Purification and activity assays of the catalytic domains of the kinase/endoribonuclease Ire1p from Saccharomyces cerevisiae.
Nock
S
S
Department of Biochemistry and Biophysics, Howard Hughes Medical Institute, University of California, San Francisco, California 94143, USA.
Gonzalez
T N
TN
Sidrauski
C
C
Niwa
M
M
Walter
P
P
D001483:Base Sequence; D020134:Catalytic Domain; D002853:Chromatography, Liquid; D004722:Endoribonucleases / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D004926:Escherichia coli / Q000378:metabolism; D005656:Fungal Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D009838:Oligodeoxyribonucleotides; D011494:Protein Kinases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D017346:Protein Serine-Threonine Kinases; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins
D005656:Fungal Proteins; D008562:Membrane Glycoproteins; D009838:Oligodeoxyribonucleotides; D011994:Recombinant Proteins; D029701:Saccharomyces cerevisiae Proteins; D011494:Protein Kinases; C082863:IRE1 protein, S cerevisiae; D017346:Protein Serine-Threonine Kinases; D004722:Endoribonucleases