Microcompartments within the yeast plasma membrane
-
Hans Merzendorfer
Hans Merzendorfer studied Biology from 1988 to 1993 at the University of Munich, where he earned his doctorate in 1999 working on insect v-type ATPases. From 1999 to 2001 Hans Merzendorfer continued his work as a Postdoc at the University of Osnabrück. In 2001 he became assistant professor, and in 2006 he obtained his “Habilitation” in animal physiology. In 2007 he received a Heisenberg fellowship from the German Research Foundation. From 2008 to 2009 he joined the Department of Biochemistry at the Kansas State University. Since 2009 Hans Merzendorfer works as an adjunct (apl.) professor at the University of Osnabrück.
and
Jürgen J. Heinisch
Jürgen Heinisch studied Biology at the University of Darmstadt and earned his PhD in 1985 working on yeast phosphofructokinase genetics. After a two-year postdoc (1986–1988) at the University of Alberta (Edmonton, Canada) he became a research assistant at the University of Düsseldorf and got his “Habilitation” in Microbiology in 1993. From 2000–2002 he held a professorship in Fermentation Technology at the University of Hohenheim and since 2003 is a full professor and head of the Department of Genetics at the University of Osnabrück.
©2013 by Walter de Gruyter Berlin Boston
Articles in the same Issue
- Masthead
- Masthead
- Guest Editorial
- Highlight: The physiology and dynamics of cellular microcompartments
- Highlight: The Physiology and Dynamics of Cellular Microcompartments
- Cellular microcompartments constitute general suborganellar functional units in cells
- Dynamics of bioenergetic microcompartments
- Microcompartments within the yeast plasma membrane
- Plant cell microcompartments: a redox-signaling perspective
- Microcompartments in the Drosophila heart and the mammalian brain: general features and common principles
- Minireviews
- Beyond anemia: hepcidin, monocytes and inflammation
- Melanoma resistance to photodynamic therapy: new insights
- The biosynthesis of caprazamycins and related liponucleoside antibiotics: new insights
- cCMP, cUMP, cTMP, cIMP and cXMP as possible second messengers: Development of a hypothesis based on studies with soluble guanylyl cyclase α1β1
- Research Articles/Short Communications
- Protein Structure and Function
- Degradation of channelopsin-2 in the absence of retinal and degradation resistance in certain mutants
- Cell Biology and Signaling
- Possible role of a septin, SEPT1, in spreading in squamous cell carcinoma DJM-1 cells
- Proteolysis
- ADAMTS: Novel proteases expressed by activated mast cells
- The proinflammatory cytokines interleukin-1α and tumor necrosis factor α promote the expression and secretion of proteolytically active cathepsin S from human chondrocytes
Articles in the same Issue
- Masthead
- Masthead
- Guest Editorial
- Highlight: The physiology and dynamics of cellular microcompartments
- Highlight: The Physiology and Dynamics of Cellular Microcompartments
- Cellular microcompartments constitute general suborganellar functional units in cells
- Dynamics of bioenergetic microcompartments
- Microcompartments within the yeast plasma membrane
- Plant cell microcompartments: a redox-signaling perspective
- Microcompartments in the Drosophila heart and the mammalian brain: general features and common principles
- Minireviews
- Beyond anemia: hepcidin, monocytes and inflammation
- Melanoma resistance to photodynamic therapy: new insights
- The biosynthesis of caprazamycins and related liponucleoside antibiotics: new insights
- cCMP, cUMP, cTMP, cIMP and cXMP as possible second messengers: Development of a hypothesis based on studies with soluble guanylyl cyclase α1β1
- Research Articles/Short Communications
- Protein Structure and Function
- Degradation of channelopsin-2 in the absence of retinal and degradation resistance in certain mutants
- Cell Biology and Signaling
- Possible role of a septin, SEPT1, in spreading in squamous cell carcinoma DJM-1 cells
- Proteolysis
- ADAMTS: Novel proteases expressed by activated mast cells
- The proinflammatory cytokines interleukin-1α and tumor necrosis factor α promote the expression and secretion of proteolytically active cathepsin S from human chondrocytes
