We are analyzing https://link.springer.com/article/10.1007/s000180300026.

Title:
Anti-DNA antibodies: aspects of structure and pathogenicity | Cellular and Molecular Life Sciences
Description:
Anti-DNA antibodies contribute to the pathology of systemic lupus erythematosus. Their depositon in tissue lesions could result from localization of preformed immune complexes of antibodies with DNA or nucleosomes, or from cross-reaction of anti-DNA antibodies directly with tissue proteins. Structural analyses contribute to understanding their pathogenic potential. Primary structures of lupus immunoglobulin G double-stranded DNA-binding autoantibodies are determined by immunoglobulin genes with mutated variable region segments, indicative of selection by immunizing antigen. Arginine, lysine and asparagine residues in complementarity-determining region favor DNA binding. Heavy-chain variable regions make major contributions to DNA binding; affinity and specificity of binding are modulated or can be abrogated by the light-chain variable domain. Crytallographic structure is known for a few antibody-DNA complexes and several ligand-free Fab fragments. Computer modeling supplements this limited information. Structural information of lupus antibody interactions with both DNA and cross-reacting molecules will support use of ligands to inhibit tissue deposition of the antibodies and prevent lesion formation in lupus.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

Science
Books & Literature
Telecommunications

Content Management System {📝}

What CMS is link.springer.com built with?

Custom-built

No common CMS systems were detected on Link.springer.com, and no known web development framework was identified.

Traffic Estimate {📈}

What is the average monthly size of link.springer.com audience?

🌠 Phenomenal Traffic: 5M - 10M visitors per month

Based on our best estimate, this website will receive around 5,000,019 visitors per month in the current month.
However, some sources were not loaded, we suggest to reload the page to get complete results.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

How Does Link.springer.com Make Money? {💸}

We find it hard to spot revenue streams.

While many websites aim to make money, others are created to share knowledge or showcase creativity. People build websites for various reasons. This could be one of them. Link.springer.com might have a hidden revenue stream, but it's not something we can detect.

Keywords {🔍}

article, antibodies, lupus, information, dna, access, privacy, cookies, content, antidna, publish, search, systemic, erythematosus, data, log, journal, research, life, cmls, structure, pathogenicity, jang, stollar, tissue, immunoglobulin, variable, binding, open, discover, author, usa, springer, make, optional, personal, parties, policy, find, track, cellular, molecular, sciences, aspects, published, february, cite, explore, contribute, complexes,

Topics {✒️}

systemic lupus erythematosus double-stranded dna-binding autoantibodies anti-dna antibodies directly anti-dna antibodies contribute light-chain variable domain month download article/chapter anti-dna antibodies ligand-free fab fragments lupus antibody interactions related subjects anti-nuclear antibodies dna binding antibody-dna complexes full article pdf tissue proteins privacy choices/manage cookies pathogenic potential lupus immunoglobulin european economic area scope submit manuscript preformed immune complexes structural analyses contribute prevent lesion formation tufts university school conditions privacy policy computer modeling supplements cross-reacting molecules article cellular inhibit tissue deposition accepting optional cookies check access ajou university school instant access pathogenicity review published journal finder publish lupus article log affinity structural information author life sci article jang limited information dna article cite binding access privacy policy personal data books a

Schema {🗺️}

WebPage:
      mainEntity:
         headline:Anti-DNA antibodies: aspects of structure and pathogenicity
         description: Anti-DNA antibodies contribute to the pathology of systemic lupus erythematosus. Their depositon in tissue lesions could result from localization of preformed immune complexes of antibodies with DNA or nucleosomes, or from cross-reaction of anti-DNA antibodies directly with tissue proteins. Structural analyses contribute to understanding their pathogenic potential. Primary structures of lupus immunoglobulin G double-stranded DNA-binding autoantibodies are determined by immunoglobulin genes with mutated variable region segments, indicative of selection by immunizing antigen. Arginine, lysine and asparagine residues in complementarity-determining region favor DNA binding. Heavy-chain variable regions make major contributions to DNA binding; affinity and specificity of binding are modulated or can be abrogated by the light-chain variable domain. Crytallographic structure is known for a few antibody-DNA complexes and several ligand-free Fab fragments. Computer modeling supplements this limited information. Structural information of lupus antibody interactions with both DNA and cross-reacting molecules will support use of ligands to inhibit tissue deposition of the antibodies and prevent lesion formation in lupus.
         datePublished:2003-02-01T00:00:00Z
         dateModified:2003-02-01T00:00:00Z
         pageStart:309
         pageEnd:320
         sameAs:https://doi.org/10.1007/s000180300026
         keywords:
            Key words. Antibodies; autoantibodies; lupus; SLE; immunoglobulin genes; pathogenicity; autoimmunity; crystallography; computer models.
            Cell Biology
            Biomedicine
            general
            Life Sciences
            Biochemistry
         image:
         isPartOf:
            name:Cellular and Molecular Life Sciences CMLS
            issn:
               1420-9071
               1420-682X
            volumeNumber:60
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Birkhäuser-Verlag
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:Y. J. Jang
               affiliation:
                     name:Laboratory of Immunology, Institute for Medical Science, Ajou University School of Medicine, Suwon 442-721 (Korea), Fax +82 31 219 4503, e-mail: [email protected]
                     address:
                        name:Laboratory of Immunology, Institute for Medical Science, Ajou University School of Medicine, Suwon 442-721 (Korea), Fax +82 31 219 4503, e-mail: [email protected], Korea
                        type:PostalAddress
                     type:Organization
               type:Person
               name:B. D. Stollar
               affiliation:
                     name:Department of Biochemistry, Tufts University School of Medicine, Boston, Massachusetts 02111 (USA)
                     address:
                        name:Department of Biochemistry, Tufts University School of Medicine, Boston, Massachusetts 02111 (USA), USA
                        type:PostalAddress
                     type:Organization
               type:Person
         isAccessibleForFree:
         hasPart:
            isAccessibleForFree:
            cssSelector:.main-content
            type:WebPageElement
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:Anti-DNA antibodies: aspects of structure and pathogenicity
      description: Anti-DNA antibodies contribute to the pathology of systemic lupus erythematosus. Their depositon in tissue lesions could result from localization of preformed immune complexes of antibodies with DNA or nucleosomes, or from cross-reaction of anti-DNA antibodies directly with tissue proteins. Structural analyses contribute to understanding their pathogenic potential. Primary structures of lupus immunoglobulin G double-stranded DNA-binding autoantibodies are determined by immunoglobulin genes with mutated variable region segments, indicative of selection by immunizing antigen. Arginine, lysine and asparagine residues in complementarity-determining region favor DNA binding. Heavy-chain variable regions make major contributions to DNA binding; affinity and specificity of binding are modulated or can be abrogated by the light-chain variable domain. Crytallographic structure is known for a few antibody-DNA complexes and several ligand-free Fab fragments. Computer modeling supplements this limited information. Structural information of lupus antibody interactions with both DNA and cross-reacting molecules will support use of ligands to inhibit tissue deposition of the antibodies and prevent lesion formation in lupus.
      datePublished:2003-02-01T00:00:00Z
      dateModified:2003-02-01T00:00:00Z
      pageStart:309
      pageEnd:320
      sameAs:https://doi.org/10.1007/s000180300026
      keywords:
         Key words. Antibodies; autoantibodies; lupus; SLE; immunoglobulin genes; pathogenicity; autoimmunity; crystallography; computer models.
         Cell Biology
         Biomedicine
         general
         Life Sciences
         Biochemistry
      image:
      isPartOf:
         name:Cellular and Molecular Life Sciences CMLS
         issn:
            1420-9071
            1420-682X
         volumeNumber:60
         type:
            Periodical
            PublicationVolume
      publisher:
         name:Birkhäuser-Verlag
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Y. J. Jang
            affiliation:
                  name:Laboratory of Immunology, Institute for Medical Science, Ajou University School of Medicine, Suwon 442-721 (Korea), Fax +82 31 219 4503, e-mail: [email protected]
                  address:
                     name:Laboratory of Immunology, Institute for Medical Science, Ajou University School of Medicine, Suwon 442-721 (Korea), Fax +82 31 219 4503, e-mail: [email protected], Korea
                     type:PostalAddress
                  type:Organization
            type:Person
            name:B. D. Stollar
            affiliation:
                  name:Department of Biochemistry, Tufts University School of Medicine, Boston, Massachusetts 02111 (USA)
                  address:
                     name:Department of Biochemistry, Tufts University School of Medicine, Boston, Massachusetts 02111 (USA), USA
                     type:PostalAddress
                  type:Organization
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:Cellular and Molecular Life Sciences CMLS
      issn:
         1420-9071
         1420-682X
      volumeNumber:60
Organization:
      name:Birkhäuser-Verlag
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Laboratory of Immunology, Institute for Medical Science, Ajou University School of Medicine, Suwon 442-721 (Korea), Fax +82 31 219 4503, e-mail: [email protected]
      address:
         name:Laboratory of Immunology, Institute for Medical Science, Ajou University School of Medicine, Suwon 442-721 (Korea), Fax +82 31 219 4503, e-mail: [email protected], Korea
         type:PostalAddress
      name:Department of Biochemistry, Tufts University School of Medicine, Boston, Massachusetts 02111 (USA)
      address:
         name:Department of Biochemistry, Tufts University School of Medicine, Boston, Massachusetts 02111 (USA), USA
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Y. J. Jang
      affiliation:
            name:Laboratory of Immunology, Institute for Medical Science, Ajou University School of Medicine, Suwon 442-721 (Korea), Fax +82 31 219 4503, e-mail: [email protected]
            address:
               name:Laboratory of Immunology, Institute for Medical Science, Ajou University School of Medicine, Suwon 442-721 (Korea), Fax +82 31 219 4503, e-mail: [email protected], Korea
               type:PostalAddress
            type:Organization
      name:B. D. Stollar
      affiliation:
            name:Department of Biochemistry, Tufts University School of Medicine, Boston, Massachusetts 02111 (USA)
            address:
               name:Department of Biochemistry, Tufts University School of Medicine, Boston, Massachusetts 02111 (USA), USA
               type:PostalAddress
            type:Organization
PostalAddress:
      name:Laboratory of Immunology, Institute for Medical Science, Ajou University School of Medicine, Suwon 442-721 (Korea), Fax +82 31 219 4503, e-mail: [email protected], Korea
      name:Department of Biochemistry, Tufts University School of Medicine, Boston, Massachusetts 02111 (USA), USA
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(27)

Analytics and Tracking {📊}

Google Tag Manager

Libraries {📚}

Clipboard.js
Prism.js

CDN Services {📦}

Crossref

4.62s.

LINK . SPRINGER . COM {}