Vakkasoglu相关文献与解析，生知库 | 链接生命科学的每一步

Ronald D Seidel, Zohra Merazga, Dharma Raj Thapa, Jonathan Soriano, Emily Spaulding, Ahmet S Vakkasoglu, Paige Ruthardt, Wynona Bautista, Steven N Quayle, Peter A Kiener, Simon Low, John F Ross, Saso Cemerski, Anish Suri, Steven C Almo, Rodolfo J Chaparro

免疫

T细胞

发表日期：2021

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D-helix influences dimerization of the ATP-binding cassette (ABC) transporter associated with antigen processing 1 (TAP1) nucleotide-binding domain

D螺旋影响与抗原加工相关的ATP结合盒（ABC）转运蛋白1（TAP1）核苷酸结合域的二聚化

期刊:PLoS One

影响因子:2.6

doi:10.1371/journal.pone.0178238

Vakkasoglu, Ahmet S; Srikant, Sriram; Gaudet, Rachelle

发表日期：2017

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Structure changes upon deprotonation of the proton release group in the bacteriorhodopsin photocycle

细菌视紫红质光循环中质子释放基团去质子化后的结构变化

期刊:Biophysical Journal

影响因子:3.1

doi:10.1016/j.bpj.2012.06.022

Morgan, Joel E; Vakkasoglu, Ahmet S; Lanyi, Janos K; Lugtenburg, Johan; Gennis, Robert B; Maeda, Akio

微生物学

发表日期：2012

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Properties of Arg481 mutants of the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides suggest that neither R481 nor the nearby D-propionate of heme a3 is likely to be the proton loading site of the proton pump

来自球形红细菌（Rhodobacter sphaeroides）的aa3型细胞色素c氧化酶Arg481突变体的特性表明，R481及其附近的血红素a3的D-丙酸酯都不太可能是质子泵的质子加载位点。

期刊:Biochemistry

影响因子:3

doi:10.1021/bi901015d

Lee, Hyun Ju; Ojemyr, Linda; Vakkasoglu, Ahmet; Brzezinski, Peter; Gennis, Robert B

Water structural changes in the L and M photocycle intermediates of bacteriorhodopsin as revealed by time-resolved step-scan Fourier transform infrared (FTIR) spectroscopy

利用时间分辨步进扫描傅里叶变换红外光谱（FTIR）揭示细菌视紫红质L和M光循环中间体的水结构变化

期刊:Biochemistry

影响因子:3

doi:10.1021/bi0616596

Morgan, Joel E; Vakkasoglu, Ahmet S; Gennis, Robert B; Maeda, Akio

微生物学

发表日期：2007

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Peptide-HLA-based immunotherapeutics platforms for direct modulation of antigen-specific T cells

基于肽-HLA的免疫治疗平台，用于直接调节抗原特异性T细胞

D-helix influences dimerization of the ATP-binding cassette (ABC) transporter associated with antigen processing 1 (TAP1) nucleotide-binding domain

D螺旋影响与抗原加工相关的ATP结合盒（ABC）转运蛋白1（TAP1）核苷酸结合域的二聚化

Structure changes upon deprotonation of the proton release group in the bacteriorhodopsin photocycle

细菌视紫红质光循环中质子释放基团去质子化后的结构变化

Properties of Arg481 mutants of the aa3-type cytochrome c oxidase from Rhodobacter sphaeroides suggest that neither R481 nor the nearby D-propionate of heme a3 is likely to be the proton loading site of the proton pump

来自球形红细菌（Rhodobacter sphaeroides）的aa3型细胞色素c氧化酶Arg481突变体的特性表明，R481及其附近的血红素a3的D-丙酸酯都不太可能是质子泵的质子加载位点。

Water structural changes in the L and M photocycle intermediates of bacteriorhodopsin as revealed by time-resolved step-scan Fourier transform infrared (FTIR) spectroscopy

利用时间分辨步进扫描傅里叶变换红外光谱（FTIR）揭示细菌视紫红质L和M光循环中间体的水结构变化