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Ed Luk - One of the best experts on this subject based on the ideXlab platform.
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Structure and interaction of Chz1-C in complex of H2A.Z-H2B.
2019Co-Authors: Yunyun Wang, Sheng Liu, Lu Sun, Shan Shan, Xiaoping Liang, Yingzi Huang, Ed LukAbstract:(A) Schematic View of aligned fungi Chz1-MC sequences. Blue and purple lines represent Chz1-M and Chz1-C. Black lines: CHZ motifs. The conserved Phe/Tyr residues are highlighted by star. (B) The overall structure of Chz1-C in complex with yeast H2A.Z-H2B. Magenta, Chz1-C; yellow, H2A.Z; red, H2B. (C) Close View of the interaction between Chz1 residue F151 and H2B pocket formed by the H2B α1 helix, L1 loop, and α2 helix (top panel) and interaction between Chz1-C polar residues and H2A.Z L2 loop and H2B L1 loop (lower panel). (D) Comparison of DEF/Y motif adopted by different histone chaperones. (Top) Aligned DEF/Y motif sequences with known structures. The Phe/Tyr residues are highlighted by star. (Bottom) Structural comparison of histone H2B pockets interacting with DEF/Y motifs from human YL1 (cyan), Anp32e (blue), Swr1 (green), Spt16 (orange). The F/Y residues corresponding to Chz1 F151, the histone H2A.Z R86 (and the H2A counterparts) serving as the arginine finger are highlighted in the structures. (E) Effect of Chz1 mutations on H2A.Z-H2B interaction revealed by CSP analysis. The 1H-15N HSQC spectrum of 15N labeled scZB in complex with Chz1-MC and mutated Chz1-MC (Mut1, Mut2, Mut3, Mut4) or Chz1-M are compared. The chemical shift of H2A.Z residue R86 in association with different Chz1 mutants are displayed in the same color as shown in the sequences of corresponding Chz1. The underlying data can be found in S2 Data. Anp32e, acidic leucine-rich nuclear phosphoprotein 32 family member e; CHZ, a defined Chz1 region showing sequence conservation across all species; Chz1, chaperone for H2A.Z-H2B; Chz1-C, C-terminal region of Chz1; Chz1-M, middle region of Chz1; Chz1-MC, middle and C-terminal region of Chz1; C.g., Candida glabrata; CSP, chemical shift perturbation; E.g., Eremothecium gossypii; DEF/Y, the consecutive D/E residues followed by a single aromatic residue; H.s., Homo sapiens; HSQC, heteronuclear single-quantum coherence; S.c., Saccharmyces cerevisiae; scZB, single-chain H2A.Z-H2B; S.p., Schizosaccharomyces pombe; Spt16, Suppressor of Ty 16; Swc2, SWR complex protein 2; Swr1, Swi2/snif2-related 1; YL1, Swc2 homolog in higher eukaryotes; V.p., Vanderwaltozyma polyspora.
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Identification of Chz1 regions dictates the preference for H2A.Z. (A) Schematic View of Chz1-FL according to a previous mapping result.
2019Co-Authors: Yunyun Wang, Sheng Liu, Lu Sun, Shan Shan, Xiaoping Liang, Yingzi Huang, Ed LukAbstract:Shown below the scheme include the N-terminal region (residues 1–63), middle region (residues 64–124), and C-terminal region (residues 125–153) of Chz1 termed Chz1-N, Chz1-M, and Chz1-C, respectively. (B) Effect of Chz1-MC and Chz1-M on the binding of H2A.Z-H2B dimer and H2A-H2B dimer by ITC. Histone dimers were titrated by Chz1-M (left) and Chz1-MC (right). The underlying data can be found in S1 Data. (C) Effect of Chz1-MC and Chz1-M on dictating the preference for H2A.Z. The folds of binding affinity decrease between all histone dimers (in single-chain form) and scZB are denoted as Kd/Kd (H2A.Z) and calculated for comparison. The underlying data can be found in S1 Data. (D) CSP mapping analysis of H2A.Z-H2B residues interacting with different Chz1. The 1H-15N HSQC spectrum of 15N labeled scZB in complex with Chz1-M serves as the reference spectra to monitor the CSP changes. The CSP changes are calculated as Δδ = [(Δδ1H)2 + (Δδ15N/5)2]1/2 and plotted as a function of scZB residues for comparison. From the top to bottom: CSP changes of scZB residues interacting with Chz1-FL, Chz1-MC, Chz1-NM, Chz1 F151A mutant. On the top is displayed the Schematic View of scZB and secondary structures of H2A.Z and H2B, which are colored in yellow and red, respectively. The underlying data can be found in S2 Data. Chz1, chaperone for H2A.Z-H2B; Chz1-C, C-terminal region of Chz1; Chz1-FL, full-length Chz1; Chz1-M, middle region of Chz1; Chz1-MC, middle and C-terminal region of Chz1; Chz1-N, N-terminal region of Chz1; Chz1-NM, N-terminal and middle region of Chz1; CSP, chemical shift perturbation; HSQC, heteronuclear single-quantum coherence; ITC, isothermal titration calorimetry; scAB, single-chain H2A-H2B; scZB, single-chain H2A.Z-H2B.
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H2A.Z residues with key roles for preferential recognition of Chz1.
2019Co-Authors: Yunyun Wang, Sheng Liu, Lu Sun, Shan Shan, Xiaoping Liang, Yingzi Huang, Ed LukAbstract:(A) Schematic View of aligned H2A.Z and H2A. Shown on the top is a Schematic View of the secondary structure of both histones. H2A.Z-specific residues and their H2A counterparts are colored in red. Residues interchanged for ITC analysis are highlighted with dots or triangles. Black dots highlight H2A.Z residues playing central roles in preferential recognition of Chz1. (B) Structural model of Chz1 in complex with H2A.Z-H2B. Structure of Chz1-C complex is superimposed with the structure of Chz1-M complex (PDB 2JSS). The dotted line stands for Chz1 residues 125–141, which are not visible in both structures. Blue: Chz1-M; magenta: Chz1-C; red: H2B; yellow: H2A.Z. (C) Close View of the binding interface between H2A.Z α2-helix and Chz1 αN-helix. H2A.Z residue A57 and its H2A counterpart P50 are colored in yellow and gray. H2A-H2B structure from nucleosome (PDB: 1ID3) is superimposed for comparison. (D) Close View of the binding interface between H2A.Z α3-helix and Chz1 αC-helix. H2A.Z residue G98 and its H2A counterpart N91 are colored in yellow and gray. H2A-H2B structure from nucleosome (PDB: 1ID3) is superimposed for comparison. (E) Effect of H2A.Z-H2A and H2A-H2A.Z interchanges on Chz1 recognition by ITC analysis. The underlying data can be found in S1 Data. (F) ITC analysis showing the effect of H2A.Z mutant A57G/G98N and H2A residues P50G/N91G on recognition of H2A.Z-chaperone Swc2. The underlying data can be found in S1 Data. A.t., Arabidopsis thaliana; Chz1, chaperone for H2A.Z-H2B; Chz1-C, C-terminal region of Chz1; Chz1-M, middle region of Chz1; H.s., Homo sapiens; ITC, isothermal titration calorimetry; M.m., Mus musculus; PDB, protein data bank; S.c., Saccharmyces cerevisiae; Swc2, SWR complex protein 2.
Mateusz Koziej - One of the best experts on this subject based on the ideXlab platform.
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Schematic View of the external carotid artery tree with marked measurements points.
2019Co-Authors: Mateusz Koziej, Jakub Polak, Jakub Wnuk, Marek Trybus, Jerzy Walocha, Anna Chrapusta, Paweł Zegowy, Ewa Mizia, Tadeusz Popiela, Mateusz HołdaAbstract:A—the length of transverse facial artery (TFA), measured on its course; B—distance between the TFA origin and bifurcation of common carotid artery; C—distance between the TFA origin and bifurcation of external carotid artery; D—distance between the TFA origin and superficial temporal artery bifurcation; E—distance between the TFA origin and lower border of the zygomatic arch.
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Schematic View of the interatrial septum in the ovine heart.
2018Co-Authors: Mateusz K. Hołda, Marek Trybus, Agnieszka Pietsch-fulbiszewska, Mateusz KoziejAbstract:[A] Patent foramen ovale (PFO) channel connecting both atria. [B] Right septal pouch (RSP)–diverticulum located on the right side of the interatrial septum, without connection between both atria across the septum (fusion limited to the superior portion zone of overlap). [C] Left septal pouch (LSP)–diverticulum located on the left side of the interatrial septum, without connection between both atria across the septum (fusion limited to the inferior portion of the zone of overlap). [D] Left septal ridge (LSR)–tissue fold on the left side of the interatrial septum in the location in which the LSP would be expected. [E] Left septal bridge (LSB)–tissue bridge located on the left side of the interatrial septum in the location in which the LSP would be expected. [F] Smooth septum—fusion between the septum primum and secundum occurs along the entire zone of overlap. LA–left atrium, RA–right atrium.
Sahel Rahimi - One of the best experts on this subject based on the ideXlab platform.
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Additional file 1 of Optimization of expression, purification and secretion of functional recombinant human growth hormone in Escherichia coli using modified staphylococcal protein a signal peptide
2021Co-Authors: Garshasb Rigi, Amin Rostami, Habib Ghomi, Gholamreza Ahmadian, Vasiqe Sadat Mirbagheri, Meisam Jeiranikhameneh, Majid Vahed, Sahel RahimiAbstract:Additional file 1. The Schematic View of the pET26 plasmid as well as the designed gene structure
Yunyun Wang - One of the best experts on this subject based on the ideXlab platform.
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Structure and interaction of Chz1-C in complex of H2A.Z-H2B.
2019Co-Authors: Yunyun Wang, Sheng Liu, Lu Sun, Shan Shan, Xiaoping Liang, Yingzi Huang, Ed LukAbstract:(A) Schematic View of aligned fungi Chz1-MC sequences. Blue and purple lines represent Chz1-M and Chz1-C. Black lines: CHZ motifs. The conserved Phe/Tyr residues are highlighted by star. (B) The overall structure of Chz1-C in complex with yeast H2A.Z-H2B. Magenta, Chz1-C; yellow, H2A.Z; red, H2B. (C) Close View of the interaction between Chz1 residue F151 and H2B pocket formed by the H2B α1 helix, L1 loop, and α2 helix (top panel) and interaction between Chz1-C polar residues and H2A.Z L2 loop and H2B L1 loop (lower panel). (D) Comparison of DEF/Y motif adopted by different histone chaperones. (Top) Aligned DEF/Y motif sequences with known structures. The Phe/Tyr residues are highlighted by star. (Bottom) Structural comparison of histone H2B pockets interacting with DEF/Y motifs from human YL1 (cyan), Anp32e (blue), Swr1 (green), Spt16 (orange). The F/Y residues corresponding to Chz1 F151, the histone H2A.Z R86 (and the H2A counterparts) serving as the arginine finger are highlighted in the structures. (E) Effect of Chz1 mutations on H2A.Z-H2B interaction revealed by CSP analysis. The 1H-15N HSQC spectrum of 15N labeled scZB in complex with Chz1-MC and mutated Chz1-MC (Mut1, Mut2, Mut3, Mut4) or Chz1-M are compared. The chemical shift of H2A.Z residue R86 in association with different Chz1 mutants are displayed in the same color as shown in the sequences of corresponding Chz1. The underlying data can be found in S2 Data. Anp32e, acidic leucine-rich nuclear phosphoprotein 32 family member e; CHZ, a defined Chz1 region showing sequence conservation across all species; Chz1, chaperone for H2A.Z-H2B; Chz1-C, C-terminal region of Chz1; Chz1-M, middle region of Chz1; Chz1-MC, middle and C-terminal region of Chz1; C.g., Candida glabrata; CSP, chemical shift perturbation; E.g., Eremothecium gossypii; DEF/Y, the consecutive D/E residues followed by a single aromatic residue; H.s., Homo sapiens; HSQC, heteronuclear single-quantum coherence; S.c., Saccharmyces cerevisiae; scZB, single-chain H2A.Z-H2B; S.p., Schizosaccharomyces pombe; Spt16, Suppressor of Ty 16; Swc2, SWR complex protein 2; Swr1, Swi2/snif2-related 1; YL1, Swc2 homolog in higher eukaryotes; V.p., Vanderwaltozyma polyspora.
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Identification of Chz1 regions dictates the preference for H2A.Z. (A) Schematic View of Chz1-FL according to a previous mapping result.
2019Co-Authors: Yunyun Wang, Sheng Liu, Lu Sun, Shan Shan, Xiaoping Liang, Yingzi Huang, Ed LukAbstract:Shown below the scheme include the N-terminal region (residues 1–63), middle region (residues 64–124), and C-terminal region (residues 125–153) of Chz1 termed Chz1-N, Chz1-M, and Chz1-C, respectively. (B) Effect of Chz1-MC and Chz1-M on the binding of H2A.Z-H2B dimer and H2A-H2B dimer by ITC. Histone dimers were titrated by Chz1-M (left) and Chz1-MC (right). The underlying data can be found in S1 Data. (C) Effect of Chz1-MC and Chz1-M on dictating the preference for H2A.Z. The folds of binding affinity decrease between all histone dimers (in single-chain form) and scZB are denoted as Kd/Kd (H2A.Z) and calculated for comparison. The underlying data can be found in S1 Data. (D) CSP mapping analysis of H2A.Z-H2B residues interacting with different Chz1. The 1H-15N HSQC spectrum of 15N labeled scZB in complex with Chz1-M serves as the reference spectra to monitor the CSP changes. The CSP changes are calculated as Δδ = [(Δδ1H)2 + (Δδ15N/5)2]1/2 and plotted as a function of scZB residues for comparison. From the top to bottom: CSP changes of scZB residues interacting with Chz1-FL, Chz1-MC, Chz1-NM, Chz1 F151A mutant. On the top is displayed the Schematic View of scZB and secondary structures of H2A.Z and H2B, which are colored in yellow and red, respectively. The underlying data can be found in S2 Data. Chz1, chaperone for H2A.Z-H2B; Chz1-C, C-terminal region of Chz1; Chz1-FL, full-length Chz1; Chz1-M, middle region of Chz1; Chz1-MC, middle and C-terminal region of Chz1; Chz1-N, N-terminal region of Chz1; Chz1-NM, N-terminal and middle region of Chz1; CSP, chemical shift perturbation; HSQC, heteronuclear single-quantum coherence; ITC, isothermal titration calorimetry; scAB, single-chain H2A-H2B; scZB, single-chain H2A.Z-H2B.
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H2A.Z residues with key roles for preferential recognition of Chz1.
2019Co-Authors: Yunyun Wang, Sheng Liu, Lu Sun, Shan Shan, Xiaoping Liang, Yingzi Huang, Ed LukAbstract:(A) Schematic View of aligned H2A.Z and H2A. Shown on the top is a Schematic View of the secondary structure of both histones. H2A.Z-specific residues and their H2A counterparts are colored in red. Residues interchanged for ITC analysis are highlighted with dots or triangles. Black dots highlight H2A.Z residues playing central roles in preferential recognition of Chz1. (B) Structural model of Chz1 in complex with H2A.Z-H2B. Structure of Chz1-C complex is superimposed with the structure of Chz1-M complex (PDB 2JSS). The dotted line stands for Chz1 residues 125–141, which are not visible in both structures. Blue: Chz1-M; magenta: Chz1-C; red: H2B; yellow: H2A.Z. (C) Close View of the binding interface between H2A.Z α2-helix and Chz1 αN-helix. H2A.Z residue A57 and its H2A counterpart P50 are colored in yellow and gray. H2A-H2B structure from nucleosome (PDB: 1ID3) is superimposed for comparison. (D) Close View of the binding interface between H2A.Z α3-helix and Chz1 αC-helix. H2A.Z residue G98 and its H2A counterpart N91 are colored in yellow and gray. H2A-H2B structure from nucleosome (PDB: 1ID3) is superimposed for comparison. (E) Effect of H2A.Z-H2A and H2A-H2A.Z interchanges on Chz1 recognition by ITC analysis. The underlying data can be found in S1 Data. (F) ITC analysis showing the effect of H2A.Z mutant A57G/G98N and H2A residues P50G/N91G on recognition of H2A.Z-chaperone Swc2. The underlying data can be found in S1 Data. A.t., Arabidopsis thaliana; Chz1, chaperone for H2A.Z-H2B; Chz1-C, C-terminal region of Chz1; Chz1-M, middle region of Chz1; H.s., Homo sapiens; ITC, isothermal titration calorimetry; M.m., Mus musculus; PDB, protein data bank; S.c., Saccharmyces cerevisiae; Swc2, SWR complex protein 2.
Joep Cornelissen - One of the best experts on this subject based on the ideXlab platform.
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metaphor and the dynamics of knowledge in organization theory a case study of the organizational identity metaphor
Journal of Management Studies, 2006Co-Authors: Joep CornelissenAbstract:Despite the increased salience of metaphor in organization theory, there is still very little conceptual machinery for capturing and explaining how metaphor creates and/or reorders knowledge within organization theory. Moreover, prior work on metaphor has insufficiently accounted for the context of interpreting a metaphor. Many metaphors in organization theory, including the 'organizational identity' metaphor, have often been treated in singular and monolithic terms; seen to offer a similar or largely synonymous interpretation to theorists and researchers working along the entire spectrum of disciplines (e.g. organizational behaviour, organizational psychology) in organization theory. We argue in this paper that contextual variation however exists in the interpretation of metaphors in organization theory. This argument is developed by proposing and elaborating on a so-called image-Schematic model of metaphor, which suggests that the image-schemata (abstract imaginative structures) that are triggered by the metaphorical comparison of concepts may vary among individuals. Accordingly, once different schemata are triggered the completion and interpretation of a metaphor may equally vary among different individuals or, indeed, research communities. These points associated with the image-Schematic model of metaphor are illustrated with a case study of the 'organizational identity' metaphor. The case study shows that this particular metaphor has spiralled out into different research communities and has been comprehended in very different ways as different communities work from very different conceptions, or image-schemata, of 'organization' and 'identity', and use different theoretical frameworks and constructs as a result. The implications of the image-Schematic View of metaphor for knowledge development and theoretical progress in organization theory are discussed. Copyright Blackwell Publishing Ltd 2006.
