В свободном доступе выложены статьи Нобелевского лауреата по медицине 2016 г. (от Wiley)
The Nobel Prize in Physiology or Medicine for 2016 has been awarded to Yoshinori Ohsumi, a cell biologist, for his discoveries on mechanisms for autophagy. Autophagy has been known for over 50 years but its fundamental importance in physiology and medicine was only recognized after Yoshinori Ohsumi's paradigm-shifting research in the 1990's. Professor Ohsumi is currently based at the Tokyo Institute of Technology.
Crystallization and preliminary X-ray analysis of LC3-I
Acta Crystallographica Section D
Crystallization and preliminary X-ray analysis of Atg3
Acta Crystallographica Section F
Crystallization of Saccharomyces cerevisiae aminopeptidase 1, the major cargo protein of the Cvt pathway
Acta Crystallographica Section F
Crystallization of Saccharomyces cerevisiaeα-mannosidase, a cargo protein of the Cvt pathway
Acta Crystallographica Section F
Expression, purification and crystallization of the Atg5–Atg16 complex essential for autophagy
Acta Crystallographica Section F
Crystallization and preliminary X-ray analysis of Atg10
Acta Crystallographica Section F
Crystallization and preliminary crystallographic analysis of human Atg4B–LC3 complex
Acta Crystallographica Section F
Two newly identified sites in the ubiquitin-like protein Atg8 are essential for autophagy
EMBO Reports
Beclin–phosphatidylinositol 3-kinase complex functions at the trans-Golgi network
EMBO Reports
Structure of the Atg12–Atg5 conjugate reveals a platform for stimulating Atg8–PE conjugation
EMBO Reports
Current knowledge of the pre-autophagosomal structure (PAS)
FEBS Letters
The amino-terminal region of Atg3 is essential for association with phosphatidylethanolamine in Atg8 lipidation
FEBS Letters
Atg8-family interacting motif crucial for selective autophagy
FEBS Letters
Mouse Apg10 as an Apg12-conjugating enzyme: analysis by the conjugation-mediated Yeast two-hybrid method
FEBS Letters
Autophagosome formation can be achieved in the absence of Atg18 by expressing engineered PAS-targeted Atg2
FEBS Letters
Hrr25 phosphorylates the autophagic receptor Atg34 to promote vacuolar transport of α-mannosidase under nitrogen starvation conditions
FEBS Letters
Localization of Atg3 to autophagy-related membranes and its enhancement by the Atg8-family interacting motif to promote expansion of the membranes
FEBS Letters
Molecular machinery of autophagosome formation in Yeast, Saccharomyces cerevisiae
FEBS Letters
Functional molecular masses of vacuolar membrane H+-ATPase from Saccharomyces cerevisiae as studied by radiation inactivation analysis
FEBS Letters
Dimeric structure of H+-translocating pyrophosphatase from pumpkin vacuolar membranes
FEBS Letters
Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae
FEBS Letters
Atg17 recruits Atg9 to organize the pre-autophagosomal structure
Genes to Cells
Structural basis of target recognition by Atg8/LC3 during selective autophagy
Genes to Cells
Hierarchy of Atg proteins in pre-autophagosomal structure organization
Genes to Cells
Transport of phosphatidylinositol 3-phosphate into the vacuole via autophagic membranes in Saccharomyces cerevisiae
Genes to Cells
The crystal structure of microtubule-associated protein light chain 3, a mammalian homologue of Saccharomyces cerevisiae Atg8
Genes to Cells
Novel families of vacuolar amino acid transporters
IUBMB Life
Protein turnover
IUBMB Life
Serial section reconstruction using a computer graphics system: Applications to intracellular structures in Yeast cells and to the periodontal structure of dogs' teeth
Microscopy Research and Technique
Crystallization of the Atg12–Atg5 conjugate bound to Atg16 by the free-interface diffusion method
Journal of Synchrotron Radiation
Phospholipid methylation controls Atg32-mediated mitophagy and Atg8 recycling
The EMBO Journal
LC3/ a mammalian homolog of Yeast Apg8p, is localized in autophagosome membranes after processing
The EMBO Journal
Bulk RNA degradation by nitrogen starvation-induced autophagy in Yeast
The EMBO Journal
LC3, a mammalian homologue of Yeast Apg8p, is localized in autophagosome membranes after processing
The EMBO Journal
The pre-autophagosomal structure organized by concerted functions of APG genes is essential for autophagosome formation
The EMBO Journal
Apg10p, a novel protein-conjugating enzyme essential for autophagy in Yeast
The EMBO Journal
The structure of Atg4B–LC3 complex reveals the mechanism of LC3 processing and delipidation during autophagy
The EMBO Journal
Apg16p is required for the function of the Apg12p–Apg5p conjugate in the Yeast autophagy pathway
The EMBO Journal
Starvation Triggers the Delivery of the Endoplasmic Reticulum to the Vacuole via Autophagy in Yeast
TRAFFIC
Interrelationships among Atg proteins during autophagy in Saccharomyces cerevisiae
Yeast
Saccharomyces cerevisiae mata mutant cells defective in pointed projection formation in response to α-factor at high concentrations
Yeast
Источник: http://eu.wiley.com/WileyCDA/Section/id-323991.html#physio-tab
