A synthetic lectin for O-linked beta-N-acetylglucosamine.
A synthetic lectin for O-linked beta-N-acetylglucosamine.
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DOI：
10.1002/anie.200804905
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发表时间：
2009
影响因子：
16.6
通讯作者：
Davis, Anthony P.
中科院分区：
文献类型：
--
作者：
Ferrand, Yann;Klein, Emmanuel;Barwell, Nicholas P.;Crump, Matthew P.;Jimenez-Barbero, Jesus;Vicent, Cristina;Boons, Geert-Jan;Ingale, Sampat;Davis, Anthony P.
Yann Ferrand、Emmanuel Klein、Nicholas P. Barwell、Matthew P. Crump、Jesus JimØnez-Barbero、Cristina Vicent、Geert-Jan Boons、Sampat Ingale 和 Anthony P. Davis* β-N-乙酰基-d-葡萄糖胺基 (β-GlcNAc, 1) 是生物化学中的常见基序。它是甲壳素 (2) 的单体构建单元，并且经常出现在其他寡糖结构中。它还通过与丝氨酸或苏氨酸的羟基连接在蛋白质调节中发挥独特的作用，如 3 所示。这种“O-GlcNAc”[1] 翻译后修饰是高度动态的 [2]，并与作为生物控制机制的蛋白质磷酸化进行了比较。它涉及基因转录、核运输、蛋白质翻译、[3] 信号转导、[4] 蛋白质-蛋白质相互作用的调节、[1, 4] 以及细胞内营养水平的感知。 [5] O-GlcNAc 失调会导致重要人类疾病的病因学，特别是糖尿病和神经系统疾病。 [2]布里斯托尔小组的研究目标是仿生碳水化合物受体[6]，这些受体能够通过非共价相互作用结合水中的糖类。这个目标具有挑战性，因为常见的碳水化合物具有高度亲水性，因此本质上很难与其自然环境结合。事实上，凝集素 [7]（天然碳水化合物受体的主要类别）通常表现出适度的亲和力，对单糖的亲和力通常在毫摩尔范围内。 [8]我们特别关注糖类的 β-葡萄糖基家族的结合，其特征是极性官能团的“全赤道”阵列。我们的方法如方案 1a 所示。极地群叶的赤道位置
Yann Ferrand, Emmanuel Klein, Nicholas P. Barwell, Matthew P. Crump, Jesus JimØnez-Barbero, Cristina Vicent, Geert-Jan Boons, Sampat Ingale, and Anthony P. Davis* β-N-Acetyl-d-glucosaminyl (β-GlcNAc, 1) is a common motif in biological chemistry. It is the monomer building block for chitin (2), and occurs frequently in other oligosaccharide structures. It also plays a unique role in protein regulation through linkage to the hydroxy group of serine or threonine as in 3. This “O–GlcNAc”[1] posttranslational modification is highly dynamic [2] and draws comparisons with protein phosphorylation as a biological control mechanism. It has been implicated in gene transcription, nuclear trafficking, protein translation,[3] signal transduction,[4] the regulation of proteinprotein interactions,[1, 4] and the sensing of nutritional levels within the cell.[5] Dysregulation of O–GlcNAc contributes to the aetiology of important human diseases, particularly diabetes and neurological disorders.[2] Research in the Bristol group is aimed at biomimetic carbohydrate receptors [6] that are capable of binding saccharides in water through noncovalent interactions. This goal is challenging as the common carbohydrates are highly hydrophilic and therefore intrinsically difficult to bind from their natural environment. Indeed, lectins [7](the main class of natural carbohydrate receptors) often show modest affinities, which are typically in the millimolar range for monosaccharides.[8] We have focused especially on binding the β-glucosyl family of saccharides, characterized by “all-equatorial” arrays of polar functional groups. Our approach is illustrated in Scheme 1a. Equatorial positioning of the polar groups leaves
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影响因子：
4.8
作者：
Kreppel, LK;Hart, GW
通讯作者：
Hart, GW
影响因子：
15
作者：
Fernández, MD;Cañada, FJ;Cuevas, G
通讯作者：
Cuevas, G
影响因子：
2.9
作者：
BAINS, G;LEE, RT;FREIRE, E
通讯作者：
FREIRE, E
DOI：
10.1016/0005-2795(75)90313-x
发表时间：
1975-01-01
期刊：
BIOCHIMICA ET BIOPHYSICA ACTA
影响因子：
--
作者：
GOLDSTEIN, IJ;HAMMARSTROM, S;SUNDBLAD, G
通讯作者：
SUNDBLAD, G
影响因子：
5.6
作者：
LEVITT, M;PERUTZ, MF
通讯作者：
PERUTZ, MF