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3P-032 Atomic Resolution Structures Indicate A Molecular Mechanism for Iron Release Through Functional Pore in Ferritin.(Protein:Structure & Function,The 47th Annual Meeting of the Biophysical Society of Japan)

Seibutsu Butsuri, 2009/09/20, Vol.49(supplement), pp.S156

2009

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3P-032 高分解能結晶構造によるフェリチンにおける鉄放出の分子機構の解明(蛋白質-構造機能相関,第47回日本生物物理学会年会)

生物物理, 2009/09/20, Vol.49(supplement), pp.S156

2009

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Absence of interdomain contacts in the crystal structure of the RNA recognition motifs of Sex-lethal

Proceedings of the National Academy of Sciences - PNAS, 1999-04, Vol.96 (9), p.4892-4897

1999

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Accessing protein conformational ensembles using room-temperature X-ray crystallography

Proceedings of the National Academy of Sciences - PNAS, 2011-09, Vol.108 (39), p.16247-16252

2011

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AFF1 is a ubiquitous P-TEFb partner to enable Tat extraction of P-TEFb from 7SK snRNP and formation of SECs for HIV transactivation

Proceedings of the National Academy of Sciences - PNAS, 2014-01, Vol.111 (1), p.E15-E24

2014

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AFF1 is a ubiquitous P-TEFb partner to enable Tat extraction of P-TEFb from 7SK snRNP and formation of SECs for HIV transactivation

Proceedings of the National Academy of Sciences - PNAS, 2014-01, Vol.111 (1), p.11-11

2014

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AFF4 binding to Tat-P-TEFb indirectly stimulates TAR recognition of super elongation complexes at the HIV promoter

eLife, 2014-04, Vol.3, p.e02375-e02375

2014

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The AFF4 scaffold binds human P-TEFb adjacent to HIV Tat

eLife, 2013-03, Vol.2, p.e00327

2013

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AIDS-related mycoses: the way forward

Trends in microbiology, 2014-03, Vol.22 (3), p.107-109

2014

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Allosteric Activation by Dimerization of the PknD Receptor Ser/Thr Protein Kinase from Mycobacterium tuberculosis

The Journal of biological chemistry, 2007-04, Vol.282 (15), p.11427-11435

2007

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Allosteric Activation Mechanism of the Mycobacterium tuberculosis Receptor Ser/Thr Protein Kinase, PknB

Structure (London), 2010-12, Vol.18 (12), p.1667-1677

2010

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An Alternate Conformation and a Third Metal in PstP/Ppp, the M. tuberculosis PP2C-Family Ser/Thr Protein Phosphatase

Structure (London), 2004-11, Vol.12 (11), p.1947-1954

2004

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Assessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystal structure of the unregulated catalytic subunit

Proceedings of the National Academy of Sciences - PNAS, 1999-05, Vol.96 (10)

1999

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Assessment of the Allosteric Mechanism of Aspartate Transcarbamoylase Based on the Crystalline Structure of the Unregulated Catalytic Subunit

Proceedings of the National Academy of Sciences - PNAS, 1999-05, Vol.96 (10), p.5388-5393

1999

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atypical receiver domain controls the dynamic polar localization of the Myxococcus xanthus social motility protein FrzS

Molecular microbiology, 2007-07, Vol.65 (2), p.319-332

2007

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Auto-activation mechanism of the Mycobacterium tuberculosis PknB receptor Ser/Thr kinase

The EMBO journal, 2008-12, Vol.27 (23), p.3186-3197

2008

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Autofluorescent Proteins with Excitation in the Optical Window for Intravital Imaging in Mammals

Chemistry & biology, 2009-11, Vol.16 (11), p.1169-1179

2009

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Automated electron‐density sampling reveals widespread conformational polymorphism in proteins

Protein science, 2010-07, Vol.19 (7), p.1420-1431

2010

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Automated Protein Crystal Structure Determination Using ELVES

Proceedings of the National Academy of Sciences - PNAS, 2004-02, Vol.101 (6), p.1537-1542

2004

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Bacterial Communities Vary between Sinuses in Chronic Rhinosinusitis Patients

Frontiers in microbiology, 2016-01, Vol.6, p.1532-1532

2016

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Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of asparate transcarbamoylase: Implications for allosteric regulation

Proceedings of the National Academy of Sciences - PNAS, 2000-05, Vol.97 (10), p.5077

2000

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Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: Implications for allosteric regulation

Atti della Accademia nazionale dei Lincei. Rendiconti Lincei. Scienze fisiche e naturali, 2006-03, Vol.17 (1-2), p.133-145

2006

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Binding of Bisubstrate Analog Promotes Large Structural Changes in the Unregulated Catalytic Trimer of Aspartate Transcarbamoylase: Implications for Allosteric Regulation

Proceedings of the National Academy of Sciences - PNAS, 2000-05, Vol.97 (10), p.5077-5082

2000

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Biochemical and Spatial Coincidence in the Provisional Ser/Thr Protein Kinase Interaction Network of Mycobacterium tuberculosis

The Journal of biological chemistry, 2014-07, Vol.289 (30), p.20422-20433

2014

Volltextzugriff (PDF)

Biochemical and Structural Basis for Partially Redundant Enzymatic and Transcriptional Functions of DCoH and DCoH2

Biochemistry (Easton), 2004-06, Vol.43 (23), p.7345-7355

2004

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3P-032 Atomic Resolution Structures Indicate A Molecular Mechanism for Iron Release Through Functional Pore in Ferritin.(Protein:Structure & Function,The 47th Annual Meeting of the Biophysical Society of Japan)

3P-032 高分解能結晶構造によるフェリチンにおける鉄放出の分子機構の解明(蛋白質-構造機能相関,第47回日本生物物理学会年会)

Absence of interdomain contacts in the crystal structure of the RNA recognition motifs of Sex-lethal

Accessing protein conformational ensembles using room-temperature X-ray crystallography

AFF1 is a ubiquitous P-TEFb partner to enable Tat extraction of P-TEFb from 7SK snRNP and formation of SECs for HIV transactivation

AFF1 is a ubiquitous P-TEFb partner to enable Tat extraction of P-TEFb from 7SK snRNP and formation of SECs for HIV transactivation

AFF4 binding to Tat-P-TEFb indirectly stimulates TAR recognition of super elongation complexes at the HIV promoter

The AFF4 scaffold binds human P-TEFb adjacent to HIV Tat

AIDS-related mycoses: the way forward

Allosteric Activation by Dimerization of the PknD Receptor Ser/Thr Protein Kinase from Mycobacterium tuberculosis

Allosteric Activation Mechanism of the Mycobacterium tuberculosis Receptor Ser/Thr Protein Kinase, PknB

An Alternate Conformation and a Third Metal in PstP/Ppp, the M. tuberculosis PP2C-Family Ser/Thr Protein Phosphatase

Assessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystal structure of the unregulated catalytic subunit

Assessment of the Allosteric Mechanism of Aspartate Transcarbamoylase Based on the Crystalline Structure of the Unregulated Catalytic Subunit

atypical receiver domain controls the dynamic polar localization of the Myxococcus xanthus social motility protein FrzS

Auto-activation mechanism of the Mycobacterium tuberculosis PknB receptor Ser/Thr kinase

Autofluorescent Proteins with Excitation in the Optical Window for Intravital Imaging in Mammals

Automated electron‐density sampling reveals widespread conformational polymorphism in proteins

Automated Protein Crystal Structure Determination Using ELVES

Bacterial Communities Vary between Sinuses in Chronic Rhinosinusitis Patients

Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of asparate transcarbamoylase: Implications for allosteric regulation

Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: Implications for allosteric regulation

Binding of Bisubstrate Analog Promotes Large Structural Changes in the Unregulated Catalytic Trimer of Aspartate Transcarbamoylase: Implications for Allosteric Regulation

Biochemical and Spatial Coincidence in the Provisional Ser/Thr Protein Kinase Interaction Network of Mycobacterium tuberculosis

Biochemical and Structural Basis for Partially Redundant Enzymatic and Transcriptional Functions of DCoH and DCoH2

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