U
Ulrike Lorenz
Researcher at University of Virginia
Publications - 36
Citations - 3730
Ulrike Lorenz is an academic researcher from University of Virginia. The author has contributed to research in topics: Protein tyrosine phosphatase & Signal transduction. The author has an hindex of 22, co-authored 33 publications receiving 3388 citations. Previous affiliations of Ulrike Lorenz include Harvard University & Max Planck Society.
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Journal ArticleDOI
Specific recruitment of sh-ptp1 to the erythropoietin receptor causes inactivation of jak2 and termination of proliferative signals
Ursula Klingmüller,Ursula Klingmüller,Ulrike Lorenz,Lewis C. Cantley,Benjamin G. Neel,Harvey F. Lodish +5 more
TL;DR: The results suggest that activation of SH-PTP1 by binding to the EPO-R plays a major role in terminating proliferative signals.
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Engulfment of apoptotic cells: signals for a good meal
TL;DR: Several new factors that regulate engulfment have been identified, whereas the roles of some of the older players require revision.
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SHP-1 and SHP-2 in T cells: two phosphatases functioning at many levels.
TL;DR: The roles of the two cytoplasmic PTPs, the Src‐homology 2 domain (SH2)‐containing SHP‐1 andSHP‐2, in T‐cell signaling, development, differentiation, and function are focused on.
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Metabolites released from apoptotic cells act as tissue messengers
Christopher B. Medina,Parul Mehrotra,Sanja Arandjelovic,Justin S. A. Perry,Yizhan Guo,Sho Morioka,Brady J. Barron,Scott F. Walk,Bart Ghesquière,Alexander S. Krupnick,Ulrike Lorenz,Kodi S. Ravichandran +11 more
TL;DR: Functionally, the apoptotic metabolite secretome induced specific gene programs in healthy neighbouring cells, including suppression of inflammation, cell proliferation, and wound healing, and a cocktail of apoptotic metabolites reduced disease severity in mouse models of inflammatory arthritis and lung transplant rejection.
Journal ArticleDOI
Intramolecular regulation of protein tyrosine phosphatase SH-PTP1: a new function for Src homology 2 domains
Dehua Pei,Ulrike Lorenz,Ulrike Lorenz,Ursula Klingmüller,Benjamin G. Neel,Benjamin G. Neel,Christopher T. Walsh,Christopher T. Walsh +7 more
TL;DR: Data suggest that the SH2 domains of SH-PTP1 serve to autoinhibit the phosphatase activity of the PTPase domain, and a model is proposed in which theSH2 domains interact with the P TPase domain in a pY-independent fashion and drive the PTTase domain into an inactive conformation.