Zobrazeno 1 - 10
of 37
pro vyhledávání: '"Nobuo Ida"'
Autor:
Reiji Nishio, Akihito Yasuda, Noriyasu Kamei, Mariko Takeda-Morishita, Nobuo Ida, Shuichi Yamamoto, Yoshiaki Terasawa, Kozo Takayama, Shingo Kikuchi
Publikováno v:
Journal of Pharmaceutical Sciences. 102:469-479
Our recent work has shown that the intestinal absorption of insulin can be improved significantly by coadministration of cell-penetrating peptides (CPPs), especially penetratin. However, a relatively high dose of penetratin is required to adequately
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::711a037c335d12af061fa30e6401875c
https://doi.org/10.1002/jps.23364
https://doi.org/10.1002/jps.23364
Publikováno v:
Journal of Controlled Release. 143:302-310
Penetratin, a 16-residue peptide, is used widely as a highly efficient delivery carrier for a wide range of poorly permeable therapeutic cargoes. The crucial structural features of penetratin remain unclear, as demonstrated by the difficulties encoun
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::093614d8029f91074096b7c1bae2abe7
https://doi.org/10.1016/j.jconrel.2010.01.019
https://doi.org/10.1016/j.jconrel.2010.01.019
Publikováno v:
International Journal of Infectious Diseases. 7(1):21-28
Objective: A new superantigen-adsorbing device (SAAD) was developed, and its characteristics and efficacy in septic animals were evaluated. Methods: The SAAD was prepared by stepwise chemical modification of a polystyrene-based composite fiber reinfo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59a219dde7bd28bfcdf840b9b89c82bc
Publikováno v:
Journal of Neurochemistry. 72:1457-1465
Amyloidogenic processing of the beta-amyloid precursor protein (APP) has been implicated in the pathology of Alzheimer's disease. Because it has been suggested that catabolic processing of the APP holoprotein occurs in acidic intracellular compartmen
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2af29202e15d3dc6cb91d134174250ba
https://doi.org/10.1046/j.1471-4159.1999.721457.x
https://doi.org/10.1046/j.1471-4159.1999.721457.x
Autor:
Sascha Weggen, Christian Haass, Konrad Beyreuther, Jürgen Grünberg, Nobuo Ida, Anke Diehlmann, Colin L. Masters, Thomas A. Bayer
Publikováno v:
Journal of Neuroscience Research. 56:405-419
Because distinct mutations in presenilin 1 and presenilin 2 are a major cause of early-onset familial Alzheimer's disease, we generated four monoclonal antibodies for the identification, localization, and investigation of presenilins in various cell
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eca176791d6434239249fe3a22f3317a
https://doi.org/10.1002/(sici)1097-4547(19990515)56:4<405::aid-jnr8>3.0.co
https://doi.org/10.1002/(sici)1097-4547(19990515)56:4<405::aid-jnr8>3.0.co
Autor:
Mari Blomberg, Nobuo Ida, Benita Engvall, Johannes Schröder, Malene Jensen, Tobias Hartmann, Konrad Beyreuther, Egon Werle, Lars Lannfelt, Johannes Pantel, M. Jauss, Lars-Olof Wahlund, Hans Basun
Publikováno v:
Annals of Neurology. 45:504-511
All mutations known to cause familial Alzheimer's disease (AD) act by increasing the levels of soluble beta-amyloid peptide (A beta), especially the longer form, A beta42. However, in vivo elevation of soluble A beta in sporadic AD has so far not bee
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f73b20c222ad6fd4d741fc92c7ce9d3a
https://doi.org/10.1002/1531-8249(199904)45:4<504::aid-ana12>3.0.co
https://doi.org/10.1002/1531-8249(199904)45:4<504::aid-ana12>3.0.co
Autor:
Nobuo Ida, Stefan Wiemann, K. G. Anthony, S. Rondot, Konrad Beyreuther, Frank Breitling, Laura S. Frost, Melvyn Little, Stefan Dübel
Publikováno v:
Journal of Molecular Biology. 279:589-603
In order to develop a system which allows infection by an epitope-specific phage-antibody via an F-pilus expressing that epitope, a study on the expression of foreign sequences on F-pilin was undertaken. Initially, a plasmid library was constructed w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d997dee35c7a435e1c3ad34fa0a979db
https://doi.org/10.1006/jmbi.1998.1773
https://doi.org/10.1006/jmbi.1998.1773
Autor:
David L. Charest, Peter B. Reiner, Nobuo Ida, Fred C. Lam, Julia Mills, Steven L. Pelech, Konrad Beyreuther
Publikováno v:
The Journal of Neuroscience. 17:9415-9422
Catabolic processing of the amyloid precursor protein (APP) is subject to regulatory control by protein kinases. We hypothesized that this regulation involves sequential activation of the enzymes mitogen-activated protein kinase kinase (MEK) and extr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed3e62c980ce73762a52f87c72b4e96d
https://doi.org/10.1523/jneurosci.17-24-09415.1997
https://doi.org/10.1523/jneurosci.17-24-09415.1997
Autor:
Gareth W. Roberts, Tobias Hartmann, Nobuo Ida, Konrad Beyreuther, David Allsop, Sophie Bieger, Colin L. Masters, Pentti J. Tienari, Carlos G. Dotti, Babara Brühl, Klaus Unsicker
Publikováno v:
Nature Medicine. 3:1016-1020
The Alzheimer amyloid precursor protein (APP) is cleaved by several proteases, the most studied, but still unidentified ones, are those involved in the release of a fragment of APP, the amyloidogenic beta-protein A beta. Proteolysis by gamma-secretas
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec32b3a2012a4ae38cd8d23ad9452397
https://doi.org/10.1038/nm0997-1016
https://doi.org/10.1038/nm0997-1016
Autor:
Konrad Beyreuther, Elina Ikonen, Mikael Simons, Andreas Weidemann, Nobuo Ida, Gerd Multhaup, Colin L. Masters, Carlos G. Dotti, Pentti J. Tienari
Publikováno v:
Proceedings of the National Academy of Sciences. 94:4125-4130
Cerebral plaques containing β-amyloid (βA4) represent an invariant pathological feature of Alzheimer disease (AD). βA4 is proteolytically generated from its parent molecule, amyloid precursor protein (APP). In nonneuronal cells βA4 has been shown
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::115c66b25566bfd0c66579a0fc071cfe
https://doi.org/10.1073/pnas.94.8.4125
https://doi.org/10.1073/pnas.94.8.4125