The structure-activity relationship of aryloxyacetylthioureas for the inhibition of radicle elongation.

Orobanchaceae root parasitic weeds cause significant damage to agriculture and become threats to global food security. Integrated pest management is a key concept in modern agriculture and requires chemicals with various modes of action. Planteose accumulates as a storage carbohydrate in the dry seeds of root parasitic weeds.

Morphology of insertion sites on patellar side of medial patellofemoral ligament.

Purpose: The purpose of this study was to clarify the insertion sites on the patellar side of the medial patellofemoral ligament (MPFL).

Methods: A total of 35 nonpaired human cadaveric knees were used in this study. After identification of the MPFL, the insertion sites on the patellar side of the MPFL were marked.

Subtoxic levels of hydrogen peroxide induce brain-derived neurotrophic factor expression to protect PC12 cells.

Background: Oxidative stress is one of the mechanisms underlying pathogenesis in neurodegenerative diseases such as Alzheimer's disease. Generally, oxidative stress represents cell toxicity; however, we recently found that oxidative stress promotes the expression of growth factor progranulin (PGRN) in HT22 murine hippocampus cells, thereby protecting the HT22 cells. In this study, we attempted to clarify whether a similar system exists in the other neuronal cell model, rat pheochromocytoma (PC12) cells.

Morphology of the femoral insertion site of the medial patellofemoral ligament.

Purpose: The purpose of this study was to identify the femoral insertion of the medial patellofemoral ligament (MPFL) and related osseous landmarks.

Methods: A total of 31 unpaired human cadaveric knees were studied. The MPFL was identified, and the site of its femoral insertion was marked.

Potential neuroprotective effects of SIRT1 induced by glucose deprivation in PC12 cells.

Nutrient availability is one of the most important signals regulating cellular fates including cell growth, differentiation, and death. Recent evidence suggests that the NAD(+)-dependent histone deacetylase sirtuin 1 (SIRT1) plays a prominent role in linking changes in nutritional availability with cellular fate regulation. SIRT1 expression is observed in neurons, yet the expressional and functional regulation of this protein is not fully understood.