Interactions between Jacques Monod and Jeffries Wyman (or the burdens of co-authorship)

被引：12

作者：

Buc H. ^{[1
]}

机构：

[1] Institut Pasteur, Bat. MA, 75724 Paris Cedex 15, 25, rue du Dr. Roux

来源：

Rendiconti Lincei | 2006年 / 1-2卷 / 31-49期

关键词：

Allosteric theory; Co-authorship; History of science;

D O I：

10.1007/BF02904500

中图分类号：

学科分类号：

摘要：

Several preliminary versions of the article describing the model put forward by Jacques Monod, Jeffries Wyman and Jean-Pierre Changeux to account for the properties of regulatory enzymes have been preserved in the Archives of the Institut Pasteur in Paris. As a result, it has been possible to reconstitute a rather precise chronology of the main scientific events that led to the elaboration of this model. I am describing here the scientific interactions that took place between Jeffries Wyman and Jacques Monod from January 1963 to January 1965 on key issues concerning the structure and function of oligomeric proteins. © 2006 Springer.

引用

页码：31 / 49

页数：18

共 17 条

[1]

Monod J.(1965)On the nature of allosteric transitions: A plausible model J. Mol. Biol. 12 88-118

[2]

Wyman J.(1996)Meanings in Search of Experiments and Vice-Versa: The Invention of Allosteric Regulation in Paris and Berkeley, 1959–1968 Historical Studies in the Physical and Biological Sciences 27 1-89

[3]

Changeux J.P.(1995)Allosteric proteins: from regulatory enzymes to receptors-personal recollections Bioassays 9 625-634

[4]

Creager N.(1963)Allosteric proteins and cellular control systems J. Mol. Biol. 6 306-329

[5]

Gaudillière J.P.(1999)Hemoglobin is an honorary enzyme TIBS 24 158-161

[6]

Changeux J.P.(1948)Heme proteins Adv. Prot. Chem. 4 407-531

[7]

Monod J.(1951)On hemoglobin and the basis of the Bohr effect J. Polymer Sci. 7 499-518

[8]

Changeux J.P.(1963)Allosteric effects in hemoglobin Cold Spr. Harb. Symp. Quant. Biol. 28 483-489

[9]

Jacob F.(1964)Linked functions and reciprocal effects in hemoglobin: a second look Adv. Prot. Chem. 19 223-286

[10]

Brunori M.(2000)Structural symmetry and protein function Annu. Rev. Biophys. Biomol. Struct. 29 105-153

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