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Crystallization and preliminary crystallographic studies of the NCoA-1/SRC-1 PAS-B domain bound to the LXXLL motif of the STAT6 transactivation domain
British Library Online Contents | 2004| -
Identifying a recombinant alkyldihydroxyacetonephosphate synthase suited for crystallographic studies
British Library Online Contents | 2007| -
Structural Basis for the Inhibitory Role of Tomosyn in Exocytosis
British Library Online Contents | 2004| -
Catalysis uncoupling in a glutamine amidotransferase bienzyme by unblocking the glutaminase active site
Free accessBASE | 2012| -
Catalysis Uncoupling in a Glutamine Amidotransferase Bienzyme by Unblocking the Glutaminase Active Site
British Library Online Contents | 2012| -
Expression, purification, crystallization and preliminary crystallographic studies of the Enterococcus faecalis cytolysin repressor CylR2
British Library Online Contents | 2004| -
The Crucial Step in Ether Phospholipid Biosynthesis: Structural Basis of a Noncanonical Reaction Associated with a Peroxisomal Disorder
British Library Online Contents | 2007| -
Development of a Very Low-Noise Cryogenic Preamplifier for Large-Area SiPM Devices
British Library Online Contents | 2018| -
Domain Closure, Substrate Specificity and Catalysis of D-Lactate Dehydrogenase from Lactobacillus bulgaricus
British Library Online Contents | 2002| -
Performance of Hamamatsu VUV4 SiPMs for detecting liquid argon scintillation
IOP Institute of Physics | 2022| -
The Borexino Muon Detector and Muon Induced Backgrounds
British Library Conference Proceedings | 2002| -
The Borexino read out electronics and trigger system
British Library Conference Proceedings | 2001| -
NCoA-1/SRC-1 is an essential coactivator for the cytokine induced signal transducers and activators of transcription (STATs) and binds to a specific interface motif
British Library Conference Proceedings | 2003| -
Roles of His205, His296, His303 and Asp259 in catalysis by NAD^+ -specific D-lactate dehydrogenase
British Library Online Contents | 2000| -
Role of the His57-Glu214 Ionic Couple Located in the Active Site of Mycobacterium tuberculosis FprA
British Library Online Contents | 2006|
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