Racial differences in the prevalence of diabetes but not diabetic retinopathy in a multi-ethnic asian population

10.1167/iovs.11-7698Investigative Ophthalmology and Visual Science52107586-7592IOVS

Impact of glaucoma severity and laterality on vision-specific functioning: The Singapore Malay Eye Study

10.1167/iovs.12-10258Investigative Ophthalmology and Visual Science5421169-1175IOVS

Modeling and Optimization of Substrate Resistance for RF-CMOS

A predictive, physically based substrate resistance model for CMOS transistors operating at radio frequencies (RF) is described. This analytical mod el is scalable with transistor size and layout geometry. Measurement results confirm that the model accurately predicts the effect of substrate resistance on the transistor output impedance up to 20 GHz, including gate and drain bias dependencies. Minimization of the substrate resistance can be achieved by using substrate tap rings with small spacer distances and short finger widths

How much eye care services do Asian populations need projection from the Singapore epidemiology of eye disease (SEED) study

10.1167/iovs.12-11393Investigative Ophthalmology and Visual Science5432171-2177IOVS

Impact of Cryotherapy on Sensory, Motor, and Autonomic Neuropathy in Breast Cancer Patients Receiving Paclitaxel: A Randomized, Controlled Trial

10.3389/fneur.2020.604688Frontiers in Neurology1160468

GS32, a Novel Golgi SNARE of 32 kDa, Interacts Preferentially with Syntaxin 6

Syntaxin 1, synaptobrevins or vesicle-associated membrane proteins, and the synaptosome-associated protein of 25 kDa (SNAP-25) are key molecules involved in the docking and fusion of synaptic vesicles with the presynaptic membrane. We report here the molecular, cell biological, and biochemical characterization of a 32-kDa protein homologous to both SNAP-25 (20% amino acid sequence identity) and the recently identified SNAP-23 (19% amino acid sequence identity). Northern blot analysis shows that the mRNA for this protein is widely expressed. Polyclonal antibodies against this protein detect a 32-kDa protein present in both cytosol and membrane fractions. The membrane-bound form of this protein is revealed to be primarily localized to the Golgi apparatus by indirect immunofluorescence microscopy, a finding that is further established by electron microscopy immunogold labeling showing that this protein is present in tubular-vesicular structures of the Golgi apparatus. Biochemical characterizations establish that this protein behaves like a SNAP receptor and is thus named Golgi SNARE of 32 kDa (GS32). GS32 in the Golgi extract is preferentially retained by the immobilized GST–syntaxin 6 fusion protein. The coimmunoprecipitation of syntaxin 6 but not syntaxin 5 or GS28 from the Golgi extract by antibodies against GS32 further sustains the preferential interaction of GS32 with Golgi syntaxin 6