Actin: Structure and Function in Muscle and Non-Muscle Cells. Proceedings of an International Seminar, Held in Conjuction with the 12th International Congress of Biochemistry, at The University Sydney, 23-25 August 1982.Cristobal G. dos Remedios, Julian A. Barden

1984 ◽  
Vol 59 (2) ◽  
pp. 169-170
Author(s):  
Carl Moos
2018 ◽  
Vol 28 (2) ◽  
pp. 120-123
Author(s):  
Dugald Gardner

William Rutherford Sanders spent a childhood and early student days divided between Edinburgh and Montpelier, France before graduating in Medicine in Edinburgh. An early interest in the spleen was encouraged by a two-year period in Europe where he became familiar with the work of Helmholtz, Bernard and Henle. Returning to Edinburgh, his growing experience led to the position of assistant in the Infirmary pathology department. He conducted classes in the University of Edinburgh and on behalf of the Royal Colleges became familiar with the museum of the Royal College of Surgeons where he was chosen as Conservator in 1853. Criticised by 20th century historians for concentrating on verbal teaching rather than on the conservation of the museum, Sanders became a consultant physician to the Royal Infirmary in 1861 and in 1869 Professor of General Pathology. Throughout these years, Sanders gave as much time as possible to the study of the structure and function of the spleen and to neurological disorders such as hemiplegia. His later life was interrupted by a series of illnesses commencing with an abdominal abscess. A prolonged convalescence allowed the resumption of work but deranged vision and hemiplegia preceded his death on 18 February 1881.


2007 ◽  
Vol 282 (50) ◽  
pp. 36133-36137 ◽  
Author(s):  
Emil Reisler ◽  
Edward H. Egelman

1937 ◽  
Vol 59 (1) ◽  
pp. 119-164 ◽  
Author(s):  
Vera Fretter

The work described in this paper was carried out in the Department of Zoology of Birkbeck College, University of London, and at the Marine Laboratories at Plymouth and Port Erin. I wish to acknowledge my indebtedness to the University of London for the use of their table at Plymouth, to Birkbeck College for a grant of £5 towards the illustrations, and, in particular, I would express my gratitude to Mr Graham, under whose direction the work was carried out, for his continued kindness and help.The specimens of Lepidochitona cinereus which were used for the investigation were collected at Bangor, Plymouth and Port Erin, and also obtained from Cullercoats. Most of the material from Plymouth and one specimen from Cullercoats was infected with the Haplosporidian parasite Haplosporidium chitonis (Debaisieux, 1920) and was therefore unreliable for histological and physiological work. Specimens of Acanthochitona crinitus were collected at Plymouth, and showed no sign of infection with Haplosporidium chitonis; a few, however, were slightly parasitised with another Sporozoan. The Californian species Ischnochiton magdalenensis and Cryptochiton stelleri were obtained from Turtox General Biological Supply House, Chicago. Specimens of these species were fixed in formalin, which proved to be a poor fixative for histological work.


2012 ◽  
Vol 27 ◽  
pp. 355-359 ◽  
Author(s):  
S. Ramos ◽  
J. J. G. Moura ◽  
M. Aureliano

The studies about the interaction of actin with vanadium are seldom. In the present paper the effects of vanadyl, vanadate, and decavanadate in the actin structure and function were compared. Decavanadate clearly interacts with actin, as shown byV51-NMR spectroscopy. Decavanadate interaction with actin induces protein cysteine oxidation and vanadyl formation, being both prevented by the natural ligand of the protein, ATP. Monomeric actin (G-actin) titration with vanadyl, as analysed by EPR spectroscopy, indicates a 1 : 1 binding stoichiometry and akdof 7.5 μM. Both decavanadate and vanadyl inhibited G-actin polymerization into actin filaments (F-actin), with aIC50of 68 and 300 μM, respectively, as analysed by light-scattering assays. However, only vanadyl induces G-actin intrinsic fluorescence quenching, which suggests the presence of vanadyl high-affinity actin-binding sites. Decavanadate increases (2.6-fold) actin hydrophobic surface, evaluated using the ANSA probe, whereas vanadyl decreases it (15%). Finally, both vanadium species increasedε-ATP exchange rate (k=6.5×10−3and4.47×10−3 s−1for decavanadate and vanadyl, resp.). Putting it all together, it is suggested that actin, which is involved in many cellular processes, might be a potential target not only for decavanadate but above all for vanadyl.


2021 ◽  
Vol 134 (8) ◽  

ABSTRACT First Person is a series of interviews with the first authors of a selection of papers published in Journal of Cell Science, helping early-career researchers promote themselves alongside their papers. Fumiya Okawa, Yutaro Hama and Sidi Zhang are co-first authors on ‘Evolution and insights into the structure and function of the DedA superfamily containing TMEM41B and VMP1’, published in JCS. Fumiya and Yutaro are PhD students and Sidi is a postdoc in the lab of Noboru Mizushima at the Department of Biochemistry and Molecular Biology, Graduate School of Medicine, The University of Tokyo, Japan, where they are investigating the molecular mechanisms and origin of autophagy.


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