prevents < primary < primes

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List of bibliographic references indexed by primary

Number of relevant bibliographic references: 9.

Ident.	Authors (with country if any)	Title
000411 (2016)	Laura A. Walters [États-Unis] ; Matthew A. Escobar [États-Unis]	The AtGRXS3/4/5/7/8 glutaredoxin gene cluster on Arabidopsis thaliana chromosome 4 is coordinately regulated by nitrate and appears to control primary root growth.
000439 (2016)	Kurt Patterson ; Laura A. Walters ; Andrew M. Cooper ; Jocelyn G. Olvera ; Miguel A. Rosas ; Allan G. Rasmusson ; Matthew A. Escobar [États-Unis]	Nitrate-Regulated Glutaredoxins Control Arabidopsis Primary Root Growth.
000798 (2012)	Karouk Said [Suède] ; Hans Glaumann ; Mikael Björnstedt ; Annika Bergquist	The value of thioredoxin family proteins and proliferation markers in dysplastic and malignant gallbladders in patients with primary sclerosing cholangitis.
001093 (1999)	J. Shi [États-Unis] ; A. Vlamis-Gardikas ; F. Aslund ; A. Holmgren ; B P Rosen	Reactivity of glutaredoxins 1, 2, and 3 from Escherichia coli shows that glutaredoxin 2 is the primary hydrogen donor to ArsC-catalyzed arsenate reduction.
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.
001275 (1992)	S C Mcfarlan ; C A Terrell ; H P Hogenkamp	The purification, characterization, and primary structure of a small redox protein from Methanobacterium thermoautotrophicum, an archaebacterium.
001344 (1987)	Z R Gan ; W W Wells	The primary structure of pig liver thioltransferase.
001360 (1984)	I M Klintrot ; J O Höög ; H. Jörnvall ; A. Holmgren ; M. Luthman	The primary structure of calf thymus glutaredoxin. Homology with the corresponding Escherichia coli protein but elongation at both ends and with an additional half-cystine/cysteine pair.
001363 (1983)	J O Höög ; H. Jörnvall ; A. Holmgren ; M. Carlquist ; M. Persson	The primary structure of Escherichia coli glutaredoxin. Distant homology with thioredoxins in a superfamily of small proteins with a redox-active cystine disulfide/cysteine dithiol.

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