LEADER 03244nam 22005415 450 001 9910253894803321 005 20250609112123.0 010 $a1-4939-3649-2 024 7 $a10.1007/978-1-4939-3649-6 035 $a(CKB)3710000000777361 035 $a(DE-He213)978-1-4939-3649-6 035 $a(MiAaPQ)EBC4626041 035 $a(PPN)194802205 035 $a(MiAaPQ)EBC6241654 035 $a(EXLCZ)993710000000777361 100 $a20160805d2016 u| 0 101 0 $aeng 135 $aurnn|008mamaa 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 10$aProtein Tyrosine Phosphatases in Cancer /$fedited by Benjamin G. Neel, Nicholas K. Tonks 205 $a1st ed. 2016. 210 1$aNew York, NY :$cSpringer New York :$cImprint: Springer,$d2016. 215 $a1 online resource (VIII, 360 p. 28 illus., 19 illus. in color.) 311 08$a1-4939-3647-6 320 $aIncludes bibliographical references at the end of each chapters and index. 327 $a1 Introduction to the PTP Superfamily -- 2 Receptor PTPs in Cancer -- 3 Non-Receptor PTPs in Cancer -- 4 HP2 -- 5 C-PTP -- 6 PTP1B -- 7 PTP-PEST -- 8 Dual Specificity Phosphatases in Cancer -- 9 Phosphatase-dependent roles for PTEN in Cancer -- 10 Phosphatase-independent roles for PTEN in Cancer -- 11 PRL family members in Cancer -- 12 Cdc25 family -- 13 PTPs, metabolism and cancer -- 14 PTPs, metabolism and cancer -- 15 Current status of PTP-based therapeutics -- 16 Summary and Perspective. . 330 $aThis book aims to bridge the gap in understanding how protein-tyrosine phosphatases (PTPs), which carry out the reverse reaction of tyrosine phosphorylation, feature in cancer cell biology. The expertly authored chapters will first review the general features of the PTP superfamily, including their overall structure and enzymological properties; use selected examples of individual PTP superfamily members, to illustrate emerging data on the role of PTPs in cancer; and will review the current status of PTP-based drug development efforts. Protein Tyrosine Phosphatases in Cancer,from renowned researchers Benjamin Neel and Nicholas Tonks, is invaluable reading for researchers in oncology, stem cell signaling,and biochemistry. . 606 $aCancer$xResearch 606 $aCytology 606 $aPost-translational modification 606 $aCancer Research$3https://scigraph.springernature.com/ontologies/product-market-codes/B11001 606 $aCell Biology$3https://scigraph.springernature.com/ontologies/product-market-codes/L16008 606 $aPosttranslational Modification$3https://scigraph.springernature.com/ontologies/product-market-codes/L14090 615 0$aCancer$xResearch. 615 0$aCytology. 615 0$aPost-translational modification. 615 14$aCancer Research. 615 24$aCell Biology. 615 24$aPosttranslational Modification. 676 $a614.5999 702 $aNeel$b Benjamin G$4edt$4http://id.loc.gov/vocabulary/relators/edt 702 $aTonks$b Nicholas K$4edt$4http://id.loc.gov/vocabulary/relators/edt 906 $aBOOK 912 $a9910253894803321 996 $aProtein Tyrosine Phosphatases in Cancer$92541167 997 $aUNINA