LEADER 03654 am 22008173u 450 001 9910139006903321 005 20200903223051.0 010 $a90-04-25572-9 024 7 $a10.1163/9789004255722 035 $a(CKB)2550000001117967 035 $a(EBL)1400630 035 $a(OCoLC)858861444 035 $a(SSID)ssj0001001472 035 $a(PQKBManifestationID)11975449 035 $a(PQKBTitleCode)TC0001001472 035 $a(PQKBWorkID)10966277 035 $a(PQKB)10606215 035 $a(OCoLC)853452480 035 $a(nllekb)BRILL9789004255722 035 $a(Au-PeEL)EBL1400630 035 $a(CaPaEBR)ebr10764666 035 $a(CaONFJC)MIL518313 035 $a(ScCtBLL)fdda6fff-694b-495b-bab8-1cc4fe614048 035 $a(MiAaPQ)EBC1400630 035 $a(oapen)https://directory.doabooks.org/handle/20.500.12854/38164 035 $a(PPN)177950137 035 $a(EXLCZ)992550000001117967 100 $a20130719d2013 uy| 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 10$aAging gracefully in the Renaissance $estories of later life from Petrarch to Montaigne /$fby Cynthia Skenazi 210 $aLeiden - Boston$cBrill$d2013 210 1$aLeiden [The Netherlands] :$cBrill,$d2013. 215 $a1 online resource (192 p.) 225 1 $aMedieval and Renaissance authors and texts,$x0925-7683 ;$vvolume 11 300 $aDescription based upon print version of record. 311 $a90-04-25466-8 311 $a1-299-87062-7 320 $aIncludes bibliographical references and index. 327 $aPreliminary Material -- Introduction -- 1 A Sound Mind in a Healthy Body -- 2 The Circulation of Power and Knowledge -- 3 Love in Old Age -- 4 Then and Now -- Bibliography -- Index. 330 $aIn Aging Gracefully in the Renaissance: Stories of Later Life from Petrarch to Montaigne Cynthia Skenazi explores a shift in attitudes towards aging and provides a historical perspective on a crucial problem of our time. From the late fourteenth to the end of the sixteenth centuries, the elderly subject became a point of new social, medical, political, and literary attention on both sides of the Alps. A movement of secularization tended to dissociate old age from the Christian preparation for death, re-orienting the concept of aging around pragmatic matters such as health care, intergenerational relationships, and accrued insights one might wish to pass along. Such changes were accompanied by an increasing number of personal accounts of later life. Listed by Choice magazine as one of the Outstanding Academic Titles of 2014 This title is available online in its entirety in Open Access 410 0$aMedieval and Renaissance authors and texts ;$vv. 11. 606 $aEuropean literature$yRenaissance, 1450-1600$xHistory and criticism 606 $aAging in literature 606 $aAging$zEurope$xHistory 606 $aOlder people$zEurope$xHistory 610 $aLiterature 610 $aHistory 610 $aAging 610 $aErasmus 610 $aGalen 610 $aMichel de Montaigne 610 $aMichel Foucault 610 $aPetrarch 610 $aPierre de Ronsard 615 0$aEuropean literature$xHistory and criticism. 615 0$aAging in literature. 615 0$aAging$xHistory. 615 0$aOlder people$xHistory. 676 $a809/.031 700 $aSkenazi$b Cynthia$0469361 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910139006903321 996 $aAging gracefully in the Renaissance$92052500 997 $aUNINA LEADER 03586nam 2200457z- 450 001 9910261133303321 005 20210211 035 $a(CKB)4100000002484753 035 $a(oapen)https://directory.doabooks.org/handle/20.500.12854/56238 035 $a(oapen)doab56238 035 $a(EXLCZ)994100000002484753 100 $a20202102d2017 |y 0 101 0 $aeng 135 $aurmn|---annan 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 00$aThe Physiological Functions of the Amyloid Precursor Protein Gene Family 210 $cFrontiers Media SA$d2017 215 $a1 online resource (275 p.) 225 1 $aFrontiers Research Topics 311 08$a2-88945-355-3 330 $aThe amyloid precursor protein APP plays a key role in the pathogenesis of Alzheimer's disease (AD), as proteolytical cleavage of APP gives rise to the Aß peptide which is deposited in the brains of Alzheimer patients. Despite this, our knowledge of the normal cell biological and physiological functions of APP and the closely related APLPs is limited. This may have hampered our understanding of AD, since evidence has accumulated that not only the production of the Aß peptide but also the loss of APP-mediated functions may contribute to AD pathogenesis. Thus, it appears timely and highly relevant to elucidate the functions of the APP gene family from the molecular level to their role in the intact organism, i.e. in the context of nervous system development, synapse formation and adult synapse function, as well as neural homeostasis and aging. Why is our understanding of the APP functions so limited? APP and the APLPs are multifunctional proteins that undergo complex proteolytical processing. They give rise to an almost bewildering array of different fragments that may each subserve specific functions. While Aß is aggregation prone and neurotoxic, the large secreted ectodomain APPsa - produced in the non-amyloidogenic a-secretase pathway - has been shown to be neurotrophic, neuroprotective and relevant for synaptic plasticity, learning and memory. Recently, novel APP cleavage pathways and enzymes have been discovered that have gained much attention not only with respect to AD but also regarding their role in normal brain physiology. In addition to the various cleavage products, there is also solid evidence that APP family proteins mediate important functions as transmembrane cell surface molecules, most notably in synaptic adhesion and cell surface signaling. Elucidating in more detail the molecular mechanisms underlying these divers functions thus calls for an interdisciplinary approach ranging from the structural level to the analysis in model organisms. Thus, in this research topic of Frontiers we compile reviews and original studies, covering our current knowledge of the physiological functions of this intriguing and medically important protein family. 606 $aNeurosciences$2bicssc 610 $aAlzheimers disease 610 $aAmyloid precursor protein 610 $aAmyloid precursor-like protein 610 $aanimal model 610 $alearning and memory 610 $aneuroprotection 610 $aspines 610 $asynaptic adhesion 610 $asynaptic plasticity 610 $asynaptogenesis 615 7$aNeurosciences 700 $aUlrike C. Muller$4auth$01324757 702 $aThomas Deller$4auth 906 $aBOOK 912 $a9910261133303321 996 $aThe Physiological Functions of the Amyloid Precursor Protein Gene Family$93036259 997 $aUNINA