传动方案设计专家系统的智能模型与关键技术

分析了传动方案设计的特点，探讨了如何利用人工智能理论及专家系统与常规ＣＡＤ技术解决传动方案设计问题。并给出了智能模型的建立及知识表示、约束推理、参数设计、多方案设计与布置设计的原理与方法。     

用Ω展开方法讨论化学体系的涨落

运用ＶａｎＫａｍｐｅｎ提出的Ω展开方法，对两个化学反应系统：进行了研究，建立了这两个反应系统组分浓度的一阶矩和二阶矩。     

大坝变形信息判据与分析

应用概率统计原理，对水库大坝变形观测中的变形值与随机因素干扰建立了变形数学模型。为排除干扰，提取真正变形信息，正确判据和分析大坝变形状态与规律提供理论依据。该数学模型在水库的实际应用中获得良好效果。     

求解k阶线性递归方程组的一种更有效的并行算法

将求解ｋ（ｋ≥２）阶线性递归方程组问题转化为求矩阵序列部分积问题，在ＳＩＭＤ共享存储模型上提出了求解ｋ阶线性递归方程组的一种新的有效并行算法．研究表明，本算法的加速和效率比现有算法均有较大的改善．     

使过半数规则具有传递性的偏好断面的规模

证明了当ｎ＞３时，使过半数投票表决的结果具有传递性的个人偏好序的最大数目大于２￣（ｎ－），从而否定了Ｃｒａｖｅｎ猜想。文中给出了最大偏好序的递推公式以及确定相应约束集的三条规则。     

应用扩展的Monod模型关联醋酸菌比生长速率

应用扩展的Ｍｏｎｏｄ模型关联了醋酸菌ＩＡＭ１８０２和Ｍ２３的比生长速率，ＩＡＭ１８０２的比生长速率关联式为μ＝０．４８７（１－ＣＰ／２３．８）＾０．２４８ＣＡ／ＣＭ＋ＣＡ；Ｍ２３的关联式为μ＝０．５６８（１－ＣＰ／６１．０）＾０．３０６ＣＡ／ＣＭ＋ＣＡ除临界生长抑制剂浓度附近外，模型良好地表达了两种醋力的比生长速率。     

A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitors

The amyloid proteins isolated from neuritic plaques and the cerebrovasculature of Alzheimer's disease are self-aggregating moieties termed A4 protein and beta-protein, respectively. A putative A4 amyloid precursor (herein termed A4(695] has been characterized by analysis of a human brain complementary DNA. We report here the sequence of a closely related amyloid cDNA, A4(751), distinguished from A4(695) by the presence of a 168 base-pair (bp) sequence which adds 57 amino acids to, and removes one residue from, the predicted A4(695) protein. The peptide predicted from this insert is very similar to the Kunitz family of serine proteinase inhibitors. The two A4-specific messenger RNAs are differentially expressed: in a limited survey, A4(751) mRNA appears to be ubiquitous, whereas A4(695) mRNA has a restricted pattern of expression which includes cells from neuronal tissue. These data may have significant implications for understanding amyloid deposition in Alzheimer's disease.     

Insulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase II

Ribosomal protein S6 is a component of the eukaryotic 40S ribosomal subunit that becomes phosphorylated on multiple serine residues in response to a variety of mitogens, including insulin, growth factors, and transforming proteins of many oncogenic viruses. Recently, an activated S6 kinase (S6 K II) has been purified to homogeneity from Xenopus eggs, and characterized immunologically and at the molecular level. Purified S6 K II can be deactivated in vitro by incubation with either protein phosphatase 1 or protein phosphatase 2A. Reactivation and phosphorylation of S6 K II occurs in vitro with an insulin-stimulated microtubule-associated protein-2 (MAP-2) protein kinase which is itself a phosphoprotein that can be deactivated by protein phosphatase 2A. These studies suggest that a step in insulin signalling involves sequential activation by phosphorylation of at least two serine/threonine protein kinases.     

Protease inhibitor domain encoded by an amyloid protein precursor mRNA associated with Alzheimer's disease

Amyloid B-protein/amyloid A4 is a peptide present in the neuritic plaques, neurofibrillary tangles and cerebrovascular deposits in patients with Alzheimer's disease and Down's syndrome (trisomy 21) and may be involved in the pathogenesis of Alzheimer's disease. Recent molecular genetic studies have indicated that amyloid protein is encoded as part of a larger protein by a gene on human chromosome 21 (refs 6-9). The amyloid protein precursor (APP) gene is expressed in brain and in several peripheral tissues, but the specific biochemical events leading to deposition of amyloid are not known. We have now screened complementary DNA libraries constructed from peripheral tissues to determine whether the messenger RNA encoding APP in these tissues is identical to that expressed in brain, and we identify a second APP mRNA that encodes an additional internal domain with a sequence characteristic of a Kunitz-type serine protease inhibitor. The alternative APP mRNA is present in both brain and peripheral tissues of normal individuals and those with Alzheimer's disease, but its pattern of expression differs from that of the previously reported APP mRNA.     

Novel precursor of Alzheimer's disease amyloid protein shows protease inhibitory activity

Alzheimer's disease is characterized by cerebral deposits of amyloid beta-protein (AP) as senile plaque core and vascular amyloid, and a complementary DNA encoding a precursor of this protein (APP) has been cloned from human brain. From a cDNA library of a human glioblastoma cell line, we have isolated a cDNA identical to that previously reported, together with a new cDNA which contains a 225-nucleotide insert. The sequence of the 56 amino acids at the N-terminal of the protein deduced from this insert is highly homologous to the basic trypsin inhibitor family, and the lysate from COS-1 cells transfected with the longer APP cDNA showed an increased inhibition of trypsin activity. Partial sequencing of the genomic DNA encoding APP showed that the 225 nucleotides are located in two exons. At least three messenger RNA species, apparently transcribed from a single APP gene by alternative splicing, were found in human brain. We suggest that protease inhibition by the longer APP(s) could be related to aberrant APP catabolism.