UB Paderborn / Katalog / Suche / in CDI

1 – 25 von 1.904

Sortiert nach

The ACT Domain: A Small Molecule Binding Domain and Its Role as a Common Regulatory Element

The Journal of biological chemistry, 2006-11, Vol.281 (45), p.33825-33829

Grant, Gregory A.

2006

Link zum Volltext

Verfügbarkeit prüfen

D-3-Phosphoglycerate Dehydrogenase

Frontiers in molecular biosciences, 2018-12, Vol.5, p.110-110

Grant, Gregory A

2018

Link zum Volltext

Verfügbarkeit prüfen

Contrasting catalytic and allosteric mechanisms for phosphoglycerate dehydrogenases

Archives of biochemistry and biophysics, 2012-03, Vol.519 (2), p.175-185

Grant, Gregory A.

2012

Link zum Volltext

Verfügbarkeit prüfen

Regulation of Mycobacterium tuberculosis d‑3-Phosphoglycerate Dehydrogenase by Phosphate-Modulated Quaternary Structure Dynamics and a Potential Role for Polyphosphate in Enzyme Regulation

Biochemistry (Easton), 2014-07, Vol.53 (26), p.4239-4249

2014

Link zum Volltext

Verfügbarkeit prüfen

The many faces of partial inhibition: Revealing imposters with graphical analysis

Archives of biochemistry and biophysics, 2018-09, Vol.653, p.10-23

Grant, Gregory A.

2018

Link zum Volltext

Verfügbarkeit prüfen

Elucidation of a Self-Sustaining Cycle in Escherichia coli l‑Serine Biosynthesis That Results in the Conservation of the Coenzyme, NAD

Biochemistry (Easton), 2018-03, Vol.57 (11), p.1798-1806

Grant, Gregory A

2018

Link zum Volltext

Verfügbarkeit prüfen

Regulatory Mechanism of Mycobacterium tuberculosis Phosphoserine Phosphatase SerB2

Biochemistry (Easton), 2017-12, Vol.56 (49), p.6481-6490

Grant, Gregory A

2017

Link zum Volltext

Verfügbarkeit prüfen

Structural Analysis of Substrate and Effector Binding in Mycobacterium tuberculosis d-3-Phosphoglycerate Dehydrogenase

Biochemistry (Easton), 2008-08, Vol.47 (32), p.8271-8282

2008

Link zum Volltext

Verfügbarkeit prüfen

Stopped Flow Transient Kinetic Analysis of Substrate Binding and Catalysis in Escherichia coli D-3-Phosphoglycerate Dehydrogenase

The Journal of biological chemistry, 2008-10, Vol.283 (44), p.29706-29714

2008

Link zum Volltext

Verfügbarkeit prüfen

Novel Mechanism for Substrate Inhibition in Mycobacterium tuberculosis D-3-Phosphoglycerate Dehydrogenase

The Journal of biological chemistry, 2007-10, Vol.282 (43), p.31517-31524

2007

Link zum Volltext

Verfügbarkeit prüfen

Kinetic Evidence of a Noncatalytic Substrate Binding Site That Regulates Activity in Legionella pneumophila l‑Serine Dehydratase

Biochemistry (Easton), 2012-09, Vol.51 (35), p.6961-6967

Grant, Gregory A

2012

Link zum Volltext

Verfügbarkeit prüfen

Modification of Cysteine

Current Protocols in Protein Science, 2017-02, Vol.87 (1), p.15.1.1-15.1.23

Grant, Gregory A.

2017

Link zum Volltext

Verfügbarkeit prüfen

Vmax Regulation through Domain and Subunit Changes. The Active Form of Phosphoglycerate Dehydrogenase

Biochemistry (Easton), 2005-04, Vol.44 (15), p.5763-5773

2005

Link zum Volltext

Verfügbarkeit prüfen

Mutagenic and chemical analyses provide new insight into enzyme activation and mechanism of the type 2 iron-sulfur l-serine dehydratase from Legionella pneumophila

Archives of biochemistry and biophysics, 2016-04, Vol.596, p.108-117

2016

Link zum Volltext

Verfügbarkeit prüfen

D-3-Phosphoglycerate Dehydrogenase from Mycobacterium tuberculosis Is a Link between the Escherichia coli and Mammalian Enzymes

The Journal of biological chemistry, 2005-04, Vol.280 (15), p.14884-14891

2005

Link zum Volltext

Verfügbarkeit prüfen

Hydrogen–Deuterium Exchange Mass Spectrometry Reveals Unique Conformational and Chemical Transformations Occurring upon [4Fe-4S] Cluster Binding in the Type 2 l‑Serine Dehydratase from Legionella pneumophila

Biochemistry (Easton), 2015-09, Vol.54 (34), p.5322-5328

2015

Link zum Volltext

Verfügbarkeit prüfen

The Effect of Hinge Mutations on Effector Binding and Domain Rotation in Escherichia coli D-3-Phosphoglycerate Dehydrogenase

The Journal of biological chemistry, 2007-06, Vol.282 (25), p.18418-18426

2007

Link zum Volltext

Verfügbarkeit prüfen

Structure of l‑Serine Dehydratase from Legionella pneumophila: Novel Use of the C‑Terminal Cysteine as an Intrinsic Competitive Inhibitor

Biochemistry (Easton), 2014-12, Vol.53 (48), p.7615-7624

2014

Link zum Volltext

Verfügbarkeit prüfen

Identification and characterization of two new types of bacterial l-serine dehydratases and assessment of the function of the ACT domain

Archives of biochemistry and biophysics, 2013-12, Vol.540 (1-2), p.62-69

2013

Link zum Volltext

Verfügbarkeit prüfen

Transient Kinetic Analysis of l-Serine Interaction with Escherichia coli d-3-Phosphoglycerate Dehydrogenase Containing Amino Acid Mutations in the Hinge Regions

Biochemistry (Easton), 2011-04, Vol.50 (14), p.2900-2906

Grant, Gregory A

2011

Link zum Volltext

Verfügbarkeit prüfen

Allosteric Activation and Contrasting Properties of l-Serine Dehydratase Types 1 and 2

Biochemistry (Easton), 2012-07, Vol.51 (26), p.5320-5328

2012

Link zum Volltext

Verfügbarkeit prüfen

Kinetic, mutagenic, and structural homology analysis of l-serine dehydratase from Legionella pneumophila

Archives of biochemistry and biophysics, 2011-11, Vol.515 (1-2), p.28-36

2011

Link zum Volltext

Verfügbarkeit prüfen

Comparison of Type 1 D-3-phosphoglycerate dehydrogenases reveals unique regulation in pathogenic Mycobacteria

Archives of biochemistry and biophysics, 2015-03, Vol.570, p.32-39

2015

Link zum Volltext

Verfügbarkeit prüfen

Quantitative Relationships of Site to Site Interaction in Escherichia coli d-3-Phosphoglycerate Dehydrogenase Revealed by Asymmetric Hybrid Tetramers

The Journal of biological chemistry, 2004-04, Vol.279 (14), p.13452-13460

2004

Link zum Volltext

Verfügbarkeit prüfen

Crystal structure of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase: extreme asymmetry in a tetramer of identical subunits

The Journal of biological chemistry, 2005-04, Vol.280 (15), p.14892-14899

2005

Link zum Volltext

Verfügbarkeit prüfen

1 – 25 von 1.904

Suche als RSS-Feed

Suchergebnisse filtern

Filter anzeigen

Nur zeigen

Geprüft (Peer-Review)
(1.676)
Mit Volltextzugriff
(1.699)

Publikationsform

5 weitere anzeigen...

Weniger anzeigen...

Sprache

3 weitere anzeigen...

Weniger anzeigen...

Erscheinungsjahr

n.n

Thema

Science & Technology
(1.165)
Life Sciences & Biomedicine
(914)
Humans
(597)
Male
(351)
Female
(318)
Animals
(223)
Biological And Medical Sciences
(214)
Adult
(203)
Physical Sciences
(189)
Middle Aged
(179)
Medical Sciences
(141)
Biochemistry & Molecular Biology
(123)
Technology
(116)
Aged
(113)
Surgery
(111)
Chemistry
(102)
Orthopedics
(94)
Neurosciences & Neurology
(90)
Science & Technology - Other Topics
(88)
Mice
(83)

15 weitere anzeigen...

Weniger anzeigen...

Neu hinzugefügt

Menü

Weitere Dienste

Einstellungen

The ACT Domain: A Small Molecule Binding Domain and Its Role as a Common Regulatory Element

D-3-Phosphoglycerate Dehydrogenase

Contrasting catalytic and allosteric mechanisms for phosphoglycerate dehydrogenases

Regulation of Mycobacterium tuberculosis d‑3-Phosphoglycerate Dehydrogenase by Phosphate-Modulated Quaternary Structure Dynamics and a Potential Role for Polyphosphate in Enzyme Regulation

The many faces of partial inhibition: Revealing imposters with graphical analysis

Elucidation of a Self-Sustaining Cycle in Escherichia coli l‑Serine Biosynthesis That Results in the Conservation of the Coenzyme, NAD

Regulatory Mechanism of Mycobacterium tuberculosis Phosphoserine Phosphatase SerB2

Structural Analysis of Substrate and Effector Binding in Mycobacterium tuberculosis d-3-Phosphoglycerate Dehydrogenase

Stopped Flow Transient Kinetic Analysis of Substrate Binding and Catalysis in Escherichia coli D-3-Phosphoglycerate Dehydrogenase

Novel Mechanism for Substrate Inhibition in Mycobacterium tuberculosis D-3-Phosphoglycerate Dehydrogenase

Kinetic Evidence of a Noncatalytic Substrate Binding Site That Regulates Activity in Legionella pneumophila l‑Serine Dehydratase

Modification of Cysteine

Vmax Regulation through Domain and Subunit Changes. The Active Form of Phosphoglycerate Dehydrogenase

Mutagenic and chemical analyses provide new insight into enzyme activation and mechanism of the type 2 iron-sulfur l-serine dehydratase from Legionella pneumophila

D-3-Phosphoglycerate Dehydrogenase from Mycobacterium tuberculosis Is a Link between the Escherichia coli and Mammalian Enzymes

Hydrogen–Deuterium Exchange Mass Spectrometry Reveals Unique Conformational and Chemical Transformations Occurring upon [4Fe-4S] Cluster Binding in the Type 2 l‑Serine Dehydratase from Legionella pneumophila

The Effect of Hinge Mutations on Effector Binding and Domain Rotation in Escherichia coli D-3-Phosphoglycerate Dehydrogenase

Structure of l‑Serine Dehydratase from Legionella pneumophila: Novel Use of the C‑Terminal Cysteine as an Intrinsic Competitive Inhibitor

Identification and characterization of two new types of bacterial l-serine dehydratases and assessment of the function of the ACT domain

Transient Kinetic Analysis of l-Serine Interaction with Escherichia coli d-3-Phosphoglycerate Dehydrogenase Containing Amino Acid Mutations in the Hinge Regions

Allosteric Activation and Contrasting Properties of l-Serine Dehydratase Types 1 and 2

Kinetic, mutagenic, and structural homology analysis of l-serine dehydratase from Legionella pneumophila

Comparison of Type 1 D-3-phosphoglycerate dehydrogenases reveals unique regulation in pathogenic Mycobacteria

Quantitative Relationships of Site to Site Interaction in Escherichia coli d-3-Phosphoglycerate Dehydrogenase Revealed by Asymmetric Hybrid Tetramers

Crystal structure of Mycobacterium tuberculosis D-3-phosphoglycerate dehydrogenase: extreme asymmetry in a tetramer of identical subunits

Suchergebnisse filtern