Academia Sinica

About: Academia Sinica is a facility organization based out in Taipei, Taiwan. It is known for research contribution in the topics: Population & Gene. The organization has 52086 authors who have published 65998 publications receiving 1728114 citations. The organization is also known as: Central Research Academy.

Genome-wide association analysis identifies three new breast cancer susceptibility loci

Abstract: Breast cancer is the most common cancer among women. To date, 22 common breast cancer susceptibility loci have been identified accounting for ∼8% of the heritability of the disease. We attempted to replicate 72 promising associations from two independent genome-wide association studies (GWAS) in ∼70,000 cases and ∼68,000 controls from 41 case-control studies and 9 breast cancer GWAS. We identified three new breast cancer risk loci at 12p11 (rs10771399; P = 2.7 × 10(-35)), 12q24 (rs1292011; P = 4.3 × 10(-19)) and 21q21 (rs2823093; P = 1.1 × 10(-12)). rs10771399 was associated with similar relative risks for both estrogen receptor (ER)-negative and ER-positive breast cancer, whereas the other two loci were associated only with ER-positive disease. Two of the loci lie in regions that contain strong plausible candidate genes: PTHLH (12p11) has a crucial role in mammary gland development and the establishment of bone metastasis in breast cancer, and NRIP1 (21q21) encodes an ER cofactor and has a role in the regulation of breast cancer cell growth.

Targeting the carbohydrates on HIV-1: Interaction of oligomannose dendrons with human monoclonal antibody 2G12 and DC-SIGN.

Abstract: It is widely accepted that the heavily glycosylated glycoprotein gp120 on the surface of HIV-1 shields peptide epitopes from recognition by the immune system and may promote infection in vivo by interaction with dendritic cells and transport to tissue rich in CD4(+) T cells such as lymph nodes A conserved cluster of oligomannose glycans on gp120 has been identified as the epitope recognized by the broadly HIV-1-neutralizing monoclonal antibody 2G12 Oligomannose glycans are also the ligands for DC-SIGN, a C-type lectin found on the surface of dendritic cells Multivalency is fundamental for carbohydrate-protein interactions, and mimicking of the high glycan density on the virus surface has become essential for designing carbohydrate-based HIV vaccines and antiviral agents We report an efficient synthesis of oligomannose dendrons, which display multivalent oligomannoses in high density, and characterize their interaction with 2G12 and DC-SIGN by a glycan microarray binding assay The solution and the surface binding analysis of 2G12 to a prototype oligomannose dendron clearly demonstrated the efficacy of dendrimeric display We further showed that these glycodendrons inhibit the binding of gp120 to 2G12 and recombinant dimeric DC-SIGN with IC(50) in the nanomolar range A second-generation Man(9) dendron was identified as a potential immunogen for HIV vaccine development and as a potential antiviral agent

Selective binding of mannose-encapsulated gold nanoparticles to type 1 pili in Escherichia coli.

Abstract: The synthesis, characterization and biological application of mannose encapsulated gold nanoparticles (m-AuNP) are reported. m-AuNP is well dispersed and very stable without aggregation in the media of broad ion strength and pH ranges. The selective binding of m-AuNP to the mannose adhesin FimH of bacterial type 1 pili is demonstrated using transmission electron microscopy. The competition assay with free mannose suggests that m-AuNP binds FimH better than free mannose does. This work demonstrates that carbohydrate attached nanoparticles can be used as an efficient affinity label and a multi-ligand carrier in a biological system.

Graphene/MoS2 Heterostructures for Ultrasensitive Detection of DNA Hybridisation

Abstract: The photoluminescence signals of a graphene/MoS2 heterostructural stacking film are sensitive to environmental charges, which allows the single-base sequence-selective detection of DNA hybridization with sensitivity to the level of aM.