Edmund R.S. Kunji

Prof. Edmund R.S. Kunji


Research Focus & Metrics

Academic Career Length

34Years (1993-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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28 March 2018 in Nature
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Journal Article
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EMEvanna L. Mills
Evanna L. Mills
DRDylan G. Ryan
Dylan G. Ryan
HPHiran A. Prag
Hiran A. Prag
DDDina Dikovskaya
Dina Dikovskaya
DMDeepthi Menon
Deepthi Menon
LOLuke A. O’neill
Luke A. O’neill

6 July 2012 in Science
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Journal Article
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SHSébastien Herzig
Sébastien Herzig
EREtienne Raemy
Etienne Raemy
SMSylvie Montessuit
Sylvie Montessuit
JVJean-Luc Veuthey
Jean-Luc Veuthey
NZNicola Zamboni
Nicola Zamboni
JMJean-claude Martinou
Jean-claude Martinou
Letting Pyruvate In: Transport of pyruvate is an important event in metabolism whereby the pyruvate formed in glycolysis is transported into mitochondria to feed into the tricarboxylic acid cycle (see the Perspective by Murphy and Divakaruni ). Two groups have now identified proteins that are components of the mitochondrial pyruvate transporter. Bricker et al. (p. 96 , published online 24 May) found that the proteins mitochondrial pyruvate carrier 1 and 2 (MPC1 and MPC2) are required for full pyruvate transport in yeast and Drosophila cells and that humans with mutations in MPC1 have metabolic defects consistent with loss of the transporter. Herzig et al. (p. 93 , published online 24 May) identified the same proteins as components of the carrier in yeast. Furthermore, expression of the mouse proteins in bacteria conferred increased transport of pyruvate into bacterial cells.

1 October 1996 in Antonie van Leeuwenhoek
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EKEdmund R.S. Kunji
Edmund R.S. Kunji
IMIgor Mierau
Igor Mierau
AHAnja Hagting
Anja Hagting
BPBert Poolman
Bert Poolman
WKWil N. Konings
Wil N. Konings

29 November 2019 in Trends in Biochemical Sciences
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Journal Article
Open access
JRJonathan J. Ruprecht
Jonathan J. Ruprecht
EKEdmund R.S. Kunji
Edmund R.S. Kunji
Members of the mitochondrial carrier family (SLC25) provide the transport steps for amino acids, carboxylic acids, fatty acids, cofactors, inorganic ions, and nucleotides across the mitochondrial inner membrane and are crucial for many cellular processes. Here, we use new insights into the transport mechanism of the mitochondrial ADP/ATP carrier to examine the structure and function of other mitochondrial carriers. They all have a single substrate-binding site and two gates, which are present on either side of the membrane and involve salt-bridge networks. Transport is likely to occur by a common mechanism, in which the coordinated movement of six structural elements leads to the alternating opening and closing of the matrix or cytoplasmic side of the carriers.

1 April 2006 in Nature Methods
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DDDavid Drew
David Drew
MLMirjam Lerch
Mirjam Lerch
EKEdmund R.S. Kunji
Edmund R.S. Kunji
DSDirk-Jan Slotboom
Dirk-Jan Slotboom
JGJan-Willem de Gier
Jan-Willem de Gier

8 April 2011 in Nature Biotechnology
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Roslyn BillRoslyn Bill
Roslyn Bill
PHPeter J F Henderson
Peter J F Henderson
SISo Iwata
So Iwata
EKEdmund R.S. Kunji
Edmund R.S. Kunji
HMHartmut Michel
Hartmut Michel
HVHorst Vogel
Horst Vogel