UB Paderborn / Katalog / Suche / in CDI

Sortiert nach

Einfacher Volltextzugriff von (fast) überall

Installieren Sie die LibKey Nomad-Browsererweiterung und erhalten Sie von vielen Webseiten einfachen Zugriff auf lizenzierte Volltexte oder Open Access Publikationen. Mehr erfahren...

Molecular enzymology of 5-Aminolevulinate synthase, the gatekeeper of heme biosynthesis

Biochimica et biophysica acta, 2011-11, Vol.1814 (11), p.1467-1473

2011

Volltextzugriff (PDF)

Anti-Correlation between the Dynamics of the Active Site Loop and C-Terminal Tail in Relation to the Homodimer Asymmetry of the Mouse Erythroid 5-Aminolevulinate Synthase

International journal of molecular sciences, 2018-06, Vol.19 (7), p.1899

2018

Volltextzugriff (PDF)

Expression of murine 5-aminolevulinate synthase variants causes protoporphyrin IX accumulation and light-induced mammalian cell death

PloS one, 2014-04, Vol.9 (4), p.e93078-e93078

2014

Volltextzugriff (PDF)

Metal Ion Substrate Inhibition of Ferrochelatase

The Journal of biological chemistry, 2008-08, Vol.283 (35), p.23685-23691

2008

Volltextzugriff (PDF)

Porphyrin Binding and Distortion and Substrate Specificity in the Ferrochelatase Reaction: The Role of Active Site Residues

Journal of molecular biology, 2008-05, Vol.378 (5), p.1074-1083

2008

Volltextzugriff (PDF)

ALAS2 acts as a modifier gene in patients with congenital erythropoietic porphyria

Blood, 2011-08, Vol.118 (6), p.1443-1451

2011

Volltextzugriff (PDF)

Transient State Kinetic Investigation of 5-Aminolevulinate Synthase Reaction Mechanism

The Journal of biological chemistry, 2002-11, Vol.277 (47), p.44660-44669

2002

Volltextzugriff (PDF)

Isoniazid inhibits human erythroid 5-aminolevulinate synthase: Molecular mechanism and tolerance study with four X-linked protoporphyria patients

Biochimica et biophysica acta. Molecular basis of disease, 2017-02, Vol.1863 (2), p.428-439

2017

Volltextzugriff (PDF)

The Conserved Active-Site Loop Residues of Ferrochelatase Induce Porphyrin Conformational Changes Necessary for Catalysis

Biochemistry (Easton), 2006-03, Vol.45 (9), p.2904-2912

2006

Volltextzugriff (PDF)

Hypoxic up-regulation of erythroid 5-aminolevulinate synthase

Blood, 2003-01, Vol.101 (1), p.348-350

2003

Volltextzugriff (PDF)

Molecular and functional analysis of the C-terminal region of human erythroid-specific 5-aminolevulinic synthase associated with X-linked dominant protoporphyria (XLDPP)

Human molecular genetics, 2013-04, Vol.22 (7), p.1280-1288

2013

Volltextzugriff (PDF)

Porphyrin overdrive rewires cancer cell metabolism

Life science alliance, 2024-07, Vol.7 (7), p.e202302547

2024

Volltextzugriff (PDF)

Human Erythroid 5‑Aminolevulinate Synthase Mutations Associated with X‑Linked Protoporphyria Disrupt the Conformational Equilibrium and Enhance Product Release

Biochemistry (Easton), 2015-09, Vol.54 (36), p.5617-5631

2015

Volltextzugriff (PDF)

Identification and Characterization of an Inhibitory Metal Ion-binding Site in Ferrochelatase

The Journal of biological chemistry, 2010-12, Vol.285 (53), p.41836-41842

2010

Volltextzugriff (PDF)

Chelatases: distort to select?

Trends in biochemical sciences (Amsterdam. Regular ed.), 2006-03, Vol.31 (3), p.135-142

2006

Volltextzugriff (PDF)

Transcriptional regulation of the murine erythroid-specific 5-aminolevulinate synthase gene

Gene, 2000-04, Vol.247 (1), p.153-166

2000

Volltextzugriff (PDF)

Assembly of Human Frataxin Is a Mechanism for Detoxifying Redox-Active Iron

Biochemistry (Easton), 2005-01, Vol.44 (2), p.537-545

2005

Volltextzugriff (PDF)

A continuous anaerobic fluorimetric assay for ferrochelatase by monitoring porphyrin disappearance

Analytical biochemistry, 2003-07, Vol.318 (1), p.18-24

2003

Volltextzugriff (PDF)

The First Structure from the SOUL/HBP Family of Heme-binding Proteins, Murine P22HBP

The Journal of biological chemistry, 2006-10, Vol.281 (42), p.31553-31561

2006

Volltextzugriff (PDF)

5-aminolevulinate synthase: catalysis of the first step of heme biosynthesis

Cellular and molecular biology (Noisy-le-Grand, France), 2009-02, Vol.55 (1), p.102-110

2009

Volltextzugriff (PDF)

Mutations in the iron-sulfur cluster ligands of the human ferrochelatase lead to erythropoietic protoporphyria

Blood, 2000-08, Vol.96 (4), p.1545-1549

2000

Volltextzugriff (PDF)

Circular permutation of 5-aminolevulinate synthase as a tool to evaluate folding, structure and function

Cellular and molecular biology (Noisy-le-Grand, France), 2002-02, Vol.48 (1), p.11

2002

Volltextzugriff (PDF)

Heme biosynthesis: biochemistry, molecular biology, and relationship to disease

Journal of bioenergetics and biomembranes, 1995-04, Vol.27 (2), p.147-150

Ferreira, G C

1995

Volltextzugriff (PDF)

Ferrochelatase

The international journal of biochemistry & cell biology, 1999-10, Vol.31 (10), p.995-1000

Ferreira, Gloria C.

1999

Volltextzugriff (PDF)

5-Aminolevulinate synthase and the first step of heme biosynthesis

Journal of bioenergetics and biomembranes, 1995-04, Vol.27 (2), p.151-159

1995

Volltextzugriff (PDF)

1 – 25 von 60

Suche als RSS-Feed

Aktive Filter

ThemaHumans

Suchergebnisse filtern

Filter anzeigen

Nur zeigen

Geprüft (Peer-Review)
(59)
Mit Volltextzugriff
(54)

Publikationsform

Artikel
(60)

Sprache

Englisch
(60)

Erscheinungsjahr

n.n

Thema

Science & Technology
(56)
Life Sciences & Biomedicine
(53)
Female
(27)
Male
(23)
Animals
(22)
Adult
(17)
Biochemistry & Molecular Biology
(17)
Middle Aged
(17)
Mice
(13)
Aged
(12)
Biological And Medical Sciences
(10)
5-Aminolevulinate Synthetase - Genetics
(9)
5-Aminolevulinate Synthetase - Metabolism
(9)
Adolescent
(9)
Mutation
(9)
Young Adult
(9)
5-Aminolevulinate Synthetase - Chemistry
(8)
Cell Biology
(8)
Heme
(8)

14 weitere anzeigen...

Weniger anzeigen...

Neu hinzugefügt

... seit 90 Tagen
(1)

Menü

Weitere Dienste

Einstellungen

Molecular enzymology of 5-Aminolevulinate synthase, the gatekeeper of heme biosynthesis

Anti-Correlation between the Dynamics of the Active Site Loop and C-Terminal Tail in Relation to the Homodimer Asymmetry of the Mouse Erythroid 5-Aminolevulinate Synthase

Expression of murine 5-aminolevulinate synthase variants causes protoporphyrin IX accumulation and light-induced mammalian cell death

Metal Ion Substrate Inhibition of Ferrochelatase

Porphyrin Binding and Distortion and Substrate Specificity in the Ferrochelatase Reaction: The Role of Active Site Residues

ALAS2 acts as a modifier gene in patients with congenital erythropoietic porphyria

Transient State Kinetic Investigation of 5-Aminolevulinate Synthase Reaction Mechanism

Isoniazid inhibits human erythroid 5-aminolevulinate synthase: Molecular mechanism and tolerance study with four X-linked protoporphyria patients

The Conserved Active-Site Loop Residues of Ferrochelatase Induce Porphyrin Conformational Changes Necessary for Catalysis

Hypoxic up-regulation of erythroid 5-aminolevulinate synthase

Molecular and functional analysis of the C-terminal region of human erythroid-specific 5-aminolevulinic synthase associated with X-linked dominant protoporphyria (XLDPP)

Porphyrin overdrive rewires cancer cell metabolism

Human Erythroid 5‑Aminolevulinate Synthase Mutations Associated with X‑Linked Protoporphyria Disrupt the Conformational Equilibrium and Enhance Product Release

Identification and Characterization of an Inhibitory Metal Ion-binding Site in Ferrochelatase

Chelatases: distort to select?

Transcriptional regulation of the murine erythroid-specific 5-aminolevulinate synthase gene

Assembly of Human Frataxin Is a Mechanism for Detoxifying Redox-Active Iron

A continuous anaerobic fluorimetric assay for ferrochelatase by monitoring porphyrin disappearance

The First Structure from the SOUL/HBP Family of Heme-binding Proteins, Murine P22HBP

5-aminolevulinate synthase: catalysis of the first step of heme biosynthesis

Mutations in the iron-sulfur cluster ligands of the human ferrochelatase lead to erythropoietic protoporphyria

Circular permutation of 5-aminolevulinate synthase as a tool to evaluate folding, structure and function

Heme biosynthesis: biochemistry, molecular biology, and relationship to disease

Ferrochelatase

5-Aminolevulinate synthase and the first step of heme biosynthesis

Aktive Filter

Suchergebnisse filtern