O-GlcNAcylation is the addition of β-N-acetylglucosamine(O-GlcNAc) to serine or threonine residues of nuclear and cytoplasmic proteins. It is highly abundant on myriad proteins, and cycles on proteins with a timescale similar to protein phosphorylation, and has surprisingly extensive cross talk with phosphorylation, where is serves as a nutrient/stress sensor to modulate signaling, transcription, and cytoskeletal functions. Abnormal amounts of O-GlcNAcylation underlie the etiology of insulin resistance and glucose toxicity in diabetes, and this type of modification plays a direct role in neurodegenerative disease. Many oncogenic proteins and tumor suppressor proteins are also regulated by O-GlcNAcylation. Mitochondrial membrane ATP synthase(F1F0 ATP synthase complex) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. Subunits α and β form the catalytic core in F
저자
Ryum Joo-hwan [ Glycobiology Laboratory, Yonsei University, Seoul, Korea ]
Cho Jin-won [ Glycobiology Laboratory, Yonsei University, Seoul, Korea ]
본 학회는 화학, 생화학, 분자생물학, 미생물학, 식품공학, 의학, 약학, 유전공학 및 생물공학, 환경 및 기타 공업 등 전 분야의 탄수화물관련 이론과 기술을 연구 발전시키고 산학협동을 통해 이를 보급하여 국내 관련 산업의 발전 및 국민생활의 과학화에 기여하고자 하며, 이러한 목표와 비젼의 실현을 위해 회원들이 적극적인 참여와 활동을 전개하고자 한다.