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神经肽与神经营养因子-神经科学百科全书-3 版权信息
- ISBN:9787030280879
- 条形码:9787030280879 ; 978-7-03-028087-9
- 装帧:暂无
- 册数:暂无
- 重量:暂无
- 所属分类:>>
神经肽与神经营养因子-神经科学百科全书-3 本书特色
《神经科学百科全书3:神经肽与神经营养因子(影印版·导读版)》:原书篇幅巨大,为所有神经科学百科全书之首。由来自世界各地的2400多位专家撰稿人合力打造,覆盖了神经科学全部主要领域。书中每个词条在收入书中之前均经过顾问委员会的同行评议。词条中均含有词汇表、引言、参考文献和丰富的交叉参考内容。主编为著名神经科学家、美国神经科学学会前主席Larry R.Squire。内容平易,本科生即可读懂。深度和广度独一无二,足可满足专家学者的需要。导读版精选原书中的部分主题,按内容重新编排,更适合国内读者购买和阅读。
神经肽与神经营养因子-神经科学百科全书-3 目录
神经肽与神经营养因子-神经科学百科全书-3 节选
《神经科学百科全书3:神经肽与神经营养因子(影印版·导读版)》旨在将本学科丰富多元的内容条理化并仔细介绍,从而推动不同学术分支之间的沟通,提供权威的信息来源。该书面向较为广泛的读者群体,既包括初入神经科学研究的学生,也包括寻求特定专题知识的普通读者。无论是神经科学家,还是正在学习神经科学的本科生和研究生,或生命科学领域的教师、科普作家,都会从该参考书中获益。
神经肽与神经营养因子-神经科学百科全书-3 相关资料
插图:A core of gene clusters within the granular glandcells of frog skin codes for these secreted peptides.A mild transdermal electrical stimulation of the frogreleases granular gland contents on the skin surface asa result of glandular syncythia rupture produced bythe contraction of myoepithelial cells surrounding theglands. These skin secretions contain the entire pepti-dome, transcriptome, and genome of the granulargland syncythia (olocryne secretion). The polyadeny-lated mRNAs constituting the secreted transcriptomeand the peptides constituting the secreted proteomeare protected from degradation by interactionswith co-released amphipathic peptides and muco-proteins endowed with antimicrobial, RNAse-, andprotease-inhibitory activities. Thus, amino acid se-quencing of secreted peptides, nucleic acid sequencingof peptide-encoding mRNAs, and genomic informa-tion retrieving from the secreted DNA can be easilyperformed in secretion samples collected from fewfrogs on a regular basis and stored, lyophilized orfrozen, for at least 6 years. This is a powerful methodof determining evolutionary information on theancestral sequences of biologically active peptidesand proteins and understanding the sequence-function relationship of the human orthologs. Becausedifficult-to-synthesize bioactive peptides and proteinsare currently obtained in large quantities from skinsecretions of few amphibian specimens, extensivepharmacological studies have been performed withthese amphibian molecules in order to elucidate thefunctional role of the mammalian orthologs. Whereassome of amphibian skin peptides represent analogs ofalready known mammalian peptide families (Table 1),others represent prototype peptides not encounteredbefore in nature. In many instances, the discovery ofnew amphibian skin peptides led to the discovery ofnovel mammalian neuropeptides; notable examplesare caerulein, bombesin, and sauvagin (Table 2). Inthe amphibian skin, opioid peptides are representedby two prototypes named dermorphin and deltorphin.
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