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Unravelling the Carbohydrate‐Binding Preferences of the Carbohydrate‐Binding Modules of AMP‐Activated Protein Kinase
ChemBioChem ( IF 2.6 ) Pub Date : 2018-01-09 , DOI: 10.1002/cbic.201700589 Jesse I. Mobbs 1, 2, 3 , Alex Di Paolo 1, 2, 4 , Riley D. Metcalfe 1, 2 , Emily Selig 1, 2 , David I. Stapleton 1, 2 , Michael D. W. Griffin 1, 2 , Paul R. Gooley 1, 2
ChemBioChem ( IF 2.6 ) Pub Date : 2018-01-09 , DOI: 10.1002/cbic.201700589 Jesse I. Mobbs 1, 2, 3 , Alex Di Paolo 1, 2, 4 , Riley D. Metcalfe 1, 2 , Emily Selig 1, 2 , David I. Stapleton 1, 2 , Michael D. W. Griffin 1, 2 , Paul R. Gooley 1, 2
Affiliation
Ancient conservation: The β subunit of adenosine monophosphate (AMP)‐activated protein kinase, which exists as two isoforms (β1 and β2) in humans, has a carbohydrate‐binding module that interacts with glycogen. Investigations through ancestral sequence reconstruction and mutagenesis reveal conserved residues for carbohydrate binding.
中文翻译:
揭示AMP活化蛋白激酶的糖结合模块的糖结合偏好
古代保护:腺苷一磷酸(AMP)激活的蛋白激酶的β亚基以两种同种型(β1和β2)存在于人类中,具有与糖原相互作用的碳水化合物结合模块。通过祖先序列重建和诱变的研究揭示了与碳水化合物结合的保守残基。
更新日期:2018-01-09
中文翻译:
揭示AMP活化蛋白激酶的糖结合模块的糖结合偏好
古代保护:腺苷一磷酸(AMP)激活的蛋白激酶的β亚基以两种同种型(β1和β2)存在于人类中,具有与糖原相互作用的碳水化合物结合模块。通过祖先序列重建和诱变的研究揭示了与碳水化合物结合的保守残基。