| 词条 | Andrea Musacchio |
| 释义 |
| name = Andrea Musacchio | image = AndreaMusacchio.png | image_size = | alt = | caption = |birth_name=Andrea Musacchio | birth_date = {{Birth date and age|1964|07|11}} | birth_place = Rome, Italy | death_date = | death_place = | nationality = Italian | fields = Crystallography | workplaces = Harvard Medical School, European Institute of Oncology, Max Planck Institute for Molecular Physiology | alma_mater = University of Rome Tor Vergata, European Molecular Biology Laboratory | doctoral_advisor = Matti Saraste | academic_advisors = Gianni Cesareni | doctoral_students = | notable_students = | awards = }}Andrea Musacchio (born July 11, 1964) [1] is an Italian structural biologist. He is Max Planck director at the Institute of Molecular Physiology in Dortmund. He is also Honorary Professor at the Center for Medical Biotechnology at the University of Duisburg-Essen. He was named European Molecular Biology Organization member in 2009.[2] Education and careerMusacchio received a Laurea in Biology from the University of Rome Tor Vergata summa cum laude in 1990, and earned his Ph.D., summa cum laude, from the Heidelberg University in 1995 working at the European Molecular Biology Laboratory. For his postdoctoral studies he joined Stephen C. Harrison laboratory at the Harvard Medical School in Boston. In 1999 he returned to Italy to found his laboratory at the European Institute of Oncology in Milan, where he started working on mechanisms of cell division. He was a European Molecular Biology Organization Young Investigator from 2000-2004. Musacchio moved to Dortmund in 2011 to direct the Department of Mechanistic Cell Biology at the Max Planck Institute for Molecular Physiology[3] ResearchMusacchio approached structural biology during his Ph.D., contributing to the determination of the first crystallographic structures of the SH3 [4] and PH [5] domains. During his post-doctoral training, he was involved in the determination of the clathrin triskelion structure,[6] one of the first studies combining X-ray crystallography and electron microscopy. As an independent scientist, his interests focused on the understanding of the molecular basis of mitosis, with emphasis on the spindle assembly checkpoint. Since the early days, Musacchio's lab adopted a multi-disciplinary approach merging structural biology, biochemistry and cellular biology, this way gaining comprehensive views on protein functions in living cells.[7] He is best known for his work on Mad1/Mad2 complexes,[8][9] which led to the formulation of the template model,[10] and for his contributions to the understanding of the role of the kinase Aurora B, Mps1 and Haspin in mitosis.[11][12][13][14] In 2008, the structure of the Ndc80 complex [15] set the foundation of a new line of his investigations on kinetochore assembly and attachment to microtubules[16][17][18] Personal lifeMusacchio spent his childhood in Rome, where he grew to be a strong supporter of A.S. Roma. He has started embracing Borussia Dortmund. He is married to Roberta Palumbo, and is father of two boys, Edoardo and Tommaso. References1. ^http://www.mpg.de/1040358/molekulare_physiologie_musacchio 2. ^2009 EMBO Press Release 3. ^{{cite journal | author=Musacchio A. | title=Andrea Musacchio | journal=Current Biology | volume=22 | issue=14 | pages=R552-R554 | year=2012 | pmid=23012739 | doi=10.1016/j.cub.2012.06.024}} 4. ^{{cite journal|last1=Musacchio|first1=A|last2=Noble|first2=M|last3=Pauptit|first3=R|last4=Wierenga|first4=R|last5=Saraste|first5=M|title=Crystal structure of a Src-homology 3 (SH3) domain.|journal=Nature|date=Oct 29, 1992|volume=359|issue=6398|pages=851–5|pmid=1279434|doi=10.1038/359851a0}} 5. ^{{cite journal|last1=Macias|first1=MJ|last2=Musacchio|first2=A|last3=Ponstingl|first3=H|last4=Nilges|first4=M|last5=Saraste|first5=M|last6=Oschkinat|first6=H|title=Structure of the pleckstrin homology domain from beta-spectrin.|journal=Nature|date=Jun 23, 1994|volume=369|issue=6482|pages=675–7|pmid=8208297|doi=10.1038/369675a0}} 6. ^{{cite journal|last1=Musacchio|first1=A|last2=Smith|first2=CJ|last3=Roseman|first3=AM|last4=Harrison|first4=SC|last5=Kirchhausen|first5=T|last6=Pearse|first6=BM|title=Functional Organization of Clathrin in Coats: Combining Electron Cryomicroscopy and X-Ray Crystallography|journal=Molecular Cell|date=Jun 1999|volume=3|issue=6|pages=761–70|pmid=10394364|doi=10.1016/S1097-2765(01)80008-3}} 7. ^{{cite journal|last1=Nasmyth|first1=K|title=How do so few control so many?|journal=Cell|date=Mar 25, 2005|volume=120|issue=6|pages=739–46|pmid=15797376|doi=10.1016/j.cell.2005.03.006}} 8. ^{{cite journal|last1=Sironi|first1=L|last2=Mapelli|first2=M|last3=Knapp|first3=S|last4=De Antoni|first4=A|last5=Jeang|first5=KT|last6=Musacchio|first6=A|title=Crystal structure of the tetrameric Mad1-Mad2 core complex: implications of a 'safety belt' binding mechanism for the spindle checkpoint.|journal=The EMBO Journal|date=May 15, 2002|volume=21|issue=10|pages=2496–506|pmid=12006501|doi=10.1093/emboj/21.10.2496|pmc=126000}} 9. ^{{cite journal|last1=Mapelli|first1=M|last2=Massimiliano|first2=L|last3=Santaguida|first3=S|last4=Musacchio|first4=A|title=The Mad2 conformational dimer: structure and implications for the spindle assembly checkpoint.|journal=Cell|date=Nov 16, 2007|volume=131|issue=4|pages=730–43|pmid=18022367|doi=10.1016/j.cell.2007.08.049}} 10. ^{{cite journal|last1=De Antoni|first1=A|last2=Pearson|first2=CG|last3=Cimini|first3=D|last4=Canman|first4=JC|last5=Sala|first5=V|last6=Nezi|first6=L|last7=Mapelli|first7=M|last8=Sironi|first8=L|last9=Faretta|first9=M|last10=Salmon|first10=ED|last11=Musacchio|first11=A|title=The Mad1/Mad2 complex as a template for Mad2 activation in the spindle assembly checkpoint.|journal=Current Biology|date=Feb 8, 2005|volume=15|issue=3|pages=214–25|pmid=15694304|doi=10.1016/j.cub.2005.01.038}} 11. ^{{cite journal|last1=De Antoni|first1=A|last2=Maffini|first2=S|last3=Knapp|first3=S|last4=Musacchio|first4=A|last5=Santaguida|first5=S|title=A small-molecule inhibitor of Haspin alters the kinetochore functions of Aurora B.|journal=The Journal of Cell Biology|date=Oct 15, 2012|volume=199|issue=2|pages=269–84|pmid=23071153|doi=10.1083/jcb.201205119|pmc=3471222|url=http://dspace.mit.edu/bitstream/1721.1/77635/1/Antoni-2012-A%20small-molecule%20inh.pdf}} 12. ^{{cite journal|last1=Santaguida|first1=S|last2=Vernieri|first2=C|last3=Villa|first3=F|last4=Ciliberto|first4=A|last5=Musacchio|first5=A|title=Evidence that Aurora B is implicated in spindle checkpoint signalling independently of error correction.|journal=The EMBO Journal|date=Apr 20, 2011|volume=30|issue=8|pages=1508–19|pmid=21407176|doi=10.1038/emboj.2011.70|pmc=3102279}} 13. ^{{cite journal|last1=Santaguida|first1=S|last2=Tighe|first2=A|last3=D'Alise|first3=AM|last4=Taylor|first4=SS|last5=Musacchio|first5=A|title=Dissecting the role of MPS1 in chromosome biorientation and the spindle checkpoint through the small molecule inhibitor reversine.|journal=The Journal of Cell Biology|date=Jul 12, 2010|volume=190|issue=1|pages=73–87|pmid=20624901|doi=10.1083/jcb.201001036|pmc=2911657}} 14. ^{{cite journal|last1=Sessa|first1=F|last2=Mapelli|first2=M|last3=Ciferri|first3=C|last4=Tarricone|first4=C|last5=Areces|first5=LB|last6=Schneider|first6=TR|last7=Stukenberg|first7=PT|last8=Musacchio|first8=A|title=Mechanism of Aurora B activation by INCENP and inhibition by hesperadin.|journal=Molecular Cell|date=Apr 29, 2005|volume=18|issue=3|pages=379–91|pmid=15866179|doi=10.1016/j.molcel.2005.03.031}} 15. ^{{cite journal|last1=Ciferri|first1=C|last2=Pasqualato|first2=S|last3=Screpanti|first3=E|last4=Varetti|first4=G|last5=Santaguida|first5=S|last6=Dos Reis|first6=G|last7=Maiolica|first7=A|last8=Polka|first8=J|last9=De Luca|first9=JG|last10=De Wulf|first10=P|last11=Salek|first11=M|last12=Rappsilber|first12=J|last13=Moores|first13=CA|last14=Salmon|first14=ED|last15=Musacchio|first15=A|title=Implications for kinetochore-microtubule attachment from the structure of an engineered Ndc80 complex.|journal=Cell|date=May 2, 2008|volume=133|issue=3|pages=427–39|pmid=18455984|doi=10.1016/j.cell.2008.03.020|pmc=4754795}} 16. ^{{cite journal|last1=Santaguida|first1=S|last2=Musacchio|first2=A|title=The life and miracles of kinetochores.|journal=The EMBO Journal|date=Sep 2, 2009|volume=28|issue=17|pages=2511–31|pmid=19629042|doi=10.1038/emboj.2009.173|pmc=2722247}} 17. ^{{cite journal|last1=Petrovic|first1=A|last2=Mosalaganti|first2=S|last3=Keller|first3=J|last4=Mattiuzzo|first4=M|last5=Overlack|first5=K|last6=Krenn|first6=V|last7=De Antoni|first7=A|last8=Wohlgemuth|first8=S|last9=Cecatiello|first9=V|last10=Pasqualato|first10=S|last11=Raunser|first11=S|last12=Musacchio|first12=A|title=Modular assembly of RWD domains on the Mis12 complex underlies outer kinetochore organization.|journal=Molecular Cell|date=Feb 20, 2014|volume=53|issue=4|pages=591–605|pmid=24530301|doi=10.1016/j.molcel.2014.01.019}} 18. ^{{cite journal|last1=Basilico|first1=F|last2=Maffini|first2=S|last3=Weir|first3=JR|last4=Prumbaum|first4=D|last5=Rojas|first5=AM|last6=Zimniak|first6=T|last7=De Antoni|first7=A|last8=Jeganethan|first8=S|last9=Voss|first9=B|last10=van Gerwen|first10=S|last11=Krenn|first11=V|last12=Massimiliano|first12=L|last13=Valencia|first13=A|last14=Vetter|first14=IR|last15=Herzog|first15=F|last16=Raunser|first16=S|last17=Pasqualato|first17=S|last18=Musacchio|first18=A|title=The pseudo GTPase CENP-M drives human kinetochore assembly.|journal=eLife|date=Jul 8, 2014|volume=3|issue=|pages=e02978|pmid=25006165|doi=10.7554/elife.02978|pmc=4080450}} External links
6 : Italian biologists|1964 births|Living people|People from Rome|Heidelberg University alumni|Members of the European Molecular Biology Organization |
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