亨尼斯多夫市政厅，亨尼斯多夫，德国

这个市政厅起到了连接的作用。它将历史上线性城市边缘的一个小公园和铁路另一边已经发展形成的新城市中心连接起来。这栋新建筑的高度，介于沿主路的农舍和其附近的5层居住建筑之间。柔和的几何形体和首层视觉的渗透性，使它很轻易就融入到新公园的流动空间当中。     

Engineering Microneedle Patches for Improved Penetration:Analysis,Skin Models and Factors Affecting Needle Insertion

Transdermal microneedle(MN)patches are a promising tool used to transport a wide variety of active compounds into the skin.To serve as a substitute for common h...     

Progress for on-line acoustic emission monitoring of cracks in reactor systems

This paper reviews accomplishments and planned tasks for the NRC-sponsored research program concerned with “Acoustic Emission/Flaw Relationships for Inservice Monitoring of Nuclear Reactor Pressure Boundaries”. The objective of the acoustic emission (AE) monitoring program is to develop and validate the use of AE methods for continuous surveillance of reactor pressure boundaries to detect flaw growth. Topics discussed include testing AE monitoring on reactors, refinement of an AE signal identification relationship, study of slow crack growth rate effects on AE generation, and activity to produce an ASTM standard for AE monitoring and to gain ASME code acceptance of AE monitoring.     

Peptides Derived from Vascular Endothelial Growth Factor B Show Potent Binding to Neuropilin-1

Vascular endothelial growth factors (VEGFs) regulate significant pathways in angiogenesis, myocardial and neuronal protection, metabolism, and cancer progression. The VEGF-B growth factor is involved in cell survival, anti-apoptotic and antioxidant mechanisms, through binding to VEGF receptor 1 and neuropilin-1 (NRP1). We employed surface plasmon resonance technology and X-ray crystallography to analyse the molecular basis of the interaction between VEGF-B and the b1 domain of NRP1, and developed VEGF-B C-terminus derived peptides to be used as chemical tools for studying VEGF-B - NRP1 related pathways. Peptide lipidation was used as a means to stabilise the peptides. VEGF-B-derived peptides containing a C-terminal arginine show potent binding to NRP1-b1. Peptide lipidation increased binding residence time and improved plasma stability. A crystal structure of a peptide with NRP1 demonstrated that VEGF-B peptides bind at the canonical C-terminal arginine binding site. VEGF-B C-terminus imparts higher affinity for NRP1 than the corresponding VEGF-A₁₆₅ region. This tight binding may impact on the activity and selectivity of the full-length protein. The VEGF-B₁₆₇ derived peptides were more effective than VEGF-A₁₆₅ peptides in blocking functional phosphorylation events. Blockers of VEGF-B function have potential applications in diabetes and non-alcoholic fatty liver disease.