Stephan Grzesiek
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View article: A high-resolution analysis of arrestin2 interactions responsible for CCR5 endocytosis
A high-resolution analysis of arrestin2 interactions responsible for CCR5 endocytosis Open
Clathrin-mediated endocytosis (CME) is crucial for regulating G protein-coupled receptors (GPCRs) via phosphorylation-dependent arrestin interactions. Despite detailed structural knowledge on the arrestin interactions with phosphorylated t…
View article: A high-resolution analysis of arrestin2 interactions responsible for CCR5 endocytosis
A high-resolution analysis of arrestin2 interactions responsible for CCR5 endocytosis Open
Clathrin-mediated endocytosis (CME) is crucial for regulating G protein-coupled receptors (GPCRs) via phosphorylation-dependent arrestin interactions. Despite detailed structural knowledge on the arrestin interactions with phosphorylated t…
View article: A high-resolution analysis of arrestin2 interactions responsible for CCR5 endocytosis
A high-resolution analysis of arrestin2 interactions responsible for CCR5 endocytosis Open
Clathrin-mediated endocytosis (CME) is crucial for regulating G protein-coupled receptors (GPCRs) via phosphorylation-dependent arrestin interactions. Despite detailed structural knowledge on the arrestin interactions with phosphorylated t…
View article: Arrestin recognizes GPCRs independently of the receptor state
Arrestin recognizes GPCRs independently of the receptor state Open
Only two nonvisual arrestins recognize many hundreds of different, intracellularly phosphorylated G protein-coupled receptors (GPCRs). Due to the highly dynamic nature of GPCR•arrestin complexes, the critical determinants of GPCR–arrestin …
View article: Functional dynamics of G protein-coupled receptors reveal new routes for drug discovery
Functional dynamics of G protein-coupled receptors reveal new routes for drug discovery Open
View article: A high-resolution analysis of arrestin2 interactions responsible for CCR5 endocytosis
A high-resolution analysis of arrestin2 interactions responsible for CCR5 endocytosis Open
Clathrin-mediated endocytosis (CME) is crucial for regulating G protein-coupled receptors (GPCRs) via phosphorylation-dependent arrestin interactions. Despite detailed structural knowledge on the arrestin interactions with phosphorylated t…
View article: Micrographs of carvedilol-B1AR-arrestin2-V2Rpp complex
Micrographs of carvedilol-B1AR-arrestin2-V2Rpp complex Open
View article: The molecular basis of Abelson kinase regulation by its αI-helix
The molecular basis of Abelson kinase regulation by its αI-helix Open
Abelson tyrosine kinase (Abl) is regulated by the arrangement of its regulatory core, consisting sequentially of the SH3, SH2, and kinase (KD) domains, where an assembled or disassembled core corresponds to low or high kinase activity, res…
View article: Author response: The molecular basis of Abelson kinase regulation by its αI-helix
Author response: The molecular basis of Abelson kinase regulation by its αI-helix Open
Full text Figures and data Peer review Side by side Abstract eLife assessment Introduction Results and discussion Materials and methods Data availability References Article and author information Metrics Abstract Abelson tyrosine kinase (A…
View article: Reviewer #1 (Public Review): The molecular basis of Abelson kinase regulation by its αI-helix
Reviewer #1 (Public Review): The molecular basis of Abelson kinase regulation by its αI-helix Open
Abelson tyrosine kinase (Abl) is regulated by the arrangement of its regulatory core, consisting sequentially of the SH3, SH2 and kinase (KD) domains, where an assembled or disassembled core corresponds to low or high kinase activity, resp…
View article: The molecular basis of Abelson kinase regulation by its αI-helix
The molecular basis of Abelson kinase regulation by its αI-helix Open
Abelson tyrosine kinase (Abl) is regulated by the arrangement of its regulatory core, consisting sequentially of the SH3, SH2 and kinase (KD) domains, where an assembled or disassembled core corresponds to low or high kinase activity, resp…
View article: Author Response: The molecular basis of Abelson kinase regulation by its αI-helix
Author Response: The molecular basis of Abelson kinase regulation by its αI-helix Open
Abelson tyrosine kinase (Abl) is regulated by the arrangement of its regulatory core, consisting sequentially of the SH3, SH2 and kinase (KD) domains, where an assembled or disassembled core corresponds to low or high kinase activity, resp…
View article: Reviewer #2 (Public Review): The molecular basis of Abelson kinase regulation by its αI-helix
Reviewer #2 (Public Review): The molecular basis of Abelson kinase regulation by its αI-helix Open
Abelson tyrosine kinase (Abl) is regulated by the arrangement of its regulatory core, consisting sequentially of the SH3, SH2 and kinase (KD) domains, where an assembled or disassembled core corresponds to low or high kinase activity, resp…
View article: The molecular basis of Abelson kinase regulation by its αI-helix
The molecular basis of Abelson kinase regulation by its αI-helix Open
Abelson tyrosine kinase (Abl) is regulated by the arrangement of its regulatory core, consisting sequentially of the SH3, SH2 and kinase (KD) domains, where an assembled or disassembled core corresponds to low or high kinase activity, resp…
View article: The molecular basis of Abelson kinase regulation by its αI-helix
The molecular basis of Abelson kinase regulation by its αI-helix Open
Abelson tyrosine kinase (Abl) is regulated by the arrangement of its regulatory core, consisting sequentially of the SH3, SH2, and kinase (KD) domains, where an assembled or disassembled core corresponds to low or high kinase activity, res…
View article: Reviewer #1 (Public Review): The molecular basis of Abelson kinase regulation by its αI-helix
Reviewer #1 (Public Review): The molecular basis of Abelson kinase regulation by its αI-helix Open
Abelson tyrosine kinase (Abl) is regulated by the arrangement of its regulatory core, consisting sequentially of the SH3, SH2 and kinase (KD) domains, where an assembled or disassembled core corresponds to low or high kinase activity, resp…
View article: The molecular basis of Abelson kinase regulation by its αI-helix
The molecular basis of Abelson kinase regulation by its αI-helix Open
Abelson tyrosine kinase (Abl) is regulated by the arrangement of its regulatory core, consisting sequentially of the SH3, SH2 and kinase (KD) domains, where an assembled or disassembled core corresponds to low or high kinase activity, resp…
View article: The key role of glutamine for protein expression and isotopic labeling in insect cells
The key role of glutamine for protein expression and isotopic labeling in insect cells Open
View article: Nanobody GPS by PCS: An Efficient New NMR Analysis Method for G Protein Coupled Receptors and Other Large Proteins
Nanobody GPS by PCS: An Efficient New NMR Analysis Method for G Protein Coupled Receptors and Other Large Proteins Open
NMR chemical shift changes can report on the functional dynamics of biomacromolecules in solution with sizes >1 MDa. However, their interpretation requires chemical shift assignments to individual nuclei, which for large molecules often ca…
View article: Correspondence on “Synergy and Antagonism between Allosteric and Active‐Site Inhibitors of Abl Tyrosine Kinase”**
Correspondence on “Synergy and Antagonism between Allosteric and Active‐Site Inhibitors of Abl Tyrosine Kinase”** Open
Soellner published on the interplay between allosteric and adenosine triphosphate (ATP)‐competitive inhibitors of ABL kinase, showing that the latter preferably binds to different conformational states of ABL compared to allosteric agents …
View article: A key GPCR phosphorylation motif discovered in arrestin2•CCR5 phosphopeptide complexes
A key GPCR phosphorylation motif discovered in arrestin2•CCR5 phosphopeptide complexes Open
Summary The two non-visual arrestin isoforms, arrestin2 and arrestin3 recognize and bind hundreds of G protein-coupled receptors (GPCRs) with different phosphorylation patterns leading to distinct functional outcomes. The impact of phospho…
View article: Filling of a water-free void explains the allosteric regulation of the β1-adrenergic receptor by cholesterol
Filling of a water-free void explains the allosteric regulation of the β1-adrenergic receptor by cholesterol Open
View article: Datasets for "Filling of a water-free void explains the allosteric regulation of the β1-adrenergic receptor by cholesterol"
Datasets for "Filling of a water-free void explains the allosteric regulation of the β1-adrenergic receptor by cholesterol" Open
Raw data for the X-ray structure determination of a xenon-derivatized isoprenaline∙β1AR crystal, the xenon atom anomalous maps, NMR spectra, and for the ITC curves presented in the manuscript "Filling of a water-free void explai…
View article: Imatinib disassembles the regulatory core of Abelson kinase by binding to its ATP site and not by binding to its myristoyl pocket
Imatinib disassembles the regulatory core of Abelson kinase by binding to its ATP site and not by binding to its myristoyl pocket Open
It was recently reported (Xie et al., 2022) that the Abelson tyrosine kinase (Abl) ATP-site inhibitor imatinib also binds to Abl's myristoyl binding pocket, which is the target of allosteric Abl inhibitors. This was based on a crystal stru…
View article: Comment on mr-2022-6
Comment on mr-2022-6 Open
Abstract. It was recently reported (Xie et al., 2022) that the Abelson tyrosine kinase (Abl) ATP-site inhibitor imatinib also binds to Abl's myristoyl binding pocket, which is the target of allosteric Abl inhibitors. This …
View article: Reply on CEC1
Reply on CEC1 Open
Abstract. It was recently reported (Xie et al., 2022) that the Abelson tyrosine kinase (Abl) ATP-site inhibitor imatinib also binds to Abl's myristoyl binding pocket, which is the target of allosteric Abl inhibitors. This …
View article: Reply on CC2
Reply on CC2 Open
Abstract. It was recently reported (Xie et al., 2022) that the Abelson tyrosine kinase (Abl) ATP-site inhibitor imatinib also binds to Abl's myristoyl binding pocket, which is the target of allosteric Abl inhibitors. This …
View article: Comment on mr-2022-6
Comment on mr-2022-6 Open
Abstract. It was recently reported (Xie et al., 2022) that the Abelson tyrosine kinase (Abl) ATP-site inhibitor imatinib also binds to Abl's myristoyl binding pocket, which is the target of allosteric Abl inhibitors. This …
View article: Imatinib disassembles the regulatory core of Abelson kinase by binding to its ATP site and not by binding to its myristoyl pocket
Imatinib disassembles the regulatory core of Abelson kinase by binding to its ATP site and not by binding to its myristoyl pocket Open
It was recently reported (Xie et al. Journal of Molecular Biology 2022, 434 (2), 167349) that the Abelson tyrosine kinase (Abl) ATP-site inhibitor imatinib also binds to Abl’s myristoyl binding pocket, which is the target of allosteric Abl…
View article: Imatinib disassembles the regulatory core of Abelson kinase by binding to its ATP site and not by binding to its myristoyl pocket
Imatinib disassembles the regulatory core of Abelson kinase by binding to its ATP site and not by binding to its myristoyl pocket Open
NMR raw 1H-15N TROSY data and processed spectra of a titration of U-15N-labeled Abl83-534 with imatinib presented in the manuscript "Imatinib disassembles the regulatory core of Abelson kinase by…