Literature DB >> 146356

The quaternary structure of yeast aminopeptidase I. 2. Geometric arrangement of subunits.

R Marx, G Metz, K H Röhn.   

Abstract

Electron micrographs of native aminopeptidase I and of isolated subfragments were taken after negative staining with uranyl formate. From these studies and from the chemical evidence summarized in the preceding paper it is concluded that the active enzyme is a dodecamer possessing pseudo-D3 symmetry with the dimer as the smallest symmetric unit.

Entities:  

Mesh:

Substances:

Year:  1977        PMID: 146356     DOI: 10.1515/znc-1977-11-1210

Source DB:  PubMed          Journal:  Z Naturforsch C Biosci        ISSN: 0341-0382


  3 in total

1.  Structure of yeast Ape1 and its role in autophagic vesicle formation.

Authors:  Ming-Yuan Su; Wen-Hsin Peng; Meng-Ru Ho; Shih-Chieh Su; Yuan-Chih Chang; Guang-Chao Chen; Chung-I Chang
Journal:  Autophagy       Date:  2015       Impact factor: 16.016

2.  Higher-order assemblies of oligomeric cargo receptor complexes form the membrane scaffold of the Cvt vesicle.

Authors:  Chiara Bertipaglia; Sarah Schneider; Arjen J Jakobi; Abul K Tarafder; Yury S Bykov; Andrea Picco; Wanda Kukulski; Jan Kosinski; Wim Jh Hagen; Arvind C Ravichandran; Matthias Wilmanns; Marko Kaksonen; John Ag Briggs; Carsten Sachse
Journal:  EMBO Rep       Date:  2016-06-06       Impact factor: 8.807

Review 3.  Recent Advances in Single-Particle Electron Microscopic Analysis of Autophagy Degradation Machinery.

Authors:  Yiu Wing Sunny Cheung; Sung-Eun Nam; Calvin K Yip
Journal:  Int J Mol Sci       Date:  2020-10-28       Impact factor: 5.923

  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.