从编辑角度分析如何提高科技论文的质量

科技论文是科研成果交流和延续的载体,其质量是衡量个人、科研单位乃至国家学术水平的重要指标。文章根据科技论文的特点,结合多年从事科技期刊编辑工作的经验,从如何确保论文学术水平、选题方向和写作思路、杜绝学术不端、保护知识产权等方面进行了阐述,并就科技论文撰写过程中应该注意的几个问题：科技论文的层次结构、语言表达和写作水平、确保数据真实有效和可重复性、表格插图的规范使用、规范参考文献的著录格式,从编辑角度分析了如何提高科技论文的质量,以期为科技论文的撰写提供参考。     

The effect of local application of homocysteine on neuronal activity in the central nervous system of the rat

Homocysteine, a monocarboxylic, sulfur-containing amino acid, produces convulsions in rats and mice when administered systemically. Convulsions and high serum concentrations of homocysteine are among the symptoms that characterize patients with homocystinuria, a hereditary disorder of amino acid metabolism. In order to evaluate the effects of homocysteine on the central nervous system directly, extracellular recordings were made from neurons in rat cerebral cortex, cerebellum and midbrain during local application of homocysteine by pressure ejection or iontophoresis. Both methods of drug delivery produced dose-dependent increases in the activity of neurons in every area tested. Activity was increased by D, L-homocysteine and L-glutamate in 67 percent of cells tested with both drugs. The doses required to produce equivalent excitations in this group of cells were similar, suggesting that homocysteine is at least as potent as glutamate. The excitatory effects of both homocysteine and glutamate were antagonized by local application of betaine, a biological methyl donor which blocks convulsions produced by systematic administration of pentylenetetrazol and electroshock as well as homocysteine. The effects of local application of homocysteine were also blocked by local application of the glutamate antagonist glutamate diethylester (GDEE). In 6 of 7 cells tested, GDEE appeared to preferentially affect homocysteine-induced excitations. These data indicate that homocysteine has an excitatory action on neurons, a finding which may account for some of the symptoms associated with certain disorders of amino acid metabolism.     

A primary role for microfilaments, but not microtubules, in hormone-induced cytoplasmic retraction

The distributions of microfilaments and microtubules were studied during transient hormone-induced changes in cell shape (retraction-respreading). Two cell types (fibroblasts and bone cells), differentially responsive to parathyroid hormone (PTH) and prostaglandin E₂ (PGE₂), were analysed. The cytoplasm of fibroblasts retracted in response to PGE₂ but not PTH, whereas bone cells could respond to both PGE₂ and PTH. Time-lapse photomicrography indicated that the retraction began within minutes of hormone addition, while respreading occurred over longer times, up to 8 h. Affinity-purified actin and tubulin antibodies were used to follow the appearance of microtubules and microfilaments during both the retraction and the respreading phases. Microtubules appeared not to reorganize noticeably, although they were squeezed closer together in cellular pseudopods; no extensive loss or growth was detectable. Microfilaments did alter drastically their appearance and distributions. Soon after hormone addition when earliest detectable cytoplasmic retraction was evident, microfilament bundles appeared to break down. Remaining microfilament bundles consisted of relatively short, non-aligned fragments or aggregates. During respreading, microfilament bundles regrew and realigned throughout the cytoplasm. These data suggest a primary role for microfilaments, but probably not microtubules, in these cell shape changes.     

Model of serine proteases charge relay system - pcilo study

The PCILO (Perturbative Configuration Interaction Using Localized Orbitals) method has been used to determine the electronic structure of the active center of serine proteases. The results show that the carboxyl group of the aspartic acid residue is the ultimate proton acceptor of the catalytic triad (Asp, His, Ser)^?. In the absence of a substrate the negative charge of the active centre is delocalized, causing polarization of the Ser O^γ-H bond and an increase of the nucleophilicity of the O^γ atom. The proton of the O^γ-H bond of the Ser residue is, however, only partially transferred to the N^?2 atom of imidazole His. The hydration of the model charge relay system is also investigated.