Zobrazeno 1 - 10
of 21
pro vyhledávání: '"Ingrid G. Haas"'
Autor:
Paul Saftig, Marcus Frank, Ingrid G. Haas, Andreas Ludwig, Thorsten Maretzky, Karina Reiss, Marc Schulte
Publikováno v:
Journal of Biological Chemistry. 281:21735-21744
Gamma-protocadherins (Pcdh gamma) are type I transmembrane proteins, which are most notably expressed in the nervous system. They are enriched at synapses and involved in synapse formation, specification, and maintenance. In this study, we show that
Publikováno v:
Current Opinion in Cell Biology. 17:446-452
Cadherins have been known for a long time to be key elements in many important biological processes. In particular, the role of classical cadherins in mediating adhesion has been examined in great detail. Over recent years, the accumulation of experi
Publikováno v:
Journal of Biological Chemistry. 280:9313-9319
The recently described protocadherin gene clusters encode cadherin-related proteins, which are highly expressed in the vertebrate nervous system. Here, we report biochemical studies addressing proteolytic processing of gamma-protocadherins. These typ
Publikováno v:
Journal of Cell Science. 115:2443-2452
The lumenal endoplasmic reticulum (ER) protein BiP, among its other functions, is believed to serve as an ER stress sensor, triggering the so-called `unfolded protein response' or UPR. For this role, BiP levels are critical. Indeed, here we show that
Autor:
Cornelia R. Kaloff, Ingrid G. Haas
Publikováno v:
Immunity. 2:629-637
The first constant domain (C H 1) of immunoglobulin heavy (H) chains is essential for BiP-mediated retention of unassembled H chains in the endoplasmic reticulum (ER). Here, we demonstrated that both wild-type and a mutant γ chain lacking the CHI do
Autor:
Josep Chillarón, Ingrid G. Haas
Publikováno v:
Recercat. Dipósit de la Recerca de Catalunya
instname
Dipòsit Digital de la UB
Universidad de Barcelona
instname
Dipòsit Digital de la UB
Universidad de Barcelona
Unassembled immunoglobulin light chains expressed by the mouse plasmacytoma cell line NS1 (κNS1) are degraded in vivo with a half-life of 50–60 min in a way that closely resembles endoplasmic reticulum (ER)-associated degradation ( Knittler et al.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45ffae1fffa28a7cd3caed68f7037dc6
http://hdl.handle.net/2445/25203
http://hdl.handle.net/2445/25203
Autor:
Laurent Morawiec, Annette Haas-Assenbaum, Benoît Kanzler, Thomas Boehm, Elsa Huber, Ingrid G. Haas
Publikováno v:
Mechanisms of Development
We report that gene silencing via intracytoplasmic microinjections of morpholino-modified antisense oligonucleotides is an effective and reproducible method to study both maternal and zygotic gene functions during early and late stages of mouse preim
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77889de81402ad8819abe67208ecac4b
https://hdl.handle.net/11858/00-001M-0000-002B-94D7-0
https://hdl.handle.net/11858/00-001M-0000-002B-94D7-0
Publikováno v:
Biological chemistry. 381(12)
In order to study the role of N-glycans in the ER-associated degradation of unassembled immunoglobulin light (Ig L) chains, we introduced N-glycan acceptor sites into the variable domain of the murine Ig L chain kappaNS1, which is unfolded in unassem
Autor:
Johanna Dudek, Wolfgang Nastainczyk, Markus H. Skowronek, Richard Zimmermann, Jörg Volkmer, Jens Tyedmers, Christiane Bies, Nicole Heim, Monika Lerner, Ingrid G. Haas
Cotranslational protein transport into dog pancreas microsomes involves the Sec61p complex plus a luminal heat shock protein 70. Posttranslational protein transport into the yeast endoplasmic reticulum (ER) involves the so-called Sec complex in the m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5772821e06a4a5a80077016107174001
https://europepmc.org/articles/PMC16525/
https://europepmc.org/articles/PMC16525/
Publikováno v:
Biological chemistry. 380(9)
We identified a human cDNA sequence encoding a polypeptide of 760 amino acids that shares 53% homology and 25.6% identity with the yeast DnaJ-like endoplasmic reticulum (ER) translocon component Sec63p. Three epitope-specific antisera revealed a prot