Go to:
Logótipo
Comuta visibilidade da coluna esquerda
Você está em: Start > Publications > View > Identification of all FK506-binding proteins from Neurospora crassa
Publication

Publications

Identification of all FK506-binding proteins from Neurospora crassa

Title
Identification of all FK506-binding proteins from Neurospora crassa
Type
Article in International Scientific Journal
Year
2008
Authors
pinto, d
(Author)
Other
The person does not belong to the institution. The person does not belong to the institution. The person does not belong to the institution. Without AUTHENTICUS Without ORCID
soares, s
(Author)
Other
The person does not belong to the institution. The person does not belong to the institution. The person does not belong to the institution. Without AUTHENTICUS Without ORCID
tropschug, m
(Author)
Other
The person does not belong to the institution. The person does not belong to the institution. The person does not belong to the institution. Without AUTHENTICUS Without ORCID
videira, a
(Author)
ICBAS
View Personal Page You do not have permissions to view the institutional email. Search for Participant Publications View Authenticus page View ORCID page
Journal
Vol. 45
Pages: 1600-1607
ISSN: 1087-1845
Publisher: Elsevier
Other information
Authenticus ID: P-003-TFM
Abstract (EN): Immunophilins are intracellular receptors of immunosuppressive drugs, carrying peptidyl-prolyl cis-trans isomerase activity, with a general role in protein folding but also involved in specific regulatory mechanisms. Four immunophilins of the FKBP-type (FK506-binding proteins) were identified in the genome of Neurospora crassa. Previously, FKBP22 has been located in the endoplasmic reticulum as part of chaperone/folding complexes and FKBP13 has been found to have a dual location in the cytoplasm and mitochondria. FKBP11 is apparently located exclusively in the cytoplasm. It is not expressed during vegetative development of the fungus although its expression can be induced with calcium and during sexual development. Overexpression of the respective gene appears to confer a growth advantage to the fungus in media containing some divalent ions. FKBP50 is a nuclear protein and its genetic inactivation leads to a temperature-sensitive phenotype. None of these proteins is, alone or in combination, essential for N. crassa, as demonstrated by the isolation of a mutant strain lacking all four FKBPs.
Language: English
Type (Professor's evaluation): Scientific
Contact: avideira@ibmc.up.pt
No. of pages: 8
Documents
We could not find any documents associated to the publication.
Related Publications

Of the same journal

Modulation of fungal sensitivity to staurosporine by targeting proteins identified by transcriptional profiling (2011)
Article in International Scientific Journal
fernandes, as; goncalves, ap; castro, a; lopes, ta; gardner, r; glass, nl; videira, a
Dual-specificity protein phosphatase Msg5 controls cell wall integrity and virulence in Fusarium oxysporum (2021)
Article in International Scientific Journal
Fernandes, TR; Sánchez Salvador, E; Tapia, ÁG; Di Pietro, A
Recommend this page Top
Copyright 1996-2025 © Faculdade de Direito da Universidade do Porto  I Terms and Conditions  I Acessibility  I Index A-Z
Page created on: 2025-07-25 at 09:06:19 | Privacy Policy | Personal Data Protection Policy | Whistleblowing