\/bst0110419","article-title":"Some problems in relation to the structures of insulin derivatives","volume":"11","author":"Liang","year":"1983","journal-title":"Biochem. Soc. Trans."},{"key":"2021111900575442500_B10","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1042\/bst0110411","article-title":"Insulin","volume":"11","author":"Hodgkin","year":"1983","journal-title":"Biochem. Soc. Trans."},{"key":"2021111900575442500_B11","doi-asserted-by":"crossref","first-page":"369","DOI":"10.1098\/rstb.1988.0058","article-title":"The structure of 2Zn pig insulin crystals at 1.5 \u00c5 resolution","volume":"319","author":"Baker","year":"1988","journal-title":"Philos. Trans. R Soc. London Ser. B"},{"key":"2021111900575442500_B12","doi-asserted-by":"crossref","first-page":"391","DOI":"10.1002\/bip.360230302","article-title":"Insulin's structure as a modified and monomeric molecule","volume":"23","author":"Bi","year":"1984","journal-title":"Biopolymers"},{"key":"2021111900575442500_B13","first-page":"964","article-title":"Preliminary crystallographic analysis of deshexapeptide (B25\u2013B30) insulin","volume":"33","author":"Wan","year":"1990","journal-title":"Sci. China B"},{"key":"2021111900575442500_B14","doi-asserted-by":"crossref","first-page":"2975","DOI":"10.1073\/pnas.94.7.2975","article-title":"Crystal structure of desheptapeptide(B24\u2013B30)insulin at 1.6 \u00c5 resolution: implications for receptor binding","volume":"94","author":"Bao","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021111900575442500_B15","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1107\/S0907444997004034","article-title":"Structure of monomeric porcine DesB1\u2013B2 despentapeptide (B26\u2013B30) insulin at 1.65 \u00c5 resolution","volume":"53","author":"Diao","year":"1997","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."},{"key":"2021111900575442500_B16","doi-asserted-by":"crossref","first-page":"679","DOI":"10.1038\/333679a0","article-title":"Monomeric insulins obtained by protein engineering and their medical implications","volume":"333","author":"Brange","year":"1988","journal-title":"Nature"},{"key":"2021111900575442500_B17","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1107\/S0907444901018455","article-title":"Crystallization and preliminary crystallographic investigation of a low-pH native insulin monomer with flexible behaviour","volume":"58","author":"Zhang","year":"2002","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."},{"key":"2021111900575442500_B18","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/0022-2836(91)90022-X","article-title":"X-ray analysis of the single chain B29\u2013A1 peptide-linked insulin molecule: a completely inactive analogue","volume":"220","author":"Derewenda","year":"1991","journal-title":"J. Mol. Biol."},{"key":"2021111900575442500_B19","doi-asserted-by":"crossref","first-page":"12041","DOI":"10.1021\/bi990700k","article-title":"Structural consequences of the B5 histidine\u2192tyrosine mutation in human insulin characterized by X-ray crystallography and conformational analysis","volume":"38","author":"Tang","year":"1999","journal-title":"Biochemistry"},{"key":"2021111900575442500_B20","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1107\/S0907444906006871","article-title":"I222 crystal form of despentapeptide (B26\u2013B30) insulin provides new insights into the properties of monomeric insulin","volume":"62","author":"Whittingham","year":"2006","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."},{"key":"2021111900575442500_B21","first-page":"1","article-title":"Molecular recognition through isosteric interaction: implication from studies on insulin","volume":"32","author":"Zhang","year":"2000","journal-title":"Shengwu Huaxue Yu Shengwu Wuli Xuebao"},{"key":"2021111900575442500_B22","doi-asserted-by":"crossref","first-page":"16293","DOI":"10.1021\/bi048856u","article-title":"Toward the insulin\u2013IGF-I intermediate structures: functional and structural properties of the [TyrB25NMePheB26] insulin mutant","volume":"43","author":"\u017d\u00e1kov\u00e1","year":"2004","journal-title":"Biochemistry"},{"key":"2021111900575442500_B23","doi-asserted-by":"crossref","first-page":"1966","DOI":"10.1073\/pnas.0911785107","article-title":"Implications for the active form of human insulin based on the structural convergence of highly active hormone analogues","volume":"107","author":"Jir\u00e1cek","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"2021111900575442500_B24","article-title":"Knowledge, networks and nations","author":"Royal Society","year":"2011"},{"key":"2021111900575442500_B25","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1107\/S0108768190009570","article-title":"Structure of the pig insulin dimer in the cubic crystal","volume":"47","author":"Badger","year":"1991","journal-title":"Acta Crystallogr. Sect. B Struct. Sci."}],"container-title":["Biochemical Society Transactions"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article-pdf\/39\/5\/1313\/551829\/bst0391313.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"syndication"},{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article-pdf\/39\/5\/1313\/551829\/bst0391313.pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2021,11,19]],"date-time":"2021-11-19T00:59:45Z","timestamp":1637283585000},"score":1,"resource":{"primary":{"URL":"https:\/\/portlandpress.com\/biochemsoctrans\/article\/39\/5\/1313\/87066\/Biochemical-contacts-and-collaborations-between"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2011,9,21]]},"references-count":25,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2011,9,21]]},"published-print":{"date-parts":[[2011,10,1]]}},"URL":"https:\/\/doi.org\/10.1042\/bst0391313","relation":{},"ISSN":["0300-5127","1470-8752"],"issn-type":[{"value":"0300-5127","type":"print"},{"value":"1470-8752","type":"electronic"}],"subject":[],"published":{"date-parts":[[2011,9,21]]}}}