The Experts below are selected from a list of 2883 Experts worldwide ranked by ideXlab platform
Sergio M Pontejo - One of the best experts on this subject based on the ideXlab platform.
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structural and functional analysis of ccr1l1 a rodentia restricted eosinophil selective chemokine receptor homologue
Journal of Biological Chemistry, 2021Co-Authors: Jaclyn M Kline, Lauren E Heusinkveld, Eleanor Taranto, Clare B Martin, Alessandra G Tomasi, Isabel J Hsu, Kyoungin Cho, Jaspal S Khillan, Philip M Murphy, Sergio M PontejoAbstract:Mouse Ccr1l1 (Ccr1-like 1) encodes an orphan G protein-coupled receptor (GPCR) with highest homology to the inflammatory and highly promiscuous chemokine receptors Ccr1 and Ccr3 (70 and 50% amino acid identity, respectively). Ccr1l1 was first cloned in 1995, yet current knowledge of this putative chemokine receptor is limited to its gene organization and chromosomal localization. Here we report that Ccr1l1 is a Rodentia-specific gene selectively expressed in eosinophils. However, eosinophil phenotypes, development and responsiveness to chemokines were all normal in naive Ccr1l1 knockout mice. We demonstrate for the first time that recombinant Ccr1l1 is expressed on the plasma membrane of transfected cells and contains an extracellular N-terminus and an intracellular C-terminus, consistent with GPCR topology. Using receptor internalization, β-arrestin recruitment, calcium flux and chemotaxis assays, we excluded all 37 available mouse chemokines, including Ccr1 ligands, and two viral chemokines as Ccr1l1 ligands, and demonstrated that mouse Ccr1, but not Ccr1l1, exhibits constitutive signaling activity. However, sequence analysis and structural modeling revealed that Ccr1l1 is well-equipped to act as a classical signaling GPCR, with N-terminal sulfotyrosines as the only signaling and chemokine-binding determinant absent in Ccr1l1. Hereof, we show that a sulfatable N-terminal Ccr1 Y18 residue is essential for chemotaxis and calcium responses induced by Ccl3 and Ccl9/10 but substituting the corresponding Ccr1l1 F19 residue with tyrosine failed to confer responsiveness to Ccr1 ligands. Although Ccr1l1 remains an Extreme Outlier in the chemokine receptor family, our study supports it might respond to unidentified mouse chemokine ligands in eosinophil-driven immune responses.
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structural and functional analysis of ccr1l1 a rodentia restricted eosinophil selective chemokine receptor homologue
Journal of Biological Chemistry, 2021Co-Authors: Jaclyn M Kline, Lauren E Heusinkveld, Eleanor Taranto, Clare B Martin, Alessandra G Tomasi, Isabel J Hsu, Kyoungin Cho, Jaspal S Khillan, Philip M Murphy, Sergio M PontejoAbstract:Mouse Ccr1l1 (Ccr1-like 1) encodes an orphan G-protein-coupled receptor (GPCR) with the highest homology to the inflammatory and highly promiscuous chemokine receptors Ccr1 and Ccr3 (70 and 50% amino acid identity, respectively). Ccr1l1 was first cloned in 1995, yet current knowledge of this putative chemokine receptor is limited to its gene organization and chromosomal localization. Here we report that Ccr1l1 is a Rodentia-specific gene selectively expressed in eosinophils. However, eosinophil phenotypes, development, and responsiveness to chemokines were all normal in naive Ccr1l1 knockout mice. We demonstrate for the first time that recombinant Ccr1l1 is expressed on the plasma membrane of transfected cells and contains an extracellular N terminus and an intracellular C terminus, consistent with GPCR topology. Using receptor internalization, β-arrestin recruitment, calcium flux, and chemotaxis assays, we excluded all 37 available mouse chemokines, including Ccr1 ligands, and two viral chemokines as Ccr1l1 ligands, and demonstrated that mouse Ccr1, but not Ccr1l1, exhibits constitutive signaling activity. However, sequence analysis and structural modeling revealed that Ccr1l1 is well equipped to act as a classical signaling GPCR, with N-terminal sulfotyrosines as the only signaling and chemokine-binding determinant absent in Ccr1l1. Hereof, we show that a sulfatable N-terminal Ccr1 Y18 residue is essential for chemotaxis and calcium responses induced by Ccl3 and Ccl9/10, but substituting the corresponding Ccr1l1 F19 residue with tyrosine failed to confer responsiveness to Ccr1 ligands. Although Ccr1l1 remains an Extreme Outlier in the chemokine receptor family, our study supports that it might respond to unidentified mouse chemokine ligands in eosinophil-driven immune responses.
Jaclyn M Kline - One of the best experts on this subject based on the ideXlab platform.
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structural and functional analysis of ccr1l1 a rodentia restricted eosinophil selective chemokine receptor homologue
Journal of Biological Chemistry, 2021Co-Authors: Jaclyn M Kline, Lauren E Heusinkveld, Eleanor Taranto, Clare B Martin, Alessandra G Tomasi, Isabel J Hsu, Kyoungin Cho, Jaspal S Khillan, Philip M Murphy, Sergio M PontejoAbstract:Mouse Ccr1l1 (Ccr1-like 1) encodes an orphan G protein-coupled receptor (GPCR) with highest homology to the inflammatory and highly promiscuous chemokine receptors Ccr1 and Ccr3 (70 and 50% amino acid identity, respectively). Ccr1l1 was first cloned in 1995, yet current knowledge of this putative chemokine receptor is limited to its gene organization and chromosomal localization. Here we report that Ccr1l1 is a Rodentia-specific gene selectively expressed in eosinophils. However, eosinophil phenotypes, development and responsiveness to chemokines were all normal in naive Ccr1l1 knockout mice. We demonstrate for the first time that recombinant Ccr1l1 is expressed on the plasma membrane of transfected cells and contains an extracellular N-terminus and an intracellular C-terminus, consistent with GPCR topology. Using receptor internalization, β-arrestin recruitment, calcium flux and chemotaxis assays, we excluded all 37 available mouse chemokines, including Ccr1 ligands, and two viral chemokines as Ccr1l1 ligands, and demonstrated that mouse Ccr1, but not Ccr1l1, exhibits constitutive signaling activity. However, sequence analysis and structural modeling revealed that Ccr1l1 is well-equipped to act as a classical signaling GPCR, with N-terminal sulfotyrosines as the only signaling and chemokine-binding determinant absent in Ccr1l1. Hereof, we show that a sulfatable N-terminal Ccr1 Y18 residue is essential for chemotaxis and calcium responses induced by Ccl3 and Ccl9/10 but substituting the corresponding Ccr1l1 F19 residue with tyrosine failed to confer responsiveness to Ccr1 ligands. Although Ccr1l1 remains an Extreme Outlier in the chemokine receptor family, our study supports it might respond to unidentified mouse chemokine ligands in eosinophil-driven immune responses.
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structural and functional analysis of ccr1l1 a rodentia restricted eosinophil selective chemokine receptor homologue
Journal of Biological Chemistry, 2021Co-Authors: Jaclyn M Kline, Lauren E Heusinkveld, Eleanor Taranto, Clare B Martin, Alessandra G Tomasi, Isabel J Hsu, Kyoungin Cho, Jaspal S Khillan, Philip M Murphy, Sergio M PontejoAbstract:Mouse Ccr1l1 (Ccr1-like 1) encodes an orphan G-protein-coupled receptor (GPCR) with the highest homology to the inflammatory and highly promiscuous chemokine receptors Ccr1 and Ccr3 (70 and 50% amino acid identity, respectively). Ccr1l1 was first cloned in 1995, yet current knowledge of this putative chemokine receptor is limited to its gene organization and chromosomal localization. Here we report that Ccr1l1 is a Rodentia-specific gene selectively expressed in eosinophils. However, eosinophil phenotypes, development, and responsiveness to chemokines were all normal in naive Ccr1l1 knockout mice. We demonstrate for the first time that recombinant Ccr1l1 is expressed on the plasma membrane of transfected cells and contains an extracellular N terminus and an intracellular C terminus, consistent with GPCR topology. Using receptor internalization, β-arrestin recruitment, calcium flux, and chemotaxis assays, we excluded all 37 available mouse chemokines, including Ccr1 ligands, and two viral chemokines as Ccr1l1 ligands, and demonstrated that mouse Ccr1, but not Ccr1l1, exhibits constitutive signaling activity. However, sequence analysis and structural modeling revealed that Ccr1l1 is well equipped to act as a classical signaling GPCR, with N-terminal sulfotyrosines as the only signaling and chemokine-binding determinant absent in Ccr1l1. Hereof, we show that a sulfatable N-terminal Ccr1 Y18 residue is essential for chemotaxis and calcium responses induced by Ccl3 and Ccl9/10, but substituting the corresponding Ccr1l1 F19 residue with tyrosine failed to confer responsiveness to Ccr1 ligands. Although Ccr1l1 remains an Extreme Outlier in the chemokine receptor family, our study supports that it might respond to unidentified mouse chemokine ligands in eosinophil-driven immune responses.
Luca Carlone - One of the best experts on this subject based on the ideXlab platform.
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TEASER: Fast and Certifiable Point Cloud Registration
IEEE Transactions on Robotics, 2021Co-Authors: Heng Yang, Jingnan Shi, Luca CarloneAbstract:We propose the first fast and certifiable algorithm for the registration of two sets of three-dimensional (3-D) points in the presence of large amounts of Outlier correspondences. A certifiable algorithm is one that attempts to solve an intractable optimization problem (e.g., robust estimation with Outliers) and provides readily checkable conditions to verify if the returned solution is optimal (e.g., if the algorithm produced the most accurate estimate in the face of Outliers) or bound its suboptimality or accuracy. Toward this goal, we first reformulate the registration problem using a truncated least squares (TLS) cost that makes the estimation insensitive to a large fraction of spurious correspondences. Then, we provide a general graph-theoretic framework to decouple scale, rotation, and translation estimation, which allows solving in cascade for the three transformations. Despite the fact that each subproblem (scale, rotation, and translation estimation) is still nonconvex and combinatorial in nature, we show that 1) TLS scale and (component-wise) translation estimation can be solved in polynomial time via an adaptive voting scheme, 2) TLS rotation estimation can be relaxed to a semidefinite program (SDP) and the relaxation is tight, even in the presence of Extreme Outlier rates, and 3) the graph-theoretic framework allows drastic pruning of Outliers by finding the maximum clique. We name the resulting algorithm TEASER ( Truncated least squares Estimation And SEmidefinite Relaxation ). While solving large SDP relaxations is typically slow, we develop a second fast and certifiable algorithm, named TEASER++, that uses graduated nonconvexity to solve the rotation subproblem and leverages Douglas-Rachford Splitting to efficiently certify global optimality. For both algorithms, we provide theoretical bounds on the estimation errors, which are the first of their kind for robust registration problems. Moreover, we test their performance on standard benchmarks, object detection datasets, and the 3DMatch scan matching dataset, and show that 1) both algorithms dominate the state-of-the-art (e.g., RANSAC, branch-&-bound, heuristics) and are robust to more than $\text{99}\%$ Outliers when the scale is known, 2) TEASER++ can run in milliseconds and it is currently the fastest robust registration algorithm, and 3) TEASER++ is so robust it can also solve problems without correspondences (e.g., hypothesizing all-to-all correspondences), where it largely outperforms ICP and it is more accurate than Go-ICP while being orders of magnitude faster. We release a fast open-source C++ implementation of TEASER++.
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TEASER: Fast and Certifiable Point Cloud Registration
arXiv: Robotics, 2020Co-Authors: Heng Yang, Jingnan Shi, Luca CarloneAbstract:We propose the first fast and certifiable algorithm for the registration of two sets of 3D points in the presence of large amounts of Outlier correspondences. We first reformulate the registration problem using a Truncated Least Squares (TLS) cost that is insensitive to a large fraction of spurious correspondences. Then, we provide a general graph-theoretic framework to decouple scale, rotation, and translation estimation, which allows solving in cascade for the three transformations. Despite the fact that each subproblem is still non-convex and combinatorial in nature, we show that (i) TLS scale and (component-wise) translation estimation can be solved in polynomial time via adaptive voting, (ii) TLS rotation estimation can be relaxed to a semidefinite program (SDP) and the relaxation is tight, even in the presence of Extreme Outlier rates, and (iii) the graph-theoretic framework allows drastic pruning of Outliers by finding the maximum clique. We name the resulting algorithm TEASER (Truncated least squares Estimation And SEmidefinite Relaxation). While solving large SDP relaxations is typically slow, we develop a second fast and certifiable algorithm, named TEASER++, that uses graduated non-convexity to solve the rotation subproblem and leverages Douglas-Rachford Splitting to efficiently certify global optimality. For both algorithms, we provide theoretical bounds on the estimation errors, which are the first of their kind for robust registration problems. Moreover, we test their performance on standard, object detection, and the 3DMatch benchmarks, and show that (i) both algorithms dominate the state of the art and are robust to more than 99% Outliers, (ii) TEASER++ can run in milliseconds, and (iii) TEASER++ is so robust it can also solve problems without correspondences, where it largely outperforms ICP and it is more accurate than Go-ICP while being orders of magnitude faster.
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a polynomial time solution for robust registration with Extreme Outlier rates
arXiv: Robotics, 2019Co-Authors: Heng Yang, Luca CarloneAbstract:We propose a robust approach for the registration of two sets of 3D points in the presence of a large amount of Outliers. Our first contribution is to reformulate the registration problem using a Truncated Least Squares (TLS) cost that makes the estimation insensitive to a large fraction of spurious point-to-point correspondences. The second contribution is a general framework to decouple rotation, translation, and scale estimation, which allows solving in cascade for the three transformations. Since each subproblem (scale, rotation, and translation estimation) is still non-convex and combinatorial in nature, out third contribution is to show that (i) TLS scale and (component-wise) translation estimation can be solved exactly and in polynomial time via an adaptive voting scheme, (ii) TLS rotation estimation can be relaxed to a semidefinite program and the relaxation is tight in practice, even in the presence of an Extreme amount of Outliers. We validate the proposed algorithm, named TEASER (Truncated least squares Estimation And SEmidefinite Relaxation), in standard registration benchmarks showing that the algorithm outperforms RANSAC and robust local optimization techniques, and favorably compares with Branch-and-Bound methods, while being a polynomial-time algorithm. TEASER can tolerate up to 99% Outliers and returns highly-accurate solutions.
Clare B Martin - One of the best experts on this subject based on the ideXlab platform.
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structural and functional analysis of ccr1l1 a rodentia restricted eosinophil selective chemokine receptor homologue
Journal of Biological Chemistry, 2021Co-Authors: Jaclyn M Kline, Lauren E Heusinkveld, Eleanor Taranto, Clare B Martin, Alessandra G Tomasi, Isabel J Hsu, Kyoungin Cho, Jaspal S Khillan, Philip M Murphy, Sergio M PontejoAbstract:Mouse Ccr1l1 (Ccr1-like 1) encodes an orphan G protein-coupled receptor (GPCR) with highest homology to the inflammatory and highly promiscuous chemokine receptors Ccr1 and Ccr3 (70 and 50% amino acid identity, respectively). Ccr1l1 was first cloned in 1995, yet current knowledge of this putative chemokine receptor is limited to its gene organization and chromosomal localization. Here we report that Ccr1l1 is a Rodentia-specific gene selectively expressed in eosinophils. However, eosinophil phenotypes, development and responsiveness to chemokines were all normal in naive Ccr1l1 knockout mice. We demonstrate for the first time that recombinant Ccr1l1 is expressed on the plasma membrane of transfected cells and contains an extracellular N-terminus and an intracellular C-terminus, consistent with GPCR topology. Using receptor internalization, β-arrestin recruitment, calcium flux and chemotaxis assays, we excluded all 37 available mouse chemokines, including Ccr1 ligands, and two viral chemokines as Ccr1l1 ligands, and demonstrated that mouse Ccr1, but not Ccr1l1, exhibits constitutive signaling activity. However, sequence analysis and structural modeling revealed that Ccr1l1 is well-equipped to act as a classical signaling GPCR, with N-terminal sulfotyrosines as the only signaling and chemokine-binding determinant absent in Ccr1l1. Hereof, we show that a sulfatable N-terminal Ccr1 Y18 residue is essential for chemotaxis and calcium responses induced by Ccl3 and Ccl9/10 but substituting the corresponding Ccr1l1 F19 residue with tyrosine failed to confer responsiveness to Ccr1 ligands. Although Ccr1l1 remains an Extreme Outlier in the chemokine receptor family, our study supports it might respond to unidentified mouse chemokine ligands in eosinophil-driven immune responses.
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structural and functional analysis of ccr1l1 a rodentia restricted eosinophil selective chemokine receptor homologue
Journal of Biological Chemistry, 2021Co-Authors: Jaclyn M Kline, Lauren E Heusinkveld, Eleanor Taranto, Clare B Martin, Alessandra G Tomasi, Isabel J Hsu, Kyoungin Cho, Jaspal S Khillan, Philip M Murphy, Sergio M PontejoAbstract:Mouse Ccr1l1 (Ccr1-like 1) encodes an orphan G-protein-coupled receptor (GPCR) with the highest homology to the inflammatory and highly promiscuous chemokine receptors Ccr1 and Ccr3 (70 and 50% amino acid identity, respectively). Ccr1l1 was first cloned in 1995, yet current knowledge of this putative chemokine receptor is limited to its gene organization and chromosomal localization. Here we report that Ccr1l1 is a Rodentia-specific gene selectively expressed in eosinophils. However, eosinophil phenotypes, development, and responsiveness to chemokines were all normal in naive Ccr1l1 knockout mice. We demonstrate for the first time that recombinant Ccr1l1 is expressed on the plasma membrane of transfected cells and contains an extracellular N terminus and an intracellular C terminus, consistent with GPCR topology. Using receptor internalization, β-arrestin recruitment, calcium flux, and chemotaxis assays, we excluded all 37 available mouse chemokines, including Ccr1 ligands, and two viral chemokines as Ccr1l1 ligands, and demonstrated that mouse Ccr1, but not Ccr1l1, exhibits constitutive signaling activity. However, sequence analysis and structural modeling revealed that Ccr1l1 is well equipped to act as a classical signaling GPCR, with N-terminal sulfotyrosines as the only signaling and chemokine-binding determinant absent in Ccr1l1. Hereof, we show that a sulfatable N-terminal Ccr1 Y18 residue is essential for chemotaxis and calcium responses induced by Ccl3 and Ccl9/10, but substituting the corresponding Ccr1l1 F19 residue with tyrosine failed to confer responsiveness to Ccr1 ligands. Although Ccr1l1 remains an Extreme Outlier in the chemokine receptor family, our study supports that it might respond to unidentified mouse chemokine ligands in eosinophil-driven immune responses.
Philip M Murphy - One of the best experts on this subject based on the ideXlab platform.
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structural and functional analysis of ccr1l1 a rodentia restricted eosinophil selective chemokine receptor homologue
Journal of Biological Chemistry, 2021Co-Authors: Jaclyn M Kline, Lauren E Heusinkveld, Eleanor Taranto, Clare B Martin, Alessandra G Tomasi, Isabel J Hsu, Kyoungin Cho, Jaspal S Khillan, Philip M Murphy, Sergio M PontejoAbstract:Mouse Ccr1l1 (Ccr1-like 1) encodes an orphan G protein-coupled receptor (GPCR) with highest homology to the inflammatory and highly promiscuous chemokine receptors Ccr1 and Ccr3 (70 and 50% amino acid identity, respectively). Ccr1l1 was first cloned in 1995, yet current knowledge of this putative chemokine receptor is limited to its gene organization and chromosomal localization. Here we report that Ccr1l1 is a Rodentia-specific gene selectively expressed in eosinophils. However, eosinophil phenotypes, development and responsiveness to chemokines were all normal in naive Ccr1l1 knockout mice. We demonstrate for the first time that recombinant Ccr1l1 is expressed on the plasma membrane of transfected cells and contains an extracellular N-terminus and an intracellular C-terminus, consistent with GPCR topology. Using receptor internalization, β-arrestin recruitment, calcium flux and chemotaxis assays, we excluded all 37 available mouse chemokines, including Ccr1 ligands, and two viral chemokines as Ccr1l1 ligands, and demonstrated that mouse Ccr1, but not Ccr1l1, exhibits constitutive signaling activity. However, sequence analysis and structural modeling revealed that Ccr1l1 is well-equipped to act as a classical signaling GPCR, with N-terminal sulfotyrosines as the only signaling and chemokine-binding determinant absent in Ccr1l1. Hereof, we show that a sulfatable N-terminal Ccr1 Y18 residue is essential for chemotaxis and calcium responses induced by Ccl3 and Ccl9/10 but substituting the corresponding Ccr1l1 F19 residue with tyrosine failed to confer responsiveness to Ccr1 ligands. Although Ccr1l1 remains an Extreme Outlier in the chemokine receptor family, our study supports it might respond to unidentified mouse chemokine ligands in eosinophil-driven immune responses.
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structural and functional analysis of ccr1l1 a rodentia restricted eosinophil selective chemokine receptor homologue
Journal of Biological Chemistry, 2021Co-Authors: Jaclyn M Kline, Lauren E Heusinkveld, Eleanor Taranto, Clare B Martin, Alessandra G Tomasi, Isabel J Hsu, Kyoungin Cho, Jaspal S Khillan, Philip M Murphy, Sergio M PontejoAbstract:Mouse Ccr1l1 (Ccr1-like 1) encodes an orphan G-protein-coupled receptor (GPCR) with the highest homology to the inflammatory and highly promiscuous chemokine receptors Ccr1 and Ccr3 (70 and 50% amino acid identity, respectively). Ccr1l1 was first cloned in 1995, yet current knowledge of this putative chemokine receptor is limited to its gene organization and chromosomal localization. Here we report that Ccr1l1 is a Rodentia-specific gene selectively expressed in eosinophils. However, eosinophil phenotypes, development, and responsiveness to chemokines were all normal in naive Ccr1l1 knockout mice. We demonstrate for the first time that recombinant Ccr1l1 is expressed on the plasma membrane of transfected cells and contains an extracellular N terminus and an intracellular C terminus, consistent with GPCR topology. Using receptor internalization, β-arrestin recruitment, calcium flux, and chemotaxis assays, we excluded all 37 available mouse chemokines, including Ccr1 ligands, and two viral chemokines as Ccr1l1 ligands, and demonstrated that mouse Ccr1, but not Ccr1l1, exhibits constitutive signaling activity. However, sequence analysis and structural modeling revealed that Ccr1l1 is well equipped to act as a classical signaling GPCR, with N-terminal sulfotyrosines as the only signaling and chemokine-binding determinant absent in Ccr1l1. Hereof, we show that a sulfatable N-terminal Ccr1 Y18 residue is essential for chemotaxis and calcium responses induced by Ccl3 and Ccl9/10, but substituting the corresponding Ccr1l1 F19 residue with tyrosine failed to confer responsiveness to Ccr1 ligands. Although Ccr1l1 remains an Extreme Outlier in the chemokine receptor family, our study supports that it might respond to unidentified mouse chemokine ligands in eosinophil-driven immune responses.
