Theo Wallimann (born 13 October 1946 in Alpnach, Obwalden, Switzerland) is a Swiss biologist who was research group leader and Adjunct-Professor at the Institute of Cell Biology ETH Zurich and later at the Institute of Molecular Health Science https://mhs.biol.ethz.ch/about-us/emeriti-formermembers/wallimann.html at the ETH Zurich [1] at the Biology Department https://biol.ethz.ch/en/, of the ETH Zurich, [2] Switzerland.
In 1975, Theo Wallimann completed his Ph.D. Dissertation on “M-line-bound Creatine Kinase and Myofibrillar Structure” [3] in the laboratory of Prof. Hans M. Eppenberger at the Institute of Cell Biology at ETH Zurich with distinction and received the ETH prize and medal. [4]
From 1975 - 1981, Wallimann worked as a post-doctoral research associate with Andrew G. Szent-Györgyi , [5] at the Biology Department of Brandeis University on the subject of "Myosin-linked calcium regulation of muscle contraction". [6] After rejoining the Biology Dept of the ETH-Zurich in 1981, Wallimann became a Lecturer in 1984 with his Habilitation on: "Localization and function of M-line-bound creatine kinase: M-band model and Phospho-Creatine Shuttle" [7] ). In 1994, Wallimann was awarded the title of Professor and in the next two years he became Head and Deputy Head of the Institute of Cell Biology. Wallimann resigned from his post in June 2008 and is now Emeritus and member of the ETH Alumni organisation. [8]
Wallimann was awarded with the Alfred-Vogt-Prize in 2005 [9] and received the Research.com Recognition Leader Award for Biology and Biochemistry in Switzerland in 2023 & 2024. [10]
Wallimann's main areas of interest are:
Phosphagens, also known as macroergic compounds, are high energy storage compounds, also known as high-energy phosphate compounds, chiefly found in muscular tissue in animals. They allow a high-energy phosphate pool to be maintained in a concentration range, which, if it all were adenosine triphosphate (ATP), would create problems due to the ATP-consuming reactions in these tissues. As muscle tissues can have sudden demands for much energy, these compounds can maintain a reserve of high-energy phosphates that can be used as needed, to provide the energy that could not be immediately supplied by glycolysis or oxidative phosphorylation. Phosphagens supply immediate but limited energy.
Creatine is an organic compound with the nominal formula (H2N)(HN)CN(CH3)CH2CO2H. It exists in various tautomers in solutions. Creatine is found in vertebrates where it facilitates recycling of adenosine triphosphate (ATP), primarily in muscle and brain tissue. Recycling is achieved by converting adenosine diphosphate (ADP) back to ATP via donation of phosphate groups. Creatine also acts as a buffer.
Phosphocreatine, also known as creatine phosphate (CP) or PCr (Pcr), is a phosphorylated form of creatine that serves as a rapidly mobilizable reserve of high-energy phosphates in skeletal muscle, myocardium and the brain to recycle adenosine triphosphate, the energy currency of the cell.
5' AMP-activated protein kinase or AMPK or 5' adenosine monophosphate-activated protein kinase is an enzyme that plays a role in cellular energy homeostasis, largely to activate glucose and fatty acid uptake and oxidation when cellular energy is low. It belongs to a highly conserved eukaryotic protein family and its orthologues are SNF1 in yeast, and SnRK1 in plants. It consists of three proteins (subunits) that together make a functional enzyme, conserved from yeast to humans. It is expressed in a number of tissues, including the liver, brain, and skeletal muscle. In response to binding AMP and ADP, the net effect of AMPK activation is stimulation of hepatic fatty acid oxidation, ketogenesis, stimulation of skeletal muscle fatty acid oxidation and glucose uptake, inhibition of cholesterol synthesis, lipogenesis, and triglyceride synthesis, inhibition of adipocyte lipogenesis, inhibition of adipocyte lipolysis, and modulation of insulin secretion by pancreatic β-cells.
Creatine kinase (CK), also known as creatine phosphokinase (CPK) or phosphocreatine kinase, is an enzyme expressed by various tissues and cell types. CK catalyses the conversion of creatine and uses adenosine triphosphate (ATP) to create phosphocreatine (PCr) and adenosine diphosphate (ADP). This CK enzyme reaction is reversible and thus ATP can be generated from PCr and ADP.
5'-AMP-activated protein kinase catalytic subunit alpha-2 is an enzyme that in humans is encoded by the PRKAA2 gene.
5'-AMP-activated protein kinase catalytic subunit alpha-1 is an enzyme that in humans is encoded by the PRKAA1 gene.
5'-AMP-activated protein kinase subunit beta-1 is an enzyme that in humans is encoded by the PRKAB1 gene.
5'-AMP-activated protein kinase subunit gamma-2 is an enzyme that in humans is encoded by the PRKAG2 gene.
A-kinase anchor protein 13 is a protein that in humans, is encoded by the AKAP13 gene. This protein is also called AKAP-Lbc because it encodes the lymphocyte blast crisis (Lbc) oncogene, and ARHGEF13/RhoGEF13 because it contains a guanine nucleotide exchange factor (GEF) domain for the RhoA small GTP-binding protein.
cAMP-dependent protein kinase catalytic subunit beta is an enzyme that in humans is encoded by the PRKACB gene.
Creatine kinase, mitochondrial 1B also known as CKMT1B is one of two genes which encode the ubiquitous mitochondrial creatine kinase.
Creatine kinase S-type, mitochondrial is an enzyme that in humans is encoded by the CKMT2 gene.
5'-AMP-activated protein kinase subunit beta-2 is an enzyme that in humans is encoded by the PRKAB2 gene.
Creatine kinase U-type, mitochondrial, also called ubiquitous mitochondrial creatine kinase (uMtCK), is in humans encoded by CKMT1A gene. CKMT1A catalyzes the reversible transfer of the γ-phosphate group of ATP to the guanidino group of Cr to yield ADP and PCr. The impairment of CKMT1A has been reported in ischaemia, cardiomyopathy, and neurodegenerative disorders. Overexpression of CKMT1A has been reported related with several tumors.
Creatine kinase, muscle also known as MCK is a creatine kinase that in humans is encoded by the MCK gene.
In molecular biology, the ATP:guanido phosphotransferase family is a family of structurally and functionally related enzymes, that reversibly catalyse the transfer of phosphate between ATP and various phosphagens. The enzymes belonging to this family include:
Christophe Dessimoz is a Swiss National Science Foundation (SNSF) Professor at the University of Lausanne, Associate Professor at University College London and a group leader at the Swiss Institute of Bioinformatics. He was awarded the Overton Prize in 2019 for his contributions to computational biology. Starting in April 2022, he will be joint executive director of the SIB Swiss Institute of Bioinformatics, along with Ron Appel.
Sabine Werner is a German biochemist and professor.
Paola Picotti is an Italian biochemist who is Professor for Molecular Systems Biology at ETH Zürich. She is Deputy Head of the Institute for Molecular Systems Biology. Her research investigates how the conformational changes of proteins impact molecular networks with cells. She received numerous awarded awards, among which the 2019 EMBO Gold Medal.
