一种立体视觉图像的特征选择与匹配方法

从立体图像对中获取精确的三维信息需要进行相机建模、标定和图像点的匹配［１，２］．提出了特征点的选取；利用金字塔图像结构进行立体匹配，以及对匹配点进行整体性检验的准则。实验表明，该算法匹配速度快，错误概率小，匹配点在整个景物中分布均匀。     

基于小波包的信号检测算法

针对多个相似信号分量的到达时间检测问题提出了一种基于小波包理论的新算法（ＷａｖｅｌｅｔＰａｃｋｅｔｓＤｅｔｅｃｔｉｏｎＡｌｇｏｒｉｔｈｍ，ＷＰＤＡ）．即使在各信号分量严重重叠的情况下，该算法都能非常精确地确定各分量的到达时间。为了进行比较，引用了Ｂ．Ｆｒｉｅｄｌａｎｄｅｒ提出的改进Ｇａｂｏｒ表征方法（ＩＧＲＭ）及其信号模型。实验证明，小波包检测算法可以得到更为优越的性能。还讨论了小波包检测算法中的正交镜像滤波器选择问题。     

基于LPC预测误差DWT的语音基音检测

在对语音信号进行ＬＰＣ分析的基础上，提出了一种有效的语音基音周期检测算法。该算法利用小波变换中著名的Ｍａｌｌａｔ算法逐层分解ＬＰＣ预测误差信号，在最低分辨率的逼近信号中寻找峰值，然后逐层回溯各个分辨率的逼近信号，最后在ＬＰＣ预测误差中确定出峰值，从而求出相应的基音周期。     

Regulation of the retinal interphotoreceptor matrix Na by the retinal pigment epithelium during the light response

We examined the rabbit retinal pigment epithelium (RPE) for Na transport properties which would allow it to buffer undesirable changes in Na concentrations in the interphotoreceptor matrix (IPM) during light and dark cycles. The RPE is selectivity permeable to sodium. Open and short circuit transport studies with RPE indicate a circulating (choroid to retina and back) Na current which does not compromise the electrical integrity of the blood brain barrier but together with the Na permeselectivity is of sufficient magnitude to buffer both upwards and downwards movements of IPM [Na] during light or dark responses.     

Inhibition of glucose transport in human erythrocytes by 2,3-dioxoindole (Isatin)

10 mM isatin (2,3-dioxoindole) inhibited glucose influx into human erythrocytes by over 30%. The inhibition is of the competitive type, where the affinity constant (K_t) was increased from 5.71 (control) to 11.11 mM in the presence of isatin with no change in V_max (130 nmol/min/ml packed cells). The observed inhibition of sugar transport by isatin was not mediated through membrane–SH groups accessible to iodoacetate, iodoacetamide, DTNB, DNP or sodium arsenite. Isatin inhibited sugar transport in the presence of 2 mM harmaline, an alkaloid inhibitor of Na⁺, K⁺–ATP_ase activity. The inhibition was non additive which suggests that these two compounds interact with the same or a similar site on the erythrocyte membrane.     

Calcium/calmodulin-dependent protein kinase II increases glutamate and noradrenaline release from synaptosomes

A variety of evidence indicates that calcium-dependent protein phosphorylation modulates the release of neurotransmitter from nerve terminals. For instance, the injection of rat calcium/calmodulin-dependent protein kinase II (Ca2+/CaM-dependent PK II) into the preterminal digit of the squid giant synapse leads to an increase in the release of a so-far unidentified neurotransmitter induced by presynaptic depolarization. But until now, it has not been demonstrated that Ca2+/CaM-dependent PK II can also regulate neurotransmitter release in the vertebrate nervous system. Here we report that the introduction of Ca2+/CaM-dependent PK II, autoactivated by thiophosphorylation, into rat brain synaptosomes (isolated nerve terminals) increases the initial rate of induced release of two neurotransmitters, glutamate and noradrenaline. We also show that introduction of a selective peptidergic inhibitor of Ca2+/CaM-dependent PK II inhibits the initial rate of induced glutamate release. These results support the hypothesis that activation of Ca2+/CaM-dependent PK II in the nerve terminal removes a constraint on neurotransmitter release.     

A binding site for the T-cell co-receptor CD8 on the alpha 3 domain of HLA-A2

Adhesion measurements between CD8 and 48 point mutants of HLA-A2.1 show that the CD8 alpha-chain binds to the alpha 3 domain of HLA-A2.1. Three clusters of alpha 3 residues contribute to the binding, with an exposed, negatively charged loop (residues 223-229) playing a dominant role. CD8 binding correlates with cytotoxic T-cell recognition and sensitivity to inhibition by anti-CD8 antibodies. Impaired alloreactive T-cell recognition of an HLA-A2.1 mutant with reduced affinity for CD8 is not restored by functional CD8 binding sites on an antigenically irrelevant class I molecule. Therefore, complexes of CD8 and the T-cell receptor bound to the same class I major histocompatibility complex molecule seem to be necessary for T-cell activation.