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  1. Article: Dental research--our unique contribution to medical science.

    Embery, G

    Journal of dental research

    2000  Volume 80, Issue 8, Page(s) 1688–1689

    MeSH term(s) Biocompatible Materials ; Biotechnology ; Dental Research ; Forecasting ; Genetics ; Humans ; Medicine ; Science
    Chemical Substances Biocompatible Materials
    Language English
    Publishing date 2000-11-06
    Publishing country United States
    Document type Address
    ZDB-ID 80207-4
    ISSN 1544-0591 ; 0022-0345
    ISSN (online) 1544-0591
    ISSN 0022-0345
    DOI 10.1177/00220345010800080101
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article: An update on the biochemistry of the periodontal ligament.

    Embery, G

    European journal of orthodontics

    1990  Volume 12, Issue 1, Page(s) 77–80

    MeSH term(s) Humans ; Periodontal Ligament/metabolism
    Language English
    Publishing date 1990-02
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 423731-6
    ISSN 1460-2210 ; 0141-5387
    ISSN (online) 1460-2210
    ISSN 0141-5387
    DOI 10.1093/ejo/12.1.77
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Proteoglycans and orthodontic tooth movement.

    Waddington, R J / Embery, G

    Journal of orthodontics

    2001  Volume 28, Issue 4, Page(s) 281–290

    Abstract: Proteoglycans represent an important and diverse family of extracellular matrix components within the connective tissues of the periodontium. This review focuses on the function and metabolism of the various proteoglycans in periodontal tissues, such as ... ...

    Abstract Proteoglycans represent an important and diverse family of extracellular matrix components within the connective tissues of the periodontium. This review focuses on the function and metabolism of the various proteoglycans in periodontal tissues, such as alveolar bone and periodontal ligament, and considers their potential fate in response to an orthodontic force. Such considerations provide an important background in evaluating the potential for proteoglycan metabolites, alongside other connective tissue metabolites, as biomarkers for assessing the deep-seated metabolic changes and as a diagnostic tool in monitoring orthodontic tooth movement.
    MeSH term(s) Animals ; Biomarkers ; Bone Remodeling ; Dental Stress Analysis ; Extracellular Matrix/chemistry ; Extracellular Matrix/metabolism ; Gingival Crevicular Fluid/chemistry ; Gingival Crevicular Fluid/metabolism ; Glycosaminoglycans/metabolism ; Humans ; Matrix Metalloproteinases/metabolism ; Outcome Assessment (Health Care)/methods ; Periodontal Ligament/metabolism ; Periodontium/metabolism ; Proteoglycans/metabolism ; Tooth Movement Techniques
    Chemical Substances Biomarkers ; Glycosaminoglycans ; Proteoglycans ; Matrix Metalloproteinases (EC 3.4.24.-)
    Language English
    Publishing date 2001-12
    Publishing country England
    Document type Journal Article ; Review
    ZDB-ID 2011954-9
    ISSN 1465-3125 ; 0301-228X
    ISSN 1465-3125 ; 0301-228X
    DOI 10.1093/ortho/28.4.281
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: The use of immunohistochemistry in understanding the structure and function of the extracellular matrix of dental tissues.

    Hall, R C / Embery, G

    Advances in dental research

    1997  Volume 11, Issue 4, Page(s) 478–486

    Abstract: The availability of monoclonal and polyclonal antibodies directed toward the recognition of epitopes in a variety of extracellular matrix components of the dentition represents a powerful tool in the investigation of the structure and biology of dental ... ...

    Abstract The availability of monoclonal and polyclonal antibodies directed toward the recognition of epitopes in a variety of extracellular matrix components of the dentition represents a powerful tool in the investigation of the structure and biology of dental tissues in health and disease. The immunolocalization of both whole molecule structures and specific regions of molecules has the potential to yield information on tooth development, the effects of aging, changes in tooth structure during the initiation and progression of the caries process, together with the response of the tooth to restorative treatment. This review reports on current research to elucidate the role of extracellular matrices of enamel, dentin, cementum, and bone. Attention is directed at the use of antibodies toward the small leucine-rich proteoglycans such as decorin and biglycan, in addition to their glycosaminoglycan chains. Antibodies are also being developed toward dental tissue-specific macromolecules such as phosphophoryn and amelogenin; the use of these antibodies will increase our understanding of the role of these macromolecules in mineralized tissues.
    MeSH term(s) Animals ; Bone and Bones/metabolism ; Dental Caries/metabolism ; Extracellular Matrix/metabolism ; Glycosaminoglycans/metabolism ; Humans ; Immunohistochemistry ; Proteoglycans/metabolism ; Tooth/metabolism
    Chemical Substances Glycosaminoglycans ; Proteoglycans
    Language English
    Publishing date 1997-11
    Publishing country United States
    Document type Journal Article ; Review
    ZDB-ID 639406-1
    ISSN 1544-0737 ; 0895-9374
    ISSN (online) 1544-0737
    ISSN 0895-9374
    DOI 10.1177/08959374970110041601
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: A sulphated glycopeptide in human supragingival calculus extracts.

    Embery, G

    Calcified tissue research

    1977  Volume 23, Issue 1, Page(s) 13–17

    Abstract: A method is described for the isolation and purification of a sulphated glycopeptide from human supragingival calculus. The compound was isolated after using EDTA treatment, 2 M CaCl2 extraction, proteolytic digestion, ethanol precipitation, and finally ... ...

    Abstract A method is described for the isolation and purification of a sulphated glycopeptide from human supragingival calculus. The compound was isolated after using EDTA treatment, 2 M CaCl2 extraction, proteolytic digestion, ethanol precipitation, and finally purified by DEAE cellulose chromatography. It migrated as a single component of cellulose acetate electrophoresis, and chemical and infrared spectral analysis showed the presence of covalently attached sulphate groups. The sulphated glycopeptide was distinguished from being a sulphated glycosaminoglycan.
    MeSH term(s) Calcium Chloride ; Chromatography, DEAE-Cellulose ; Dental Calculus/analysis ; Edetic Acid ; Electrophoresis ; Glycopeptides/isolation & purification ; Humans ; Methods ; Spectrophotometry, Infrared ; Sulfates
    Chemical Substances Glycopeptides ; Sulfates ; Edetic Acid (9G34HU7RV0) ; Calcium Chloride (M4I0D6VV5M)
    Language English
    Publishing date 1977-05-31
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 1413-8
    ISSN 0008-0594 ; 0944-081X
    ISSN 0008-0594 ; 0944-081X
    DOI 10.1007/bf02012761
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: Adsorption of bovine serum albumin on to titanium powder.

    Wassell, D T / Embery, G

    Biomaterials

    1996  Volume 17, Issue 9, Page(s) 859–864

    Abstract: The adsorption of bovine serum albumin (BSA) on to titanium powder has been studied as a function of protein concentration and pH, and in the presence of calcium and phosphate ions. Isotherm data have shown that the adsorption process does not follow the ...

    Abstract The adsorption of bovine serum albumin (BSA) on to titanium powder has been studied as a function of protein concentration and pH, and in the presence of calcium and phosphate ions. Isotherm data have shown that the adsorption process does not follow the Langmuir model (inflection points). The maximum adsorption (Admax) at pH 6.8 is 1.13 +/- 0.21 mg m-2. For the pH dependence of adsorption the amount adsorbed increases with decreasing pH (at pH 5.15 Admax = 1.31 +/- 0.2 mg m-2), indicating that hydration effects are important. Adsorption increases and decreases in the presence of calcium (at pH 6.8 for 0.002 M Admax = 1.73 +/- 0.23 mg m-2) and phosphate (at pH 6.8 for 0.002 M Admax = 0.64 +/- 0.14 mgm-2)ions, respectively, indicating that electrostatic effects are important. The time dependence, isotherm and desorption data provide indirect evidence of possible conformational changes in the BSA molecule.
    MeSH term(s) Adsorption ; Animals ; Biocompatible Materials ; Calcium ; Calcium Phosphates ; Cattle ; Hydrogen-Ion Concentration ; In Vitro Techniques ; Materials Testing ; Osmolar Concentration ; Phosphates ; Powders ; Serum Albumin, Bovine ; Sodium Acetate ; Surface Properties ; Time Factors ; Titanium
    Chemical Substances Biocompatible Materials ; Calcium Phosphates ; Phosphates ; Powders ; alpha-tricalcium phosphate ; tetracalcium phosphate ; Serum Albumin, Bovine (27432CM55Q) ; Sodium Acetate (4550K0SC9B) ; calcium phosphate, monobasic, anhydrous (701EKV9RMN) ; calcium phosphate (97Z1WI3NDX) ; Titanium (D1JT611TNE) ; calcium phosphate, dibasic, anhydrous (L11K75P92J) ; sodium phosphate (SE337SVY37) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 1996-05
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 603079-8
    ISSN 0142-9612
    ISSN 0142-9612
    DOI 10.1016/0142-9612(96)83280-7
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  7. Article: Glycosaminoglycans of human dental pulp.

    Embery, G

    Journal de biologie buccale

    1976  Volume 4, Issue 3, Page(s) 229–236

    Abstract: Dental pulps were obtained from sound human permanent molars and premolars. The pulps were treated to remove lipid, protein and nucleic acid and glycosaminoglycans were finally isolated by ethanol precipitation. Electrophoretic examination and CPC- ... ...

    Abstract Dental pulps were obtained from sound human permanent molars and premolars. The pulps were treated to remove lipid, protein and nucleic acid and glycosaminoglycans were finally isolated by ethanol precipitation. Electrophoretic examination and CPC-cellulose profiles revealed the presence of hyaluronic acid, dermatan sulphate, chondroitin 4 sulphate and chondroitin 6 sulphate. Hyaluronic acid accounted for only a low percentage of the total glycosaminoglycan content while dermatan sulphate was present in unusually high amounts. Chondroitin 4 and 6 sulphates represented the major glycosaminoglycan fraction.
    MeSH term(s) Chondroitin Sulfates/analysis ; Dental Pulp/analysis ; Dermatan Sulfate/analysis ; Glycosaminoglycans/analysis ; Humans ; Hyaluronic Acid/analysis
    Chemical Substances Glycosaminoglycans ; Dermatan Sulfate (24967-94-0) ; Hyaluronic Acid (9004-61-9) ; Chondroitin Sulfates (9007-28-7)
    Language English
    Publishing date 1976-09
    Publishing country France
    Document type Comparative Study ; Journal Article
    ZDB-ID 189155-8
    ISSN 0301-3952
    ISSN 0301-3952
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  8. Article: Interaction of glucuronic acid and iduronic acid-rich glycosaminoglycans and their modified forms with hydroxyapatite.

    Rees, Sarah G / Hughes, WassellDianaT / Embery, Graham

    Biomaterials

    2002  Volume 23, Issue 2, Page(s) 481–489

    Abstract: Proteoglycans and their spatial arms, glycosaminoglycans (GAGs), are known to interact with hydroxyapatite (HAP) and have been implicated as important modulators of mineralisation. In the present study isotherm data (0.02 M sodium acetate, pH 6.8) ... ...

    Abstract Proteoglycans and their spatial arms, glycosaminoglycans (GAGs), are known to interact with hydroxyapatite (HAP) and have been implicated as important modulators of mineralisation. In the present study isotherm data (0.02 M sodium acetate, pH 6.8) revealed that the iduronic-rich GAGs heparan sulphate, heparin and dermatan sulphate showed greater binding onto HAP with higher adsorption maxima compared with the glucuronic acid-rich GAGs chondroitin-4-sulphate, chondroitin-6-sulphate and hyaluronan. Chemically desulphated chondroitin showed no adsorption onto HAP. With the exception of hyaluronan, the GAGs studied showed no desorbability in sodium acetate buffer only, whereas in di-sodium orthophosphate, desorption occurred much more readily. The data indicates that GAG chemistry and conformation in solution greatly influence the interaction of these molecules with HAP. The conformational flexibility of iduronic acid residues may be an important determinant in the strong binding of iduronic acid-rich GAGs to HAP, increasing the possibility of the appended anionic groups matching calcium sites on the HAP surface, compared with more rigid glucuronic acid residues. This work provides important information concerning interfacial adsorption phenomena between the organic-inorganic phases of mineralised systems.
    MeSH term(s) Adsorption ; Glucuronic Acid/chemistry ; Glycosaminoglycans/chemistry ; Hydroxyapatites/chemistry ; Iduronic Acid/chemistry ; Thermodynamics
    Chemical Substances Glycosaminoglycans ; Hydroxyapatites ; Iduronic Acid (3402-98-0) ; Glucuronic Acid (8A5D83Q4RW)
    Language English
    Publishing date 2002-01
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 603079-8
    ISSN 0142-9612
    ISSN 0142-9612
    DOI 10.1016/s0142-9612(01)00130-2
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  9. Article: Inhibition of hydroxyapatite crystal growth by bone proteoglycans and proteoglycan components.

    Rees, Sarah G / Shellis, R Peter / Embery, Graham

    Biochemical and biophysical research communications

    2002  Volume 292, Issue 3, Page(s) 727–733

    Abstract: The small leucine-rich proteoglycans (SLRPs) interact with hydroxyapatite (HAP) and have been demonstrated to be important modulators of mineralisation. In the present study we have examined the effect of bone SLRPs, purified bone glycosaminoglycan (GAG) ...

    Abstract The small leucine-rich proteoglycans (SLRPs) interact with hydroxyapatite (HAP) and have been demonstrated to be important modulators of mineralisation. In the present study we have examined the effect of bone SLRPs, purified bone glycosaminoglycan (GAG) chains and core proteins as well as commercial chondroitin 4-sulphate, chondroitin 6-sulphate and desulphated chondroitin on HAP crystal growth. Seeded HAP growth experiments revealed that addition of bone GAG chains resulted in almost complete inhibition of crystal growth (93%), with addition of core proteins and intact PGs resulting in 55 and 37% inhibition, respectively. In contrast, commercial chondroitin 4-sulphate was significantly less inhibitory compared with the bone SLRPs and components, yielding only a 6% reduction in HAP-induced crystal growth at the same concentration. Significantly, chondroitin 6-sulphate was found to be noninhibitory, whilst desulphated chondroitin was inhibitory to seeded HAP growth. The data indicate that direct adsorption of SLRPs to growth sites and their ability to bind calcium are significant determinants in the inhibitory process. In addition, PG/GAG chemistry and the conformation of the macromolecules in solution have also been shown to be important. This work provides new information regarding the role of bone SLRPs and their components in the regulation of the mineralisation process.
    MeSH term(s) Animals ; Bone and Bones/chemistry ; Bone and Bones/metabolism ; Crystallization ; Glycosaminoglycans/chemistry ; Glycosaminoglycans/metabolism ; Hydroxyapatites/chemistry ; Proteoglycans/chemistry ; Proteoglycans/metabolism ; Sheep
    Chemical Substances Glycosaminoglycans ; Hydroxyapatites ; Proteoglycans
    Language English
    Publishing date 2002-04-05
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 205723-2
    ISSN 0006-291X ; 0006-291X
    ISSN (online) 0006-291X
    ISSN 0006-291X
    DOI 10.1006/bbrc.2002.6699
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  10. Article: The isolation of chondroitin 4-(35S)sulphate from the molar teeth of young rats receiving sodium(35S)sulphate.

    Embery, G

    Calcified tissue research

    1974  Volume 14, Issue 1, Page(s) 59–65

    MeSH term(s) Animals ; Chondroitin/analysis ; Chondroitin/biosynthesis ; Chondroitin/isolation & purification ; Chondroitin/metabolism ; Connective Tissue/metabolism ; Decalcification Technique ; Dental Pulp/analysis ; Dentin/analysis ; Electrophoresis, Paper ; Female ; Hexosamines/analysis ; Hexoses/analysis ; Injections, Intraperitoneal ; Isotope Labeling ; Male ; Methods ; Molar/analysis ; Molecular Weight ; Rats ; Sodium/administration & dosage ; Spectrophotometry, Infrared ; Sulfates/administration & dosage ; Sulfates/metabolism ; Sulfur Radioisotopes
    Chemical Substances Hexosamines ; Hexoses ; Sulfates ; Sulfur Radioisotopes ; Chondroitin (9007-27-6) ; Sodium (9NEZ333N27)
    Language English
    Publishing date 1974
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 1413-8
    ISSN 0008-0594 ; 0944-081X
    ISSN 0008-0594 ; 0944-081X
    DOI 10.1007/bf02060283
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