The Collagen Superfamily: Everything You Always Wanted to Know

Salamito, Mélanie; Nauroy, Pauline; Ruggiero, Florence

doi:10.1007/978-3-030-67592-9_1

Cited by 6 publications

(3 citation statements)

References 57 publications

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Section: Introductionmentioning

confidence: 99%

“…Collagens are structural proteins of the extracellular matrix (ECM) in multicellular animals and, with a mass fraction of more than 30 %, constitute an essential part of its structure and maintenance (Huxley-Jones et al, 2007; LeBleu et al, 2007; Patino et al, 2002; Salamito et al, 2021). Collagens are found in skin, connective tissue, vascular walls, bone, and cartilage (Ahmed et al, 2018; Bornstein & Sage, 1980; Kucharz, 1992; Miller & Gay, 1982; Zhao et al, 2021).…”

Section: Introductionmentioning

confidence: 99%

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Constructing networks for comparison of collagen types

Wesp,

Scholz,

Ziermann-Canabarro

et al. 2023

Preprint

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Collagens are structural proteins that are predominantly found in the extracellular matrix, where they are mainly responsible for the stability and structural integrity of various tissues. There are several different types of collagens, some of which differ significantly in form, function, and tissue specificity. Subdivisions into so-called collagen families exist, which are defined on the basis of mainly clinical research. Collagens contain polypeptide strands (ɑ-chains). Their sequences are often analysed in view of clinical aspects, but problems arise with highly homologous sequence segments. To increase the accuracy of collagen classification and prediction of their functions, the structure of these collagens and their expression in different tissues could result in a better focus on sequence segments of interest. Here, we analyse collagen families with different levels of conservation. As a result, families with strong interchain hydrogen bonds can be found, such as fibrillar collagens, network-forming collagens, and FACITs. Moreover, collagen IV α-chains form their own cluster, and other collagen α-chains do not bond at all.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Constructing networks for comparison of collagen types

Wesp,

Scholz,

Ziermann-Canabarro

et al. 2023

Preprint

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show abstract

“…Collagens are one of the most abundant proteins in the human body [1] and are also among the most biosynthetically complex proteins [2][3][4][5]. Collagen biosynthesis is a highly orchestrated process involving over 20 proteins that takes place in the endoplasmic reticulum (ER).…”

Section: Introductionmentioning

confidence: 99%

Local Net Charge State of Collagen Triple Helix Is a Determinant of FKBP22 Binding to Collagen III

Ishikawa,

Bonna,

Gould

et al. 2023

IJMS

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Mutations in the FKBP14 gene encoding the endoplasmic reticulum resident collagen-related proline isomerase FK506 binding protein 22 kDa (FKBP22) result in kyphoscoliotic Ehlers–Danlos Syndrome (EDS), which is characterized by a broad phenotypic outcome. A plausible explanation for this outcome is that FKBP22 participates in the biosynthesis of subsets of collagen types: FKBP22 selectively binds to collagens III, IV, VI, and X, but not to collagens I, II, V, and XI. However, these binding mechanisms have never been explored, and they may underpin EDS subtype heterogeneity. Here, we used collagen Toolkit peptide libraries to investigate binding specificity. We observed that FKBP22 binding was distributed along the collagen helix. Further, it (1) was higher on collagen III than collagen II peptides and it (2) was correlated with a positive peptide charge. These findings begin to elucidate the mechanism by which FKBP22 interacts with collagen.

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Recent Developments in Antimicrobial and Antiviral Agents Based on Natural/Synthetic Polymers and Dendrimers: Design and Therapeutic Applications

Abd‐El‐Aziz,

Fouda,

Sharaby

et al. 2024

Macro Chemistry & Physics

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This review article explores the recent innovations in the field of antimicrobial and antiviral macromolecules. With the rising challenge of antibiotic resistance, as well as the overuse of antibiotics, there is a growing demand for efficient solutions to combat microbial and viral infections. The development of new effective antimicrobial and antiviral agents is highlighted. This review was designed to give a comprehensive view of the literature focusing on a few examples of combating microbial and viral infections in each section. A brief description of naturally occurring organic‐based materials that exhibited antimicrobial and/or antiviral activities is presented, focusing on polysaccharides, peptides and proteins. Synthetic organic‐based materials are divided into subsections including polymers, dendrimers, and nanomaterials. The synthesis and applications of inorganic materials such as polyphosphazenes and polysiloxanes, as well as tin‐, germanium‐ and gallium‐based materials are emphasized in this review. Organometallic macromolecules are also described, and their antimicrobial and antiviral activities are examined. Overall, this article provides a comprehensive overview of recent advancements in the design of antimicrobial and antiviral macromolecules, offering valuable insights into their potential applications in biomedical research and combating drug‐resistant microorganisms and viruses.This article is protected by copyright. All rights reserved

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The Collagen Superfamily: Everything You Always Wanted to Know

Cited by 6 publications

References 57 publications

Constructing networks for comparison of collagen types

Constructing networks for comparison of collagen types

Local Net Charge State of Collagen Triple Helix Is a Determinant of FKBP22 Binding to Collagen III

Recent Developments in Antimicrobial and Antiviral Agents Based on Natural/Synthetic Polymers and Dendrimers: Design and Therapeutic Applications

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