LIVIVO - Search results -

Search results

Result 1 - 10 of total 10

Search options

Article ; Online: Fetal and neonatal alloimmune thrombocytopenia: Current pathophysiological insights and perspectives for future diagnostics and treatment.

Stam, Wendy / Wachholz, Gabriela Elis / de Pereda, Jose Maria / Kapur, Rick / van der Schoot, Ellen / Margadant, Coert

2022 Volume 59, Page(s) 101038

Abstract: FNAIT is a pregnancy-associated condition caused by maternal alloantibodies against paternally-inherited platelet antigens, most frequently HPA-1a on integrin β3. The clinical effects range from no symptoms to fatal intracranial hemorrhage, but ... ...

Abstract	FNAIT is a pregnancy-associated condition caused by maternal alloantibodies against paternally-inherited platelet antigens, most frequently HPA-1a on integrin β3. The clinical effects range from no symptoms to fatal intracranial hemorrhage, but underlying pathophysiological determinants are poorly understood. Accumulating evidence suggests that differential antibody-Fc-glycosylation, activation of complement/effector cells, and integrin function-blocking effects contribute to clinical outcome. Furthermore, some antibodies preferentially bind platelet integrin αIIbβ3, but others bind αvβ3 on endothelial cells and trophoblasts. Defects in endothelial cells and angiogenesis may therefore contribute to severe anti-HPA-1a associated FNAIT. Moreover, anti-HPA-1a antibodies may cause placental damage, leading to intrauterine growth restriction. We discuss current insights into diversity and actions of HPA-1a antibodies, gathered from clinical studies, in vitro studies, and mouse models. Assessment of all factors determining severity and progression of anti-HPA-1a-associated FNAIT may importantly improve risk stratification and potentially reveal novel treatment strategies, both for FNAIT and other immunohematological disorders.
MeSH term(s)	Animals ; Mice ; Pregnancy ; Female ; Humans ; Thrombocytopenia, Neonatal Alloimmune/diagnosis ; Thrombocytopenia, Neonatal Alloimmune/etiology ; Thrombocytopenia, Neonatal Alloimmune/therapy ; Placenta/metabolism ; Endothelial Cells ; Blood Platelets/metabolism ; Isoantibodies
Chemical Substances	Isoantibodies
Language	English
Publishing date	2022-12-22
Publishing country	England
Document type	Journal Article ; Review ; Research Support, Non-U.S. Gov't
ZDB-ID	639015-8
ISSN	1532-1681 ; 0268-960X
ISSN (online)	1532-1681
ISSN	0268-960X
DOI	10.1016/j.blre.2022.101038
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 2207: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: A mutation in p62 protein (p. R321C), associated to Paget's disease of bone, causes a blockade of autophagy and an activation of NF-kB pathway.

Usategui-Martín, Ricardo / Gestoso-Uzal, Nerea / Calero-Paniagua, Ismael / De Pereda, José María / Del Pino-Montes, Javier / González-Sarmiento, Rogelio

Bone

2020 Volume 133, Page(s) 115265

Abstract: Paget's disease of bone (PDB) is a bone disorder characterized by an increase in bone turnover in a disorganized way with a large increase in bone resorption followed by bone formation. The most important known genetic factor predisposing to PDB is ... ...

Abstract	Paget's disease of bone (PDB) is a bone disorder characterized by an increase in bone turnover in a disorganized way with a large increase in bone resorption followed by bone formation. The most important known genetic factor predisposing to PDB is mutation in Sequestosome1 (SQSTM1) gene. We have studied the prevalence of SQSTM1 mutations and examined genotype-phenotype correlations in a Spanish cohort of PDB patients. Also, we have characterized three PDB patients that carry the c.961C>T SQSTM1 gene mutation that it is localized in exon 6 of SQSTM1 gene and it causes the p. R321C mutation. This mutation has been reported in patients with amyotrophic lateral sclerosis and frontotemporal dementia but in our knowledge this is the first time that p62 p. R321C mutation is associated to PDB. We show that p62 p.R321C mutation could induce blockage of autophagy and cell proliferation through NF-kB pathway. These results reinforce the hypothesis of autophagy involvement in Paget's disease of bone.
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Autophagy/genetics ; Humans ; Mutation/genetics ; NF-kappa B/metabolism ; Osteitis Deformans/genetics ; RNA-Binding Proteins ; Sequestosome-1 Protein/genetics
Chemical Substances	Adaptor Proteins, Signal Transducing ; NF-kappa B ; P62 protein, human ; RNA-Binding Proteins ; Sequestosome-1 Protein
Language	English
Publishing date	2020-02-06
Publishing country	United States
Document type	Journal Article
ZDB-ID	632515-4
ISSN	1873-2763 ; 8756-3282
ISSN (online)	1873-2763
ISSN	8756-3282
DOI	10.1016/j.bone.2020.115265
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1571: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MO 332: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Increased riboflavin production by manipulation of inosine 5'-monophosphate dehydrogenase in Ashbya gossypii.

Buey, Rubén M / Ledesma-Amaro, Rodrigo / Balsera, Mónica / de Pereda, José María / Revuelta, José Luis

Applied microbiology and biotechnology

2015 Volume 99, Issue 22, Page(s) 9577–9589

Abstract: Guanine nucleotides are the precursors of essential biomolecules including nucleic acids and vitamins such as riboflavin. The enzyme inosine-5'-monophosphate dehydrogenase (IMPDH) catalyzes the ratelimiting step in the guanine nucleotide de novo ... ...

Abstract	Guanine nucleotides are the precursors of essential biomolecules including nucleic acids and vitamins such as riboflavin. The enzyme inosine-5'-monophosphate dehydrogenase (IMPDH) catalyzes the ratelimiting step in the guanine nucleotide de novo biosynthetic pathway and plays a key role in controlling the cellular nucleotide pools. Thus, IMPDH is an important metabolic bottleneck in the guanine nucleotide synthesis, susceptible of manipulation by means of metabolic engineering approaches. Herein, we report the functional and structural characterization of the IMPDH enzyme from the industrial fungus Ashbya gossypii. Our data show that the overexpression of the IMPDH gene increases the metabolic flux through the guanine pathway and ultimately enhances 40 % riboflavin production with respect to the wild type. Also, IMPDH disruption results in a 100-fold increase of inosine excretion to the culture media. Our results contribute to the developing metabolic engineering toolbox aiming at improving the production of metabolites with biotechnological interest in A. gossypii.
MeSH term(s)	Eremothecium/enzymology ; Eremothecium/genetics ; Eremothecium/metabolism ; Gene Expression ; IMP Dehydrogenase/genetics ; IMP Dehydrogenase/metabolism ; Metabolic Engineering ; Metabolic Flux Analysis ; Riboflavin/biosynthesis
Chemical Substances	IMP Dehydrogenase (EC 1.1.1.205) ; Riboflavin (TLM2976OFR)
Language	English
Publishing date	2015-11
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	392453-1
ISSN	1432-0614 ; 0171-1741 ; 0175-7598
ISSN (online)	1432-0614
ISSN	0171-1741 ; 0175-7598
DOI	10.1007/s00253-015-6710-2
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 2229: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (1.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾

Article ; Online: A nucleotide-controlled conformational switch modulates the activity of eukaryotic IMP dehydrogenases.

Buey, Rubén M / Fernández-Justel, David / Marcos-Alcalde, Íñigo / Winter, Graeme / Gómez-Puertas, Paulino / de Pereda, José María / Luis Revuelta, José

Scientific reports

2017 Volume 7, Issue 1, Page(s) 2648

Abstract: Inosine-5'-monophosphate dehydrogenase (IMPDH) is an essential enzyme for nucleotide metabolism and cell proliferation. Despite IMPDH is the target of drugs with antiviral, immunosuppressive and antitumor activities, its physiological mechanisms of ... ...

Abstract	Inosine-5'-monophosphate dehydrogenase (IMPDH) is an essential enzyme for nucleotide metabolism and cell proliferation. Despite IMPDH is the target of drugs with antiviral, immunosuppressive and antitumor activities, its physiological mechanisms of regulation remain largely unknown. Using the enzyme from the industrial fungus Ashbya gossypii, we demonstrate that the binding of adenine and guanine nucleotides to the canonical nucleotide binding sites of the regulatory Bateman domain induces different enzyme conformations with significantly distinct catalytic activities. Thereby, the comparison of their high-resolution structures defines the mechanistic and structural details of a nucleotide-controlled conformational switch that allosterically modulates the catalytic activity of eukaryotic IMPDHs. Remarkably, retinopathy-associated mutations lie within the mechanical hinges of the conformational change, highlighting its physiological relevance. Our results expand the mechanistic repertoire of Bateman domains and pave the road to new approaches targeting IMPDHs.
MeSH term(s)	Adenine Nucleotides/chemistry ; Adenine Nucleotides/metabolism ; Binding Sites ; Guanine Nucleotides/chemistry ; Guanine Nucleotides/metabolism ; IMP Dehydrogenase/chemistry ; IMP Dehydrogenase/metabolism ; Models, Molecular ; Molecular Conformation ; Saccharomycetales
Chemical Substances	Adenine Nucleotides ; Guanine Nucleotides ; IMP Dehydrogenase (EC 1.1.1.205)
Language	English
Publishing date	2017-06-01
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-017-02805-x
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article: Increased riboflavin production by manipulation of inosine 5′-monophosphate dehydrogenase in Ashbya gossypii

Buey, Rubén M. / Ledesma-Amaro, Rodrigo / Balsera, Mónica / de Pereda, José María / Revuelta, José Luis

Applied microbiology and biotechnology. 2015 Nov., v. 99, no. 22

2015

Abstract: Guanine nucleotides are the precursors of essential biomolecules including nucleic acids and vitamins such as riboflavin. The enzyme inosine-5′-monophosphate dehydrogenase (IMPDH) catalyzes the ratelimiting step in the guanine nucleotide de novo ... ...

Abstract	Guanine nucleotides are the precursors of essential biomolecules including nucleic acids and vitamins such as riboflavin. The enzyme inosine-5′-monophosphate dehydrogenase (IMPDH) catalyzes the ratelimiting step in the guanine nucleotide de novo biosynthetic pathway and plays a key role in controlling the cellular nucleotide pools. Thus, IMPDH is an important metabolic bottleneck in the guanine nucleotide synthesis, susceptible of manipulation by means of metabolic engineering approaches. Herein, we report the functional and structural characterization of the IMPDH enzyme from the industrial fungus Ashbya gossypii. Our data show that the overexpression of the IMPDH gene increases the metabolic flux through the guanine pathway and ultimately enhances 40 % riboflavin production with respect to the wild type. Also, IMPDH disruption results in a 100-fold increase of inosine excretion to the culture media. Our results contribute to the developing metabolic engineering toolbox aiming at improving the production of metabolites with biotechnological interest in A. gossypii.
Keywords	Eremothecium gossypii ; biochemical pathways ; culture media ; excretion ; fungi ; gene overexpression ; genes ; guanine ; guanine nucleotides ; metabolic engineering ; metabolites ; nucleic acids ; riboflavin
Language	English
Dates of publication	2015-11
Size	p. 9577-9589.
Publishing place	Springer Berlin Heidelberg
Document type	Article
ZDB-ID	392453-1
ISSN	1432-0614 ; 0171-1741 ; 0175-7598
ISSN (online)	1432-0614
ISSN	0171-1741 ; 0175-7598
DOI	10.1007/s00253-015-6710-2
Database	NAL-Catalogue (AGRICOLA)

In stock of ZB MED Bonn / Germany

Z 79/727: Show issues

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: C3G, through its GEF activity, induces megakaryocytic differentiation and proplatelet formation.

Ortiz-Rivero, Sara / Baquero, Cristina / Hernández-Cano, Luis / Roldán-Etcheverry, Juan José / Gutiérrez-Herrero, Sara / Fernández-Infante, Cristina / Martín-Granado, Víctor / Anguita, Eduardo / de Pereda, José María / Porras, Almudena / Guerrero, Carmen

Cell communication and signaling : CCS

2018 Volume 16, Issue 1, Page(s) 101

Abstract: Background: Megakaryopoiesis allows platelet formation, which is necessary for coagulation, also playing an important role in different pathologies. However, this process remains to be fully characterized. C3G, an activator of Rap1 GTPases, is involved ... ...

Abstract	Background: Megakaryopoiesis allows platelet formation, which is necessary for coagulation, also playing an important role in different pathologies. However, this process remains to be fully characterized. C3G, an activator of Rap1 GTPases, is involved in platelet activation and regulates several differentiation processes. Methods: We evaluated C3G function in megakaryopoiesis using transgenic mouse models where C3G and C3GΔCat (mutant lacking the GEF domain) transgenes are expressed exclusively in megakaryocytes and platelets. In addition, we used different clones of K562, HEL and DAMI cell lines with overexpression or silencing of C3G or GATA-1. Results: We found that C3G participates in the differentiation of immature hematopoietic cells to megakaryocytes. Accordingly, bone marrow cells from transgenic C3G, but not those from transgenic C3GΔCat mice, showed increased expression of the differentiation markers CD41 and CD61, upon thrombopoietin treatment. Furthermore, C3G overexpression increased the number of CD41 Conclusions: All these data indicate that C3G plays a significant role in different steps of megakaryopoiesis, acting through a mechanism dependent on its GEF activity.
MeSH term(s)	Adipogenesis ; Blood Platelets/cytology ; Cell Differentiation ; Cell Line, Tumor ; Guanine Nucleotide-Releasing Factor 2/metabolism ; Humans ; Megakaryocytes/cytology ; Megakaryocytes/metabolism ; Ploidies
Chemical Substances	Guanine Nucleotide-Releasing Factor 2
Language	English
Publishing date	2018-12-19
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1478-811X
ISSN (online)	1478-811X
DOI	10.1186/s12964-018-0311-5
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article: C3G forms complexes with Bcr-Abl and p38α MAPK at the focal adhesions in chronic myeloid leukemia cells: implication in the regulation of leukemic cell adhesion.

Maia, Vera / Ortiz-Rivero, Sara / Sanz, María / Gutierrez-Berzal, Javier / Alvarez-Fernández, Indira / Gutierrez-Herrero, Sara / de Pereda, Jose María / Porras, Almudena / Guerrero, Carmen

Cell communication and signaling : CCS

2013 Volume 11, Issue 1, Page(s) 9

Abstract: Background: Previous studies by our group and others have shown that C3G interacts with Bcr-Abl through its SH3-b domain.: Results: In this work we show that C3G and Bcr-Abl form complexes with the focal adhesion (FA) proteins CrkL, p130Cas, Cbl and ... ...

Abstract	Background: Previous studies by our group and others have shown that C3G interacts with Bcr-Abl through its SH3-b domain. Results: In this work we show that C3G and Bcr-Abl form complexes with the focal adhesion (FA) proteins CrkL, p130Cas, Cbl and Abi1 through SH3/SH3-b interactions. The association between C3G and Bcr-Abl decreased upon Abi1 or p130Cas knock-down in K562 cells, which suggests that Abi1 and p130Cas are essential partners in this interaction. On the other hand, C3G, Abi1 or Cbl knock-down impaired adhesion to fibronectin, while p130Cas silencing enhanced it. C3G, Cbl and p130Cas-SH3-b domains interact directly with common proteins involved in the regulation of cell adhesion and migration. Immunoprecipitation and immunofluorescence studies revealed that C3G form complexes with the FA proteins paxillin and FAK and their phosphorylated forms. Additionally, C3G, Abi1, Cbl and p130Cas regulate the expression and phosphorylation of paxillin and FAK. p38α MAPK also participates in the regulation of adhesion in chronic myeloid leukemia cells. It interacts with C3G, CrkL, FAK and paxillin and regulates the expression of paxillin, CrkL and α5 integrin, as well as paxillin phosphorylation. Moreover, double knock-down of C3G/p38α decreased adhesion to fibronectin, similarly to the single silencing of one of these genes, either C3G or p38α. These suggest that C3G and p38α MAPK are acting through a common pathway to regulate cell adhesion in K562 cells, as previously described for the regulation of apoptosis. Conclusions: Our results indicate that C3G-p38αMAPK pathway regulates K562 cell adhesion through the interaction with FA proteins and Bcr-Abl, modulating the formation of different protein complexes at FA.
Language	English
Publishing date	2013-01-23
Publishing country	England
Document type	Journal Article
ISSN	1478-811X
ISSN	1478-811X
DOI	10.1186/1478-811X-11-9
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: The autoimmunity risk variant LYP-W620 cooperates with CSK in the regulation of TCR signaling.

de la Puerta, María Luisa / Trinidad, Antonio G / Rodríguez, María del Carmen / de Pereda, José María / Sánchez Crespo, Mariano / Bayón, Yolanda / Alonso, Andrés

PloS one

2013 Volume 8, Issue 1, Page(s) e54569

Abstract: The protein tyrosine phosphatase LYP, a key regulator of TCR signaling, presents a single nucleotide polymorphism, C1858T, associated with several autoimmune diseases such as type I diabetes, rheumatoid arthritis, and lupus. This polymorphism changes an ... ...

Abstract	The protein tyrosine phosphatase LYP, a key regulator of TCR signaling, presents a single nucleotide polymorphism, C1858T, associated with several autoimmune diseases such as type I diabetes, rheumatoid arthritis, and lupus. This polymorphism changes an R by a W in the P1 Pro rich motif of LYP, which binds to CSK SH3 domain, another negative regulator of TCR signaling. Based on the analysis of the mouse homologue, Pep, it was proposed that LYP and CSK bind constitutively to inhibit LCK and subsequently TCR signaling. The detailed study of LYP/CSK interaction, here presented, showed that LYP/CSK interaction was inducible upon TCR stimulation, and involved LYP P1 and P2 motifs, and CSK SH3 and SH2 domains. Abrogating LYP/CSK interaction did not preclude the regulation of TCR signaling by these proteins.
MeSH term(s)	Autoimmune Diseases/genetics ; Autoimmunity ; CSK Tyrosine-Protein Kinase ; Electrophoresis, Polyacrylamide Gel ; Flow Cytometry ; HEK293 Cells ; Humans ; Immunohistochemistry ; Jurkat Cells ; Models, Molecular ; Phosphorylation ; Polymorphism, Single Nucleotide ; Protein Binding ; Protein Tyrosine Phosphatases/genetics ; Protein Tyrosine Phosphatases/physiology ; Receptors, Antigen, T-Cell/metabolism ; Signal Transduction/physiology ; src-Family Kinases/physiology
Chemical Substances	Receptors, Antigen, T-Cell ; CSK Tyrosine-Protein Kinase (EC 2.7.10.2) ; src-Family Kinases (EC 2.7.10.2) ; CSK protein, human (EC 2.7.10.23) ; Protein Tyrosine Phosphatases (EC 3.1.3.48)
Language	English
Publishing date	2013-01-24
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0054569
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

Article ; Online: Sequence determinants of a microtubule tip localization signal (MtLS).

Buey, Rubén M / Sen, Indrani / Kortt, Oliver / Mohan, Renu / Gfeller, David / Veprintsev, Dmitry / Kretzschmar, Ines / Scheuermann, Jörg / Neri, Dario / Zoete, Vincent / Michielin, Olivier / de Pereda, José María / Akhmanova, Anna / Volkmer, Rudolf / Steinmetz, Michel O

The Journal of biological chemistry

2012 Volume 287, Issue 34, Page(s) 28227–28242

Abstract: Microtubule plus-end-tracking proteins (+TIPs) specifically localize to the growing plus-ends of microtubules to regulate microtubule dynamics and functions. A large group of +TIPs contain a short linear motif, SXIP, which is essential for them to bind ... ...

Abstract	Microtubule plus-end-tracking proteins (+TIPs) specifically localize to the growing plus-ends of microtubules to regulate microtubule dynamics and functions. A large group of +TIPs contain a short linear motif, SXIP, which is essential for them to bind to end-binding proteins (EBs) and target microtubule ends. The SXIP sequence site thus acts as a widespread microtubule tip localization signal (MtLS). Here we have analyzed the sequence-function relationship of a canonical MtLS. Using synthetic peptide arrays on membrane supports, we identified the residue preferences at each amino acid position of the SXIP motif and its surrounding sequence with respect to EB binding. We further developed an assay based on fluorescence polarization to assess the mechanism of the EB-SXIP interaction and to correlate EB binding and microtubule tip tracking of MtLS sequences from different +TIPs. Finally, we investigated the role of phosphorylation in regulating the EB-SXIP interaction. Together, our results define the sequence determinants of a canonical MtLS and provide the experimental data for bioinformatics approaches to carry out genome-wide predictions of novel +TIPs in multiple organisms.
MeSH term(s)	Amino Acid Motifs ; Arabidopsis/chemistry ; Arabidopsis/genetics ; Arabidopsis/metabolism ; Arabidopsis Proteins/chemistry ; Arabidopsis Proteins/genetics ; Arabidopsis Proteins/metabolism ; Humans ; Microtubule Proteins/chemistry ; Microtubule Proteins/genetics ; Microtubule Proteins/metabolism ; Microtubules/chemistry ; Microtubules/genetics ; Microtubules/metabolism ; Protein Array Analysis ; Protein Binding ; Protein Sorting Signals/physiology ; Schizosaccharomyces/chemistry ; Schizosaccharomyces/genetics ; Schizosaccharomyces/metabolism ; Schizosaccharomyces pombe Proteins/chemistry ; Schizosaccharomyces pombe Proteins/genetics ; Schizosaccharomyces pombe Proteins/metabolism
Chemical Substances	Arabidopsis Proteins ; Microtubule Proteins ; Protein Sorting Signals ; Schizosaccharomyces pombe Proteins
Language	English
Publishing date	2012-06-13
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M112.373928
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uc I Zs.108: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article: Increased riboflavin production by manipulation of inosine 5′-monophosphate dehydrogenase in Ashbya gossypii

Buey, Rubén M. / Ledesma-Amaro, Rodrigo / Balsera, Mónica / de Pereda, José María / Revuelta, José Luis

Applied microbiology and biotechnology

Volume v. 99,, Issue no. 2

Abstract	Guanine nucleotides are the precursors of essential biomolecules including nucleic acids and vitamins such as riboflavin. The enzyme inosine-5′-monophosphate dehydrogenase (IMPDH) catalyzes the ratelimiting step in the guanine nucleotide de novo biosynthetic pathway and plays a key role in controlling the cellular nucleotide pools. Thus, IMPDH is an important metabolic bottleneck in the guanine nucleotide synthesis, susceptible of manipulation by means of metabolic engineering approaches. Herein, we report the functional and structural characterization of the IMPDH enzyme from the industrial fungus Ashbya gossypii. Our data show that the overexpression of the IMPDH gene increases the metabolic flux through the guanine pathway and ultimately enhances 40 % riboflavin production with respect to the wild type. Also, IMPDH disruption results in a 100-fold increase of inosine excretion to the culture media. Our results contribute to the developing metabolic engineering toolbox aiming at improving the production of metabolites with biotechnological interest in A. gossypii.
Keywords	metabolites ; biochemical pathways ; Eremothecium gossypii ; guanine ; genes ; riboflavin ; gene overexpression ; metabolic engineering ; excretion ; guanine nucleotides ; fungi ; nucleic acids ; culture media ; nucleotides
Language	English
Document type	Article
ISSN	0175-7598
Database	AGRIS - International Information System for the Agricultural Sciences and Technology

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Bonn / Germany

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

Order via subito

Inter-library loan at ZB MED

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED