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Dortmund, Germany

The Max Planck Institute for Molecular Physiology is located in Dortmund, Germany next to the Dortmund University of Technology. It is one of 80 institutes in the Max Planck Society .The institute is divided into five departments: Emeritus Department I Structural Biology Sometimes the tiniest of factors can determine health or disease – an important insight that Alfred Wittinghofer and his team have seen confirmed time and again during their work as researchers. And no wonder, for their main research interest is a group of proteins which are among the key regulating molecules in living organisms. Department II Systemic Cell Biology When scientists finished mapping the human genome in 2001, they were in for quite a surprise: Instead of the 80,000 to 130,000 genes that were expected, Homo sapiens has only 20,000 to 30,000 – about the same number as a mouse and just barely more than a simple one-millimetre-long worm with hardly any brain at all. Emeritus Department III Physical Biochemistry In the cells of plants, animals and humans intense activity goes on around the clock. All of the time, millions of proteins are busy transporting materials in and out, burning energy-rich nutrients, building up new molecules and disposing of old ones, fending off pathogens, passing on signals and controlling the activity of genes. Department IV Chemical Biology The plan sounded impressive, and garnering plenty of new inexpensive drugs appeared a sure thing. With the advent of synthesis robots at the beginning of the 1990s, the pharma industry could produce thousands of different small molecules in almost no time, and a veritable boom in substance research seemed in the offing. With such an enormous number of new substances available, so it was hoped, many promising candidates for innovative drug development would be found. And soon thereafter, the first “substance libraries” with more than a million compounds were synthesised. Department V Mechanistic Cell Biology Our research interests focus on a stage of the eukaryotic cell cycle known as mitosis. During mitosis, the replicated chromosomes in a mother cell undergo equational division to create two daughter cells with a full complement of the genetic material. From a molecular perspective, mitosis is an astoundingly complex process.Human physiology is a central field of medical research, and seeks to elucidate and explain the fundamental principles that describe the ways in which cells, tissues, organs, organ systems and biological information networks operate and function together in a living organism. Most fundamental principles of human physiology are relevant for warm-blooded animals of mammalia, though not necessarily for cold-blooded reptiles. Wikipedia.

Grabenbauer M.,Max Planck Institute of Molecular Physiology
Methods in Cell Biology | Year: 2012

The correlation of light and electron microscopy (EM) is a powerful tool as it combines the investigation of dynamic processes in vivo with the resolution power of the electron microscope. The green fluorescent proteins (GFPs) and its derivatives revolutionized live-cell light microscopy. Hence, this review outlines correlative microscopy of GFP through photo-oxidation, a method that allows for the direct ultrastructural visualization of fluorophores upon illumination. Oxygen radicals generated during the GFP bleaching process photo-oxidize diaminobenzidine (DAB) into an electron dense precipitate that can be visualized both by routine EM of thin sections and by electron tomography for 3D analysis. There are different levels of correlative microscopy, i.e. the correlation of certain areas, cells, or organelles from light to EM, where photo-oxidation of DAB through GFP allows the highest possible degree--the correlation of specific molecules. © 2012 Elsevier Inc. Source

Ott M.,University of California at San Francisco | Geyer M.,Max Planck Institute of Molecular Physiology | Zhou Q.,University of California at Berkeley
Cell Host and Microbe | Year: 2011

Thirteen years ago, human cyclin T1 was identified as part of the positive transcription elongation factor b (P-TEFb) and the long-sought host cofactor for the HIV-1 transactivator Tat. Recent years have brought new insights into the intricate regulation of P-TEFb function and its relationship with Tat, revealing novel mechanisms for controlling HIV transcription and fueling new efforts to overcome the barrier of transcriptional latency in eradicating HIV. Moreover, the improved understanding of HIV and Tat forms a basis for studying transcription elongation control in general. Here, we review advances in HIV transcription research with a focus on the growing family of cellular P-TEFb complexes, structural insights into the interactions between Tat, P-TEFb, and TAR RNA, and the multifaceted regulation of these interactions by posttranscriptional modifications of Tat. © 2011 Elsevier Inc. Source

Musacchio A.,Italian National Cancer Institute | Musacchio A.,Max Planck Institute of Molecular Physiology
Philosophical Transactions of the Royal Society B: Biological Sciences | Year: 2011

The spindle assembly checkpoint controls cell cycle progression during mitosis, synchronizing it with the attachment of chromosomes to spindle microtubules. After the discovery of the mitotic arrest deficient (MAD) and budding uninhibited by benzymidazole (BUB) genes as crucial checkpoint components in 1991, the second decade of checkpoint studies (2001-2010) witnessed crucial advances in the elucidation of the mechanism through which the checkpoint effector, the mitotic checkpoint complex, targets the anaphase-promoting complex (APC/C) to prevent progression into anaphase. Concomitantly, the discovery that the Ndc80 complex and other components of the microtubule-binding interface of kinetochores are essential for the checkpoint response finally asserted that kinetochores are crucial for the checkpoint response. Nevertheless, the relationship between kinetochores and checkpoint control remains poorly understood. Crucial advances in this area in the third decade of checkpoint studies (2011-2020) are likely to be brought about by the characterization of the mechanism of kinetochore recruitment, activation and inactivation of checkpoint proteins, which remains elusive for the majority of checkpoint components. Here, we take a molecular view on the main challenges hampering this task. © 2011 The Royal Society. Source

DeLuca J.G.,Colorado State University | Musacchio A.,Max Planck Institute of Molecular Physiology | Musacchio A.,Italian National Cancer Institute
Current Opinion in Cell Biology | Year: 2012

Successful mitosis depends on the stable, yet regulated attachment of chromosomes to spindle microtubules. The kinetochore, a large macromolecular structure assembled at sites of centromeric heterochromatin, is responsible for generating and regulating these essential attachments. Over the last several years, concerted experimental efforts have brought the structural view of the kinetochore-microtubule interface more clearly into focus. Here, we review important recent advancements and discuss several unresolved questions regarding how kinetochores dynamically bridge mitotic chromosomes to spindle microtubules. © 2011 Elsevier Ltd. Source

Johnson K.A.,Speedway | Goody R.S.,Max Planck Institute of Molecular Physiology
Biochemistry | Year: 2011

Nearly 100 years ago Michaelis and Menten published their now classic paper [Michaelis, L., and Menten, M. L. (1913) Die Kinetik der Invertinwirkung. Biochem. Z. 49, 333-369] in which they showed that the rate of an enzyme-catalyzed reaction is proportional to the concentration of the enzyme-substrate complex predicted by the Michaelis-Menten equation. Because the original text was written in German yet is often quoted by English-speaking authors, we undertook a complete translation of the 1913 publication, which we provide as Supporting Information. Here we introduce the translation, describe the historical context of the work, and show a new analysis of the original data. In doing so, we uncovered several surprises that reveal an interesting glimpse into the early history of enzymology. In particular, our reanalysis of Michaelis and Mentens data using modern computational methods revealed an unanticipated rigor and precision in the original publication and uncovered a sophisticated, comprehensive analysis that has been overlooked in the century since their work was published. Michaelis and Menten not only analyzed initial velocity measurements but also fit their full time course data to the integrated form of the rate equations, including product inhibition, and derived a single global constant to represent all of their data. That constant was not the Michaelis constant, but rather V max/K m, the specificity constant times the enzyme concentration (k cat/K m ± E 0). © 2011 American Chemical Society. Source

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