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- Lundholm, Thomas, et al.
(författare)
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NEW TECHNIQUES APPLIED TO ADAPTIVE CONTROLLED MACHINING
- 1992
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Ingår i: Robotics and Computer-Integrated Manufacturing. - 0736-5845 .- 1879-2537. ; 9:4-5, s. 383-389
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Tidskriftsartikel (refereegranskat)abstract
- The future capital intensive CIM and FMS systems will demand adaptive controlled (AC) machine tools. At the Department of Production Engineering of the Royal Institute of Technology in Stockholm (IMT/KTH) we are continuing the development of an advanced AC turning center. Our approach is to design and use sophisticated sensor systems to measure several features both on-line and off-line in order to obtain sufficient information on the cutting process and make adaptive feedback feasible. The AC system operates at three different levels: advanced process monitoring adaptive control constraint (ACC) adaptive control optimization (ACO). In this paper we give an overview of practical progress and improvements that have been achieved since our contribution to MSTF '87 in Cambridge.1 This includes: a new flexible sensor installation for optical tool wear measurements on-line tool wear estimation based upon a dynamic force sensor applied time series analysis for on-line chatter control real-time control of maching conditions with respect to cutting forces distributed real-time computer system solution.
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- Welsh, Michael, et al.
(författare)
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Stimulation through the T cell receptor leads to interactions between SHB and several signaling proteins
- 1998
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Ingår i: Oncogene. - 0950-9232 .- 1476-5594. ; 16:7, s. 891-901
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Tidskriftsartikel (refereegranskat)abstract
- Shb is a recently described Src homology 2 (SH2) domain-containing adaptor protein. Here we show that Shb is expressed in lymphoid tissues, and is recruited into signaling complexes upon activation of Jurkat T cells. Grb2 binds proline-rich motifs in Shb via its SH3 domains. As a result, a number of proteins detected in anti-Shb and anti-Grb2 immunoprecipitates are shared, including phosphoproteins of 22, 36/38, 55/57 and 70 kDa. Shb-association with p22, which represents the T cell receptor associated chain, occurs through the Shb SH2 domain. The central region of Shb binds p36/38. Since this interaction was inhibited by phosphotyrosine, this region of Shb is likely to contain a non-SH2 PTB (phosphotyrosine binding) domain. The Shb PTB domain was found to preferentially bind the sequence Asp-Asp-X-pTyr when incubated with a phosphopeptide library. A peptide corresponding to a phosphorylation site in 34 kDa Lnk inhibited association between Shb and p36/38. Overexpression of Shb in Jurkat cells led to increased basal phosphorylation of Shb-associated p36/38 and p70 proteins. Inactivation of the Shb SH2 domain by an R522K mutation resulted in a reduced stimulation of tyrosine phosphorylation of several proteins in response to CD3 crosslinking when expressed in Jurkat cells. Together, our results show three distinct domains of Shb all participate in the formulation of multimeric signaling complexes in activated T cells. These results indicate that the Shb protein functions in T cell receptor signaling.
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