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  1. Article ; Online: Unraveling the Mechanism of Procollagen C-Proteinase Enhancer.

    Lockhart-Cairns, Michael P / Baldock, Clair

    Structure (London, England : 1993)

    2018  Volume 26, Issue 10, Page(s) 1299–1301

    Abstract: In this issue of Structure, Pulido et al. (2018) determine the crystal structure of procollagen C ...

    Abstract In this issue of Structure, Pulido et al. (2018) determine the crystal structure of procollagen C-proteinase enhancer-1 (PCPE-1)/procollagen III complex and identify that PCPE-1 unwinds the stalk of the procollagen III trimer, liberating a single chain to facilitate binding and cleavage by BMP-1 proteinases for subsequent fibrillar collagen assembly.
    MeSH term(s) Bone Morphogenetic Protein 1 ; Extracellular Matrix Proteins ; Glycoproteins ; Procollagen
    Chemical Substances Extracellular Matrix Proteins ; Glycoproteins ; Procollagen ; Bone Morphogenetic Protein 1 (EC 3.4.24.19)
    Language English
    Publishing date 2018-10-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Comment
    ZDB-ID 1213087-4
    ISSN 1878-4186 ; 0969-2126
    ISSN (online) 1878-4186
    ISSN 0969-2126
    DOI 10.1016/j.str.2018.09.003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4141: Show issues Location:
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  2. Article ; Online: The C-terminal dimerization domain of the respiratory mucin MUC5B functions in mucin stability and intracellular packaging before secretion.

    Ridley, Caroline / Lockhart-Cairns, Michael P / Collins, Richard F / Jowitt, Thomas A / Subramani, Durai B / Kesimer, Mehmet / Baldock, Clair / Thornton, David J

    The Journal of biological chemistry

    2019  Volume 294, Issue 45, Page(s) 17105–17116

    Abstract: ... about its C-terminal dimerization domain. Here, using cryogenic electron microscopy (cryo-EM) and small-angle ... our results suggest a role for the C-terminal dimerization domain of MUC5B in compaction of mucin chains ...

    Abstract Mucin 5B (MUC5B) has an essential role in mucociliary clearance that protects the pulmonary airways. Accordingly, knowledge of MUC5B structure and its interactions with itself and other proteins is critical to better understand airway mucus biology and improve the management of lung diseases such as asthma, cystic fibrosis, and chronic obstructive pulmonary disease (COPD). The role of an N-terminal multimerization domain in the supramolecular organization of MUC5B has been previously described, but less is known about its C-terminal dimerization domain. Here, using cryogenic electron microscopy (cryo-EM) and small-angle X-ray scattering (SAXS) analyses of recombinant disulfide-linked dimeric MUC5B dimerization domain we identified an asymmetric, elongated twisted structure, with a double globular base. We found that the dimerization domain is more resistant to disruption than the multimerization domain suggesting the twisted structure of the dimerization domain confers additional stability to MUC5B polymers. Size-exclusion chromatography-multiangle light scattering (SEC-MALS), SPR-based biophysical analyses and microscale thermophoresis of the dimerization domain disclosed no further assembly, but did reveal reversible, calcium-dependent interactions between the dimerization and multimerization domains that were most active at acidic pH, suggesting that these domains have a role in MUC5B intragranular organization. In summary, our results suggest a role for the C-terminal dimerization domain of MUC5B in compaction of mucin chains during granular packaging via interactions with the N-terminal multimerization domain. Our findings further suggest that the less stable multimerization domain provides a potential target for mucin depolymerization to remove mucus plugs in COPD and other lung pathologies.
    MeSH term(s) HEK293 Cells ; Humans ; Hydrogen-Ion Concentration ; Intracellular Space/metabolism ; Models, Molecular ; Mucin-5B/chemistry ; Mucin-5B/metabolism ; Protein Domains ; Protein Multimerization ; Protein Stability ; Protein Structure, Quaternary
    Chemical Substances Mucin-5B
    Language English
    Publishing date 2019-09-30
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.RA119.010771
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    In stock of ZB MED Cologne/Königswinter

    Uc I Zs.108: Show issues Location:
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  3. Article ; Online: Fibroblasts Promote Inflammation and Pain via IL-1α Induction of the Monocyte Chemoattractant Chemokine (C-C Motif) Ligand 2.

    Paish, Hannah L / Kalson, Nicholas S / Smith, Graham R / Del Carpio Pons, Alicia / Baldock, Thomas E / Smith, Nicholas / Swist-Szulik, Katarzyna / Weir, David J / Bardgett, Michelle / Deehan, David J / Mann, Derek A / Borthwick, Lee A

    The American journal of pathology

    2017  Volume 188, Issue 3, Page(s) 696–714

    Abstract: ... chemokine (C-C motif) ligand (CCL) 2, and the innate immune trigger, IL-1α. Fibroblasts isolated ...

    Abstract Fibroblasts persist within fibrotic scar tissue and exhibit considerable phenotypic and functional plasticity. Herein, we hypothesized that scar-associated fibroblasts may be a source of stress-induced inflammatory exacerbations and pain. To test this idea, we used a human model of surgery-induced fibrosis, total knee arthroplasty (TKA). Using a combination of tissue protein expression profiling and bioinformatics, we discovered that many months after TKA, the fibrotic joint exists in a state of unresolved chronic inflammation. Moreover, the infrapatellar fat pad, a soft tissue that becomes highly fibrotic in the post-TKA joint, expresses multiple inflammatory mediators, including the monocyte chemoattractant, chemokine (C-C motif) ligand (CCL) 2, and the innate immune trigger, IL-1α. Fibroblasts isolated from the post-TKA fibrotic infrapatellar fat pad express the IL-1 receptor and on exposure to IL-1α polarize to a highly inflammatory state that enables them to stimulate the recruitment of monocytes. Blockade of fibroblast CCL2 or its transcriptional regulator NF-κB prevented IL-1α-induced monocyte recruitment. Clinical investigations discovered that levels of patient-reported pain in the post-TKA joint correlated with concentrations of CCL2 in the joint tissue, such that the chemokine is effectively a pain biomarker in the TKA patient. We propose that an IL-1α-NF-κB-CCL2 signaling pathway, operating within scar-associated fibroblasts, may be therapeutically manipulated for alleviating inflammation and pain in fibrotic joints and other tissues.
    MeSH term(s) Adipose Tissue/metabolism ; Adipose Tissue/pathology ; Adult ; Aged ; Aged, 80 and over ; Arthroplasty, Replacement, Knee ; Chemokine CCL2/metabolism ; Female ; Fibroblasts/drug effects ; Fibroblasts/metabolism ; Fibroblasts/pathology ; Humans ; Inflammation/metabolism ; Interleukin-1alpha/pharmacology ; Knee Joint/metabolism ; Knee Joint/pathology ; Knee Joint/surgery ; Male ; Middle Aged ; Pain/metabolism ; Receptors, Interleukin-1/metabolism ; Synovial Membrane/metabolism ; Synovial Membrane/pathology
    Chemical Substances Chemokine CCL2 ; Interleukin-1alpha ; Receptors, Interleukin-1
    Language English
    Publishing date 2017-12-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2943-9
    ISSN 1525-2191 ; 0002-9440
    ISSN (online) 1525-2191
    ISSN 0002-9440
    DOI 10.1016/j.ajpath.2017.11.007
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    Ud II Zs.76: Show issues Location:
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  4. Article ; Online: Tropoelastin bridge region positions the cell-interactive C terminus and contributes to elastic fiber assembly.

    Yeo, Giselle C / Baldock, Clair / Tuukkanen, Anne / Roessle, Manfred / Dyksterhuis, Leanne B / Wise, Steven G / Matthews, Jacqueline / Mithieux, Suzanne M / Weiss, Anthony S

    Proceedings of the National Academy of Sciences of the United States of America

    2012  Volume 109, Issue 8, Page(s) 2878–2883

    Abstract: ... region and a cell-interactive C-terminal foot region linked together by a highly exposed bridge region ... revealed greater conformational flexibility around the bridge and C-terminal regions. This increased ...

    Abstract The tropoelastin monomer undergoes stages of association by coacervation, deposition onto microfibrils, and cross-linking to form elastic fibers. Tropoelastin consists of an elastic N-terminal coil region and a cell-interactive C-terminal foot region linked together by a highly exposed bridge region. The bridge region is conveniently positioned to modulate elastic fiber assembly through association by coacervation and its proximity to dominant cross-linking domains. Tropoelastin constructs that either modify or remove the entire bridge and downstream regions were assessed for elastogenesis. These constructs focused on a single alanine substitution (R515A) and a truncation (M155n) at the highly conserved arginine 515 site that borders the bridge. Each form displayed less efficient coacervation, impaired hydrogel formation, and decreased dermal fibroblast attachment compared to wild-type tropoelastin. The R515A mutant protein additionally showed reduced elastic fiber formation upon addition to human retinal pigmented epithelium cells and dermal fibroblasts. The small-angle X-ray scattering nanostructure of the R515A mutant protein revealed greater conformational flexibility around the bridge and C-terminal regions. This increased flexibility of the R515A mutant suggests that the tropoelastin R515 residue stabilizes the structure of the bridge region, which is critical for elastic fiber assembly.
    MeSH term(s) Cell Adhesion ; Cell Communication ; Cells, Cultured ; Elastic Tissue/chemistry ; Elastic Tissue/metabolism ; Elastic Tissue/ultrastructure ; Fibroblasts/metabolism ; Fibroblasts/pathology ; Humans ; Hydrogels ; Microscopy, Confocal ; Models, Molecular ; Mutant Proteins/chemistry ; Mutant Proteins/metabolism ; Particle Size ; Protein Structure, Tertiary ; Proteolysis ; Solutions ; Structure-Activity Relationship ; Temperature ; Tropoelastin/chemistry ; Tropoelastin/metabolism ; Tropoelastin/ultrastructure
    Chemical Substances Hydrogels ; Mutant Proteins ; Solutions ; Tropoelastin
    Language English
    Publishing date 2012-02-10
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1111615108
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    Zs.A 1148: Show issues Location:
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  5. Article ; Online: In Australia professional registration for qualified medical physicists should be mandated through the Australian Health Practitioner Regulation Agency (AHPRA).

    Hill, Robin / Barbagallo, Cathryn / Baldock, Clive

    Physical and engineering sciences in medicine

    2024  

    Language English
    Publishing date 2024-01-02
    Publishing country Switzerland
    Document type Editorial
    ISSN 2662-4737
    ISSN (online) 2662-4737
    DOI 10.1007/s13246-023-01376-8
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  6. Article: Tropoelastin bridge region positions the cell-interactive C terminus and contributes to elastic fiber assembly

    Yeo, Giselle C / Baldock, Clair / Tuukkanen, Anne / Roessle, Manfred / Dyksterhuis, Leanne B / Wise, Steven G / Matthews, Jacqueline / Mithieux, Suzanne M / Weiss, Anthony S

    Proceedings of the National Academy of Sciences of the United States of America. 2012 Feb. 21, v. 109, no. 8

    2012  

    Abstract: ... region and a cell-interactive C-terminal foot region linked together by a highly exposed bridge region ... revealed greater conformational flexibility around the bridge and C-terminal regions. This increased ...

    Abstract The tropoelastin monomer undergoes stages of association by coacervation, deposition onto microfibrils, and cross-linking to form elastic fibers. Tropoelastin consists of an elastic N-terminal coil region and a cell-interactive C-terminal foot region linked together by a highly exposed bridge region. The bridge region is conveniently positioned to modulate elastic fiber assembly through association by coacervation and its proximity to dominant cross-linking domains. Tropoelastin constructs that either modify or remove the entire bridge and downstream regions were assessed for elastogenesis. These constructs focused on a single alanine substitution (R515A) and a truncation (M155n) at the highly conserved arginine 515 site that borders the bridge. Each form displayed less efficient coacervation, impaired hydrogel formation, and decreased dermal fibroblast attachment compared to wild-type tropoelastin. The R515A mutant protein additionally showed reduced elastic fiber formation upon addition to human retinal pigmented epithelium cells and dermal fibroblasts. The small-angle X-ray scattering nanostructure of the R515A mutant protein revealed greater conformational flexibility around the bridge and C-terminal regions. This increased flexibility of the R515A mutant suggests that the tropoelastin R515 residue stabilizes the structure of the bridge region, which is critical for elastic fiber assembly.
    Keywords X-radiation ; alanine ; arginine ; crosslinking ; epithelium ; fibroblasts ; humans ; hydrocolloids ; mutants ; nanomaterials
    Language English
    Dates of publication 2012-0221
    Size p. 2878-2883.
    Publishing place National Academy of Sciences
    Document type Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    Database NAL-Catalogue (AGRICOLA)

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  7. Article ; Online: Dose from imaging at the time of treatment should be reduced.

    Steiner, Elisabeth / Healy, Brendan / Baldock, Clive

    Physical and engineering sciences in medicine

    2023  Volume 46, Issue 3, Page(s) 959–962

    MeSH term(s) Radiation Dosage ; Radiotherapy Dosage ; Diagnostic Imaging
    Language English
    Publishing date 2023-07-12
    Publishing country Switzerland
    Document type Editorial
    ISSN 2662-4737
    ISSN (online) 2662-4737
    DOI 10.1007/s13246-023-01298-5
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Secreted ADAMTS-like 2 promotes myoblast differentiation by potentiating WNT signaling.

    Taye, Nandaraj / Singh, Mukti / Baldock, Clair / Hubmacher, Dirk

    Matrix biology : journal of the International Society for Matrix Biology

    2023  Volume 120, Page(s) 24–42

    Abstract: Myogenesis is the process that generates multinucleated contractile myofibers from muscle stem cells during skeletal muscle development and regeneration. Myogenesis is governed by myogenic regulatory transcription factors, including MYOD1. Here, we ... ...

    Abstract Myogenesis is the process that generates multinucleated contractile myofibers from muscle stem cells during skeletal muscle development and regeneration. Myogenesis is governed by myogenic regulatory transcription factors, including MYOD1. Here, we identified the secreted matricellular protein ADAMTS-like 2 (ADAMTSL2) as part of a Wnt-dependent positive feedback loop, which augmented or sustained MYOD1 expression and thus promoted myoblast differentiation. ADAMTSL2 depletion resulted in severe retardation of myoblast differentiation in vitro and its ablation in myogenic precursor cells resulted in aberrant skeletal muscle architecture. Mechanistically, ADAMTSL2 potentiated WNT signaling by binding to WNT ligands and WNT receptors. We identified the WNT-binding ADAMTSL2 peptide, which was sufficient to promote myogenesis in vitro. Since ADAMTSL2 was previously described as a negative regulator of TGFβ signaling in fibroblasts, ADAMTSL2 now emerges as a signaling hub that could integrate WNT, TGFβ and potentially other signaling pathways within the dynamic microenvironment of differentiating myoblasts during skeletal muscle development and regeneration.
    MeSH term(s) Cell Differentiation ; Muscle Development ; Muscle, Skeletal/metabolism ; Satellite Cells, Skeletal Muscle ; Transforming Growth Factor beta/metabolism ; Wnt Signaling Pathway ; Humans ; Mice ; Animals
    Chemical Substances Transforming Growth Factor beta ; ADAMTSL2 protein, human (EC 3.4.24.-) ; Adamtsl2 protein, mouse
    Language English
    Publishing date 2023-05-14
    Publishing country Netherlands
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 1183793-7
    ISSN 1569-1802 ; 0945-053X
    ISSN (online) 1569-1802
    ISSN 0945-053X
    DOI 10.1016/j.matbio.2023.05.003
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    Zs.A 1694: Show issues Location:
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    Jg. 1995 - 2021: Lesesall (1.OG)
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  9. Article ; Online: Gel dosimetry has a viable future for dosimetry in the radiation oncology clinic.

    Ceberg, Sofie / Olding, Tim / Baldock, Clive

    Physical and engineering sciences in medicine

    2023  Volume 47, Issue 1, Page(s) 1–5

    MeSH term(s) Radiation Oncology ; Radiometry ; Radiation Dosage
    Language English
    Publishing date 2023-12-19
    Publishing country Switzerland
    Document type Editorial
    ISSN 2662-4737
    ISSN (online) 2662-4737
    DOI 10.1007/s13246-023-01365-x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Is the PhD a qualification that is more or less standardised and accepted all over the world?

    Baldock, Clive / Chen, Honglin

    Physical and engineering sciences in medicine

    2021  Volume 44, Issue 4, Page(s) 1011–1012

    Language English
    Publishing date 2021-10-26
    Publishing country Switzerland
    Document type Editorial
    ISSN 2662-4737
    ISSN (online) 2662-4737
    DOI 10.1007/s13246-021-01069-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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