Malondialdehyde < Mammals < Mammary Glands, Animal

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List of bibliographic references indexed by Mammals

Number of relevant bibliographic references: 10.

Ident.	Authors (with country if any)	Title
000302 (2017)	Lianqin Li [République populaire de Chine]	The Relevance of Mammalian Peroxiredoxins to the Gametogenesis, Embryogenesis, and Pregnancy Outcomes.
000752 (2013)	Lena Dorothee Schütte [Allemagne] ; Stefan Baumeister ; Benjamin Weis ; Christoph Hudemann ; Eva-Maria Hanschmann ; Christopher Horst Lillig	Identification of potential protein dithiol-disulfide substrates of mammalian Grx2.
000881 (2012)	Marco Mariotti [États-Unis] ; Perry G. Ridge ; Yan Zhang ; Alexei V. Lobanov ; Thomas H. Pringle ; Roderic Guigo ; Dolph L. Hatfield ; Vadim N. Gladyshev	Composition and evolution of the vertebrate and mammalian selenoproteomes.
000A67 (2009)	Yves Meyer [France] ; Bob B. Buchanan ; Florence Vignols ; Jean-Philippe Reichheld	Thioredoxins and glutaredoxins: unifying elements in redox biology.
000E95 (2004)	Dan Su [États-Unis] ; Vadim N. Gladyshev	Alternative splicing involving the thioredoxin reductase module in mammals: a glutaredoxin-containing thioredoxin reductase 1.
001066 (2000)	P G Board [Australie] ; M. Coggan ; G. Chelvanayagam ; S. Easteal ; L S Jermiin ; G K Schulte ; D E Danley ; L R Hoth ; M C Griffor ; A V Kamath ; M H Rosner ; B A Chrunyk ; D E Perregaux ; C A Gabel ; K F Geoghegan ; J. Pandit	Identification, characterization, and crystal structure of the Omega class glutathione transferases.
001112 (1999)	A. Miranda-Vizuete [Suède] ; J R Pedrajas ; A E Damdimopoulos ; G. Spyrou	Cloning and sequencing of mouse glutaredoxin (grx) cDNA.
001113 (1999)	H Z Chae [Corée du Sud] ; H J Kim ; S W Kang ; S G Rhee	Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin.
001239 (1994)	V V Papov ; S A Gravina ; J J Mieyal ; K. Biemann	The primary structure and properties of thioltransferase (glutaredoxin) from human red blood cells.
001249 (1994)	W W Wells [États-Unis] ; D P Xu	Dehydroascorbate reduction.

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