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The Original Michaelis Constant: Translation of the 1913 Michaelis–Menten Paper

Biochemistry (Easton), 2011-10, Vol.50 (39), p.8264-8269

2011

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Molecular control of Rab activity by GEFs, GAPs and GDI

Small GTPases, 2018-03, Vol.9 (1-2), p.5-21

2018

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A toolkit and benchmark study for FRET-restrained high-precision structural modeling

Nature methods, 2012-12, Vol.9 (12), p.1218-1225

2012

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KRasG12C inhibitors in clinical trials: a short historical perspective

RSC medicinal chemistry, 2020-07, Vol.11 (7), p.76-77

2020

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The mechanism of activation of the actin binding protein EHBP1 by Rab8 family members

Nature communications, 2020-08, Vol.11 (1), p.4187-4187, Article 4187

2020

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RabGEFs are a major determinant for specific Rab membrane targeting

The Journal of cell biology, 2013-02, Vol.200 (3), p.287-300

2013

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role of the hypervariable C-terminal domain in Rab GTPases membrane targeting

Proceedings of the National Academy of Sciences - PNAS, 2014-02, Vol.111 (7), p.2572-2577

2014

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Rep15 interacts with several Rab GTPases and has a distinct fold for a Rab effector

Nature communications, 2022-07, Vol.13 (1), p.4262-4262, Article 4262

2022

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Direct Targeting of Rab-GTPase-Effector Interactions

Angewandte Chemie International Edition, 2014-02, Vol.53 (9), p.2498-2503

International ed. in English, 2014

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Intermediates in the Guanine Nucleotide Exchange Reaction of Rab8 Protein Catalyzed by Guanine Nucleotide Exchange Factors Rabin8 and GRAB

The Journal of biological chemistry, 2013-11, Vol.288 (45), p.32466-32474

2013

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Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase

ACS chemical biology, 2016-08, Vol.11 (8), p.2375-2382

2016

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Protein LidA from Legionella is a Rab GTPase supereffector

Proceedings of the National Academy of Sciences - PNAS, 2011-11, Vol.108 (44), p.17945-17950

2011

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Rab GTPase prenylation hierarchy and its potential role in choroideremia disease

PloS one, 2013-12, Vol.8 (12), p.e81758-e81758

2013

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Nucleotide based covalent inhibitors of KRas can only be efficient in vivo if they bind reversibly with GTP-like affinity

Scientific reports, 2017-06, Vol.7 (1), p.3687-11, Article 3687

2017

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A structural basis for Lowe syndrome caused by mutations in the Rab-binding domain of OCRL1

The EMBO journal, 2011-04, Vol.30 (8), p.1659-1670

2011

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Posttranslational modifications of Rab proteins cause effective displacement of GDP dissociation inhibitor

Proceedings of the National Academy of Sciences - PNAS, 2012-04, Vol.109 (15), p.5621-5626

2012

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Targeting oncogenic KRasG13C with nucleotide-based covalent inhibitors

eLife, 2023-03, Vol.12

2023

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Catalytic mechanism of a mammalian Rab·RabGAP complex in atomic detail

Proceedings of the National Academy of Sciences - PNAS, 2012-12, Vol.109 (52), p.21348-21353

2012

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α-Synuclein interacts with the switch region of Rab8a in a Ser129 phosphorylation-dependent manner

Neurobiology of disease, 2014-10, Vol.70, p.149-161

2014

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bMERB domains are bivalent Rab8 family effectors evolved by gene duplication

eLife, 2016-08, Vol.5

2016

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Membrane extraction of Rab proteins by GDP dissociation inhibitor characterized using attenuated total reflection infrared spectroscopy

Proceedings of the National Academy of Sciences - PNAS, 2013-08, Vol.110 (33), p.13380-13385

2013

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Analysis of the eukaryotic prenylome by isoprenoid affinity tagging

Nature chemical biology, 2009-04, Vol.5 (4), p.227-235

2009

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HIV-1 Nef membrane association depends on charge, curvature, composition and sequence

Nature chemical biology, 2010-01, Vol.6 (1), p.46-53

2010

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Highly Efficient Strategy for Modification of Proteins at the C Terminus

Angewandte Chemie (International ed.), 2010-12, Vol.49 (49), p.9417-9421

2010

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Membrane targeting mechanism of Rab GTPases elucidated by semisynthetic protein probes

Nature chemical biology, 2010-07, Vol.6 (7), p.534-540

2010

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The Original Michaelis Constant: Translation of the 1913 Michaelis–Menten Paper

Molecular control of Rab activity by GEFs, GAPs and GDI

A toolkit and benchmark study for FRET-restrained high-precision structural modeling

KRasG12C inhibitors in clinical trials: a short historical perspective

The mechanism of activation of the actin binding protein EHBP1 by Rab8 family members

RabGEFs are a major determinant for specific Rab membrane targeting

role of the hypervariable C-terminal domain in Rab GTPases membrane targeting

Rep15 interacts with several Rab GTPases and has a distinct fold for a Rab effector

Direct Targeting of Rab-GTPase-Effector Interactions

Intermediates in the Guanine Nucleotide Exchange Reaction of Rab8 Protein Catalyzed by Guanine Nucleotide Exchange Factors Rabin8 and GRAB

Protease-Resistant and Cell-Permeable Double-Stapled Peptides Targeting the Rab8a GTPase

Protein LidA from Legionella is a Rab GTPase supereffector

Rab GTPase prenylation hierarchy and its potential role in choroideremia disease

Nucleotide based covalent inhibitors of KRas can only be efficient in vivo if they bind reversibly with GTP-like affinity

A structural basis for Lowe syndrome caused by mutations in the Rab-binding domain of OCRL1

Posttranslational modifications of Rab proteins cause effective displacement of GDP dissociation inhibitor

Targeting oncogenic KRasG13C with nucleotide-based covalent inhibitors

Catalytic mechanism of a mammalian Rab·RabGAP complex in atomic detail

α-Synuclein interacts with the switch region of Rab8a in a Ser129 phosphorylation-dependent manner

bMERB domains are bivalent Rab8 family effectors evolved by gene duplication

Membrane extraction of Rab proteins by GDP dissociation inhibitor characterized using attenuated total reflection infrared spectroscopy

Analysis of the eukaryotic prenylome by isoprenoid affinity tagging

HIV-1 Nef membrane association depends on charge, curvature, composition and sequence

Highly Efficient Strategy for Modification of Proteins at the C Terminus

Membrane targeting mechanism of Rab GTPases elucidated by semisynthetic protein probes

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