COL1A1 | ENSG00000108821 | NCBI 1277

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Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

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Other Information

This section provides additional information about the gene, including a description generated by an AI language model and details about associated proteins.

Description
Proteins

## Summary [COL1A1](/details-gene/1277) (collagen type I alpha 1 chain) is a protein-coding gene located on chromosome 17q21.33. It encodes the primary alpha-1 chain of type I collagen, the most abundant collagen in the human body. As the principal fibrillar collagen in most connective tissues, it provides essential tensile strength and structural integrity to bone, skin, tendons, and ligaments. Its fundamental role is underscored by its high expression in mesenchymal-derived cells, particularly fibroblasts and smooth muscle cells. Mutations in [COL1A1](/details-gene/1277) are well-documented causes of several connective tissue disorders, including various forms of Osteogenesis Imperfecta ([120150](https://omim.org/entry/120150), [166210](https://omim.org/entry/166210)) and Ehlers-Danlos syndrome ([130060](https://omim.org/entry/130060)), highlighting its critical importance in skeletal development and tissue homeostasis [Link](https://doi.org/10.1086/301689). ## Cellular Roles and Expression Landscape The expression profile of [COL1A1](/details-gene/1277) firmly establishes its role as a cornerstone gene for cells responsible for synthesizing the extracellular matrix (ECM). **Overall**, the gene exhibits its highest significance in stromal and mesenchymal cell populations. It is most prominently expressed and serves as a key functional marker in various fibroblast subtypes, including [bronchus fibroblast of lung](/details-cell/CL2000093) (CSI: 37.93), [skin fibroblast](/details-cell/CL0002620) (CSI: 19.39), and [fibroblast of lung](/details-cell/CL0002553) (CSI: 13.48). Its high CSI scores in these cells indicate that [COL1A1](/details-gene/1277) is a highly active and abundant transcript, consistent with the primary function of fibroblasts in secreting collagen to form the structural scaffold of tissues. Beyond fibroblasts, [COL1A1](/details-gene/1277) is also highly significant in other structural and contractile cells such as [mesodermal cell](/details-cell/CL0000222) (CSI: 24.09), [enteric smooth muscle cell](/details-cell/CL0002504) (CSI: 23.20), and [myofibroblast cell](/details-cell/CL0000186) (CSI: 19.13). Its expression in [chondrocyte](/details-cell/CL0000138) (CSI: 15.63) further points to its crucial role in cartilage and skeletal development. This widespread expression across mesenchymal lineages solidifies the role of [COL1A1](/details-gene/1277) as a master gene for connective tissue architecture. ## Pathways and Molecular Function The molecular function and biological roles of [COL1A1](/details-gene/1277) are extensively annotated and center on structural biology and tissue development. Its primary molecular function is defined as an '[extracellular matrix structural constituent conferring tensile strength](/details-cell/GO:0030020)'. This is executed through its participation in forming the '[collagen type I trimer](/details-cell/GO:0005584)' within the '[collagen-containing extracellular matrix](/details-cell/GO:0062023)'. Functionally, [COL1A1](/details-gene/1277) is integral to numerous developmental and homeostatic processes. Its involvement in '[skeletal system development](/details-cell/GO:0001501)', '[ossification](/details-cell/GO:0001503)', and '[osteoblast differentiation](/details-cell/GO:0001649)' is consistent with its high expression in mesenchymal cells and its clinical link to bone fragility diseases. Reactome pathway analysis confirms this, highlighting its role in '[Collagen formation](/details-cell/R-HSA-1474290)' and the broader process of '[Extracellular matrix organization](/details-cell/R-HSA-1474244)'. Beyond its structural role, [COL1A1](/details-gene/1277) is involved in critical signaling events. It participates in the '[collagen-activated tyrosine kinase receptor signaling pathway](/details-cell/GO:0038063)' and pathways related to hemostasis, such as '[Platelet adhesion to exposed collagen](/details-cell/R-HSA-75892)'. Furthermore, its annotation in immune pathways like '[Adaptive immune system](/details-cell/R-HSA-1280218)' and '[Immunoregulatory interactions between a lymphoid and a non-lymphoid cell](/details-cell/R-HSA-198933)' suggests that the matrix produced by [COL1A1](/details-gene/1277) may also function as a key component of the tissue microenvironment, influencing cell behavior and immune responses. ## Research Directions The well-established structural role of [COL1A1](/details-gene/1277) provides a foundation for exploring its more dynamic and regulatory functions in health and disease, particularly in fibrosis and the tumor microenvironment. Based on the available data, several testable hypotheses can be proposed: 1. Given its involvement in '[positive regulation of epithelial to mesenchymal transition](/details-cell/GO:0010718)' and high expression in myofibroblasts, the over-expression of [COL1A1](/details-gene/1277) during chronic injury actively promotes a pro-fibrotic feedback loop, rather than simply being a passive structural consequence of fibroblast activation. 2. The specific structural and biochemical properties of the [COL1A1](/details-gene/1277)-rich matrix directly modulate immune cell function. Deposition of type I collagen in tissues creates physical niches that can either promote inflammatory responses or induce immune tolerance, depending on the context (e.g., wound healing vs. tumor stroma). A compelling experimental approach to test the second hypothesis would be: * To investigate the immunomodulatory role of the [COL1A1](/details-gene/1277)-derived matrix, one could co-culture activated primary human T-cells on extracellular matrices generated by fibroblasts with and without CRISPR-Cas9-mediated knockdown of [COL1A1](/details-gene/1277). Subsequent analysis of T-cell proliferation via cell tracing dyes, activation marker expression (e.g., CD69, PD-1) by flow cytometry, and cytokine secretion profiles (e.g., IFN-gamma, IL-10) by multiplex assay would reveal whether the collagen I matrix directly and specifically influences T-cell effector functions. From a therapeutic perspective, [COL1A1](/details-gene/1277) is a major target in pathological conditions characterized by excessive ECM deposition, such as idiopathic pulmonary fibrosis, cirrhosis, and the desmoplastic stroma of many cancers. The therapeutic strategy would focus on **inhibition** of its synthesis, secretion, or deposition. However, its ubiquitous and essential nature in healthy tissues makes systemic inhibition challenging. Promising future strategies may involve developing inhibitors that target the specific regulatory pathways driving its over-expression in diseased cells or using antibody-based therapies to target disease-specific post-translational modifications of type I collagen, thereby limiting off-target effects.

Disclaimer: This in-silico analysis is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

Collagen alpha-1(I) chain

Genular Protein ID: 4177201008

Symbol: CO1A1_HUMAN

Name: Collagen alpha-1(I) chain

UniProtKB Accession Codes:

P02452 O76045 P78441 Q13896 Q13902 Q13903 Q14037 Q14992 Q15176 Q15201 Q16050 Q59F64 Q7KZ30 Q7KZ34 Q8IVI5 Q8N473 Q9UML6 Q9UMM7

Database IDs:

Citations:

PubMed ID: 9443882

Title: Analysis of the COL1A1 and COL1A2 genes by PCR amplification and scanning by conformation-sensitive gel electrophoresis identifies only COL1A1 mutations in 15 patients with osteogenesis imperfecta type I: identification of common sequences of null-allele mutations.

PubMed ID: 9443882

DOI: 10.1086/301689

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 2843432

Title: Complete nucleotide sequence of the region encompassing the first twenty-five exons of the human pro alpha 1(I) collagen gene (COL1A1).

PubMed ID: 2843432

DOI: 10.1016/0378-1119(88)90013-3

PubMed ID: 3178743

Title: Structure of a full-length cDNA clone for the prepro alpha 1(I) chain of human type I procollagen.

PubMed ID: 3178743

DOI: 10.1042/bj2530919

PubMed ID: 6462220

Title: Human pro alpha 1(I) collagen gene structure reveals evolutionary conservation of a pattern of introns and exons.

PubMed ID: 6462220

DOI: 10.1038/310337a0

PubMed ID: 2822714

Title: DNA sequences in the first intron of the human pro-alpha 1(I) collagen gene enhance transcription.

PubMed ID: 2822714

DOI: 10.1016/s0021-9258(18)48151-3

PubMed ID: 2857713

Title: Fine structural analysis of the human pro-alpha 1 (I) collagen gene. Promoter structure, AluI repeats, and polymorphic transcripts.

PubMed ID: 2857713

DOI: 10.1016/s0021-9258(18)89556-4

PubMed ID: 3480516

Title: Regulatory elements in the first intron contribute to transcriptional control of the human alpha 1(I) collagen gene.

PubMed ID: 3480516

DOI: 10.1073/pnas.84.24.8869

PubMed ID: 2318855

Title: In vivo and in vitro noncovalent association of excised alpha 1 (I) amino-terminal propeptides with mutant pN alpha 2(I) collagen chains in native mutant collagen in a case of Ehlers-Danlos syndrome, type VII.

PubMed ID: 2318855

DOI: 10.1016/s0021-9258(19)39327-5

PubMed ID: 2767050

Title: A base substitution in the exon of a collagen gene causes alternative splicing and generates a structurally abnormal polypeptide in a patient with Ehlers-Danlos syndrome type VII.

PubMed ID: 2767050

DOI: 10.1002/j.1460-2075.1989.tb03562.x

PubMed ID: 5529814

Title: Isolation and characterization of the cyanogen bromide peptides from the alpha 1 and alpha 2 chains of human skin collagen.

PubMed ID: 5529814

DOI: 10.1021/bi00826a012

PubMed ID: 2169412

Title: A critical crosslink region in human-bone-derived collagen type I. Specific cleavage site at residue Leu95.

PubMed ID: 2169412

DOI: 10.1111/j.1432-1033.1990.tb19208.x

PubMed ID: 4319110

Title: A comparative study of glycopeptides derived from selected vertebrate collagens. A possible role of the carbohydrate in fibril formation.

PubMed ID: 4319110

DOI: 10.1016/s0021-9258(18)62815-7

PubMed ID: 2374517

Title: Segmental amplification of the entire helical and telopeptide regions of the cDNA for human alpha 1 (I) collagen.

PubMed ID: 2374517

DOI: 10.1016/s0934-8832(11)80178-2

PubMed ID: 6689127

Title: Nucleotide sequences of complementary deoxyribonucleic acids for the pro alpha 1 chain of human type I procollagen. Statistical evaluation of structures that are conserved during evolution.

PubMed ID: 6689127

DOI: 10.1021/bi00291a023

PubMed ID: 6183642

Title: Cloning and characterization of five overlapping cDNAs specific for the human pro alpha 1(I) collagen chain.

PubMed ID: 6183642

DOI: 10.1093/nar/10.19.5925

PubMed ID: 2981843

Title: Multiexon deletion in an osteogenesis imperfecta variant with increased type III collagen mRNA.

PubMed ID: 2981843

DOI: 10.1016/s0021-9258(20)71150-6

PubMed ID: 3857621

Title: Intron-mediated recombination may cause a deletion in an alpha 1 type I collagen chain in a lethal form of osteogenesis imperfecta.

PubMed ID: 3857621

DOI: 10.1073/pnas.82.9.2870

PubMed ID: 2339700

Title: Variable expression of osteogenesis imperfecta in a nuclear family is explained by somatic mosaicism for a lethal point mutation in the alpha 1(I) gene (COL1A1) of type I collagen in a parent.

PubMed ID: 2339700

PubMed ID: 7881420

Title: Severe (type III) osteogenesis imperfecta due to glycine substitutions in the central domain of the collagen triple helix.

PubMed ID: 7881420

DOI: 10.1093/hmg/3.12.2201

PubMed ID: 8349697

Title: Mutations in the carboxyl-terminal propeptide of the pro alpha 1(I) chain of type I collagen result in defective chain association and produce lethal osteogenesis imperfecta.

PubMed ID: 8349697

DOI: 10.1016/s0021-9258(17)46833-5

PubMed ID: 3170557

Title: Substitution of cysteine for glycine within the carboxyl-terminal telopeptide of the alpha 1 chain of type I collagen produces mild osteogenesis imperfecta.

PubMed ID: 3170557

DOI: 10.1016/s0021-9258(18)68076-7

PubMed ID: 3340531

Title: Human pro alpha 1(I) collagen: cDNA sequence for the C-propeptide domain.

PubMed ID: 3340531

DOI: 10.1093/nar/16.1.349

PubMed ID: 2295701

Title: Frameshift mutation near the 3' end of the COL1A1 gene of type I collagen predicts an elongated Pro alpha 1(I) chain and results in osteogenesis imperfecta type I.

PubMed ID: 2295701

DOI: 10.1172/jci114424

PubMed ID: 1995349

Title: Highly conserved sequences in the 3'-untranslated region of the COL1A1 gene bind cell-specific nuclear proteins.

PubMed ID: 1995349

DOI: 10.1016/0014-5793(91)80237-w

PubMed ID: 2010058

Title: Mutations in collagen genes: causes of rare and some common diseases in humans.

PubMed ID: 2010058

DOI: 10.1096/fasebj.5.7.2010058

PubMed ID: 9295084

Title: Ehlers-Danlos syndrome type VIIA and VIIB result from splice-junction mutations or genomic deletions that involve exon 6 in the COL1A1 and COL1A2 genes of type I collagen.

PubMed ID: 9295084

DOI: 10.1002/(sici)1096-8628(19971003)72:1<94::aid-ajmg20>3.0.co;2-o

PubMed ID: 9101290

Title: Mutations in fibrillar collagens (types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels.

PubMed ID: 9101290

DOI: 10.1002/(sici)1098-1004(1997)9:4<300::aid-humu2>3.0.co;2-9

PubMed ID: 1895312

Title: Osteogenesis imperfecta: translation of mutation to phenotype.

PubMed ID: 1895312

DOI: 10.1136/jmg.28.7.433

PubMed ID: 14749390

Title: TRAM2 protein interacts with endoplasmic reticulum Ca2+ pump Serca2b and is necessary for collagen type I synthesis.

PubMed ID: 14749390

DOI: 10.1128/mcb.24.4.1758-1768.2004

PubMed ID: 18409203

Title: The arthrochalasia type of Ehlers-Danlos syndrome (EDS VIIA and VIIB): the diagnostic value of collagen fibril ultrastructure.

PubMed ID: 18409203

DOI: 10.1002/ajmg.a.32213

PubMed ID: 22905912

Title: Resveratrol-induced changes of the human adipocyte secretion profile.

PubMed ID: 22905912

DOI: 10.1021/pr300539b

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 3016737

Title: Lethal osteogenesis imperfecta resulting from a single nucleotide change in one human pro alpha 1(I) collagen allele.

PubMed ID: 3016737

DOI: 10.1073/pnas.83.16.6045

PubMed ID: 3108247

Title: Lethal perinatal osteogenesis imperfecta due to the substitution of arginine for glycine at residue 391 of the alpha 1(I) chain of type I collagen.

PubMed ID: 3108247

DOI: 10.1016/s0021-9258(18)48196-3

PubMed ID: 3667599

Title: A point mutation in a type I procollagen gene converts glycine 748 of the alpha 1 chain to cysteine and destabilizes the triple helix in a lethal variant of osteogenesis imperfecta.

PubMed ID: 3667599

DOI: 10.1016/s0021-9258(18)47857-x

PubMed ID: 3403550

Title: Substitution of arginine for glycine 664 in the collagen alpha 1(I) chain in lethal perinatal osteogenesis imperfecta. Demonstration of the peptide defect by in vitro expression of the mutant cDNA.

PubMed ID: 3403550

DOI: 10.1016/s0021-9258(18)37829-3

PubMed ID: 3244312

Title: A cysteine for glycine substitution at position 1017 in an alpha 1(I) chain of type I collagen in a patient with mild dominantly inherited osteogenesis imperfecta.

PubMed ID: 3244312

PubMed ID: 2470760

Title: RNA sequence analysis of a perinatal lethal osteogenesis imperfecta mutation.

PubMed ID: 2470760

DOI: 10.1016/s0021-9258(18)81769-0

PubMed ID: 2745420

Title: Osteogenesis imperfecta type IV. Detection of a point mutation in one alpha 1(I) collagen allele (COL1A1) by RNA/RNA hybrid analysis.

PubMed ID: 2745420

DOI: 10.1016/s0021-9258(18)80150-8

PubMed ID: 2777764

Title: Characterization of point mutations in the collagen COL1A1 and COL1A2 genes causing lethal perinatal osteogenesis imperfecta.

PubMed ID: 2777764

DOI: 10.1016/s0021-9258(18)71548-2

PubMed ID: 2511192

Title: Substitution of serine for alpha 1(I)-glycine 844 in a severe variant of osteogenesis imperfecta minimally destabilizes the triple helix of type I procollagen. The effects of glycine substitutions on thermal stability are either position of amino acid specific.

PubMed ID: 2511192

DOI: 10.1016/s0021-9258(19)47168-8

PubMed ID: 2913053

Title: A lethal variant of osteogenesis imperfecta has a single base mutation that substitutes cysteine for glycine 904 of the alpha 1(I) chain of type I procollagen. The asymptomatic mother has an unidentified mutation producing an overmodified and unstable type I procollagen.

PubMed ID: 2913053

DOI: 10.1172/jci113920

PubMed ID: 2794057

Title: Osteogenesis imperfecta. The position of substitution for glycine by cysteine in the triple helical domain of the pro alpha 1(I) chains of type I collagen determines the clinical phenotype.

PubMed ID: 2794057

DOI: 10.1172/jci114286

PubMed ID: 2116413

Title: Mutations that substitute serine for glycine alpha 1-598 and glycine alpha 1-631 in type I procollagen. The effects on thermal unfolding of the triple helix are position-specific and demonstrate that the protein unfolds through a series of cooperative blocks.

PubMed ID: 2116413

DOI: 10.1016/s0021-9258(18)77447-4

PubMed ID: 2211725

Title: Substitution of arginine for glycine at position 847 in the triple-helical domain of the alpha 1 (I) chain of type I collagen produces lethal osteogenesis imperfecta. Molecules that contain one or two abnormal chains differ in stability and secretion.

PubMed ID: 2211725

DOI: 10.1016/s0021-9258(17)44798-3

PubMed ID: 2035536

Title: A single base mutation in type I procollagen (COL1A1) that converts glycine alpha 1-541 to aspartate in a lethal variant of osteogenesis imperfecta: detection of the mutation with a carbodiimide reaction of DNA heteroduplexes and direct sequencing of products of the PCR.

PubMed ID: 2035536

PubMed ID: 1953667

Title: Substitution of cysteine for glycine-alpha 1-691 in the pro alpha 1(I) chain of type I procollagen in a proband with lethal osteogenesis imperfecta destabilizes the triple helix at a site C-terminal to the substitution.

PubMed ID: 1953667

DOI: 10.1042/bj2790747

PubMed ID: 2036375

Title: A type I collagen with substitution of a cysteine for glycine-748 in the alpha 1(I) chain copolymerizes with normal type I collagen and can generate fractallike structures.

PubMed ID: 2036375

DOI: 10.1021/bi00234a035

PubMed ID: 2037280

Title: Osteogenesis imperfecta due to recurrent point mutations at CpG dinucleotides in the COL1A1 gene of type I collagen.

PubMed ID: 2037280

DOI: 10.1007/bf01213088

PubMed ID: 1988452

Title: A de novo G to T transversion in a pro-alpha 1 (I) collagen gene for a moderate case of osteogenesis imperfecta. Substitution of cysteine for glycine 178 in the triple helical domain.

PubMed ID: 1988452

DOI: 10.1016/s0021-9258(18)52374-7

PubMed ID: 1874719

Title: Substitutions for glycine alpha 1-637 and glycine alpha 2-694 of type I procollagen in lethal osteogenesis imperfecta. The conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helix.

PubMed ID: 1874719

DOI: 10.1016/s0021-9258(18)98449-8

PubMed ID: 1718984

Title: The substitution of arginine for glycine 85 of the alpha 1(I) procollagen chain results in mild osteogenesis imperfecta. The mutation provides direct evidence for three discrete domains of cooperative melting of intact type I collagen.

PubMed ID: 1718984

DOI: 10.1016/s0021-9258(18)54712-8

PubMed ID: 1939261

Title: A 9-base pair deletion in COL1A1 in a lethal variant of osteogenesis imperfecta.

PubMed ID: 1939261

DOI: 10.1016/s0021-9258(18)54581-6

PubMed ID: 1770532

Title: Substitution of cysteine for glycine at residue 415 of one allele of the alpha 1(I) chain of type I procollagen in type III/IV osteogenesis imperfecta.

PubMed ID: 1770532

DOI: 10.1136/jmg.28.11.757

PubMed ID: 1870989

Title: G to A polymorphism in exon 45 of the COL1A1 gene.

PubMed ID: 1870989

DOI: 10.1093/nar/19.15.4302

PubMed ID: 1445258

Title: Characterization of three osteogenesis imperfecta collagen alpha 1(I) glycine to serine mutations demonstrating a position-dependent gradient of phenotypic severity.

PubMed ID: 1445258

DOI: 10.1042/bj2880131

PubMed ID: 1460046

Title: Type I procollagens containing substitutions of aspartate, arginine, and cysteine for glycine in the pro alpha 1 (I) chain are cleaved slowly by N-proteinase, but only the cysteine substitution introduces a kink in the molecule.

PubMed ID: 1460046

DOI: 10.1016/s0021-9258(19)74071-x

PubMed ID: 1634225

Title: Mild dominant osteogenesis imperfecta with intrafamilial variability: the cause is a serine for glycine alpha 1(I) 901 substitution in a type-I collagen gene.

PubMed ID: 1634225

DOI: 10.1007/bf00219169

PubMed ID: 1511982

Title: A dominant mutation in the COL1A1 gene that substitutes glycine for valine causes recurrent lethal osteogenesis imperfecta.

PubMed ID: 1511982

DOI: 10.1007/bf00221955

PubMed ID: 1460047

Title: A tripeptide deletion in the triple-helical domain of the pro alpha 1(I) chain of type I procollagen in a patient with lethal osteogenesis imperfecta does not alter cleavage of the molecule by N-proteinase.

PubMed ID: 1460047

DOI: 10.1016/s0021-9258(19)74072-1

PubMed ID: 1737847

Title: An osteopenic nonfracture syndrome with features of mild osteogenesis imperfecta associated with the substitution of a cysteine for glycine at triple helix position 43 in the pro alpha 1(I) chain of type I collagen.

PubMed ID: 1737847

DOI: 10.1172/jci115622

PubMed ID: 1613761

Title: The clinicopathological features of three babies with osteogenesis imperfecta resulting from the substitution of glycine by valine in the pro alpha 1 (I) chain of type I procollagen.

PubMed ID: 1613761

DOI: 10.1136/jmg.29.2.112

PubMed ID: 8456808

Title: Chemical cleavage method for the detection of RNA base changes: experience in the application to collagen mutations in osteogenesis imperfecta.

PubMed ID: 8456808

DOI: 10.1002/ajmg.1320450216

PubMed ID: 8456809

Title: Moderately severe osteogenesis imperfecta associated with substitutions of serine for glycine in the alpha 1(I) chain of type I collagen.

PubMed ID: 8456809

DOI: 10.1002/ajmg.1320450217

PubMed ID: 8339541

Title: A cysteine for glycine substitution at position 175 in an alpha 1 (I) chain of type I collagen produces a clinically heterogeneous form of osteogenesis imperfecta.

PubMed ID: 8339541

DOI: 10.3109/03008209309061961

PubMed ID: 7679635

Title: Osteogenesis imperfecta and type-I collagen mutations. A lethal variant caused by a Gly910-->Ala substitution in the alpha 1 (I) chain.

PubMed ID: 7679635

DOI: 10.1111/j.1432-1033.1993.tb17565.x

PubMed ID: 8223589

Title: Gly85 to Val substitution in pro alpha 1(I) chain causes mild osteogenesis imperfecta and introduces a susceptibility to protease digestion.

PubMed ID: 8223589

DOI: 10.1111/j.1432-1033.1993.tb18220.x

PubMed ID: 8100209

Title: SSCP detection of a Gly565Val substitution in the pro alpha 1(I) collagen chain resulting in osteogenesis imperfecta type II.

PubMed ID: 8100209

DOI: 10.1007/bf00217768

PubMed ID: 7691343

Title: An RT-PCR-SSCP screening strategy for detection of mutations in the gene encoding the alpha 1 chain of type I collagen: application to four patients with osteogenesis imperfecta.

PubMed ID: 7691343

DOI: 10.1093/hmg/2.8.1155

PubMed ID: 8364588

Title: Paternal mosaicism for a COL1A1 dominant mutation (alpha 1 Ser-415) causes recurrent osteogenesis imperfecta.

PubMed ID: 8364588

DOI: 10.1002/humu.1380020308

PubMed ID: 8094076

Title: Serine for glycine substitutions in type I collagen in two cases of type IV osteogenesis imperfecta (OI). Additional evidence for a regional model of OI pathophysiology.

PubMed ID: 8094076

DOI: 10.1016/s0021-9258(18)53826-6

PubMed ID: 8349698

Title: BiP binds type I procollagen pro alpha chains with mutations in the carboxyl-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta.

PubMed ID: 8349698

DOI: 10.1016/s0021-9258(17)46834-7

PubMed ID: 7520724

Title: Osteogenesis imperfecta: comparison of molecular defects with bone histological changes.

PubMed ID: 7520724

DOI: 10.1016/8756-3282(94)90295-x

PubMed ID: 8019571

Title: Substitution of glycine-172 by arginine in the alpha 1 chain of type I collagen in a patient with osteogenesis imperfecta, type III.

PubMed ID: 8019571

DOI: 10.1002/humu.1380030327

PubMed ID: 7961597

Title: Substitution of cysteine for glycine-946 in the alpha 1(I) chain of type I procollagen causes lethal osteogenesis imperfecta.

PubMed ID: 7961597

DOI: 10.1093/oxfordjournals.jbchem.a124429

PubMed ID: 7982948

Title: Substitution of serine for glycine 883 in the triple helix of the pro alpha 1 (I) chain of type I procollagen produces osteogenesis imperfecta type IV and introduces a structural change in the triple helix that does not alter cleavage of the molecule by procollagen N-proteinase.

PubMed ID: 7982948

DOI: 10.1016/s0021-9258(18)43820-3

PubMed ID: 7816518

Title: Prenatal diagnosis of collagen disorders by direct biochemical analysis of chorionic villus biopsies.

PubMed ID: 7816518

DOI: 10.1203/00006450-199410000-00005

PubMed ID: 7487936

Title: Substitutions of aspartic acid for glycine-220 and of arginine for glycine-664 in the triple helix of the pro alpha 1(I) chain of type I procollagen produce lethal osteogenesis imperfecta and disrupt the ability of collagen fibrils to incorporate crystalline hydroxyapatite.

PubMed ID: 7487936

DOI: 10.1042/bj3110815

PubMed ID: 8669434

Title: Substitution of arginine for glycine at position 154 of the alpha 1 chain of type I collagen in a variant of osteogenesis imperfecta: comparison to previous cases with the same mutation.

PubMed ID: 8669434

DOI: 10.1002/(sici)1096-8628(19960111)61:2<111::aid-ajmg1>3.0.co;2-#

PubMed ID: 8786074

Title: Substitution of glycine-661 by serine in the alpha1(I) and alpha2(I) chains of type I collagen results in different clinical and biochemical phenotypes.

PubMed ID: 8786074

DOI: 10.1007/bf02185764

PubMed ID: 8723681

Title: Mutation in the carboxy-terminal propeptide of the Pro alpha 1(I) chain of type I collagen in a child with severe osteogenesis imperfecta (OI type III): possible implications for protein folding.

PubMed ID: 8723681

DOI: 10.1002/(sici)1098-1004(1996)7:4<318::aid-humu5>3.0.co;2-4

PubMed ID: 8799376

Title: Intrafamilial variable expressivity of osteogenesis imperfecta due to mosaicism for a lethal G382R substitution in the COL1A1 gene.

PubMed ID: 8799376

DOI: 10.1006/mcpr.1996.0030

PubMed ID: 8841196

Title: Reduced bone density and osteoporosis associated with a polymorphic Sp1 binding site in the collagen type I alpha 1 gene.

PubMed ID: 8841196

DOI: 10.1038/ng1096-203

PubMed ID: 9101304

Title: Serine for glycine substitutions in the C-terminal third of the alpha 1(I) chain of collagen I in five patients with nonlethal osteogenesis imperfecta.

PubMed ID: 9101304

DOI: 10.1002/(sici)1098-1004(1997)9:4<378::aid-humu16>3.0.co;2-#

PubMed ID: 9143923

Title: (G586V) substitutions in the alpha 1 and alpha 2 chains of collagen I: effect of alpha-chain stoichiometry on the phenotype of osteogenesis imperfecta?

PubMed ID: 9143923

DOI: 10.1002/(sici)1098-1004(1997)9:5<431::aid-humu9>3.0.co;2-6

PubMed ID: 9600458

Title: Three novel type I collagen mutations in osteogenesis imperfecta type IV probands are associated with discrepancies between electrophoretic migration of osteoblast and fibroblast collagen.

PubMed ID: 9600458

DOI: 10.1002/(sici)1098-1004(1998)11:5<395::aid-humu7>3.0.co;2-4

PubMed ID: 10627137

Title: Four new cases of lethal osteogenesis imperfecta due to glycine substitutions in COL1A1 and genes.

PubMed ID: 10627137

PubMed ID: 9535665

Title: Relation of alleles of the collagen type Ialpha1 gene to bone density and the risk of osteoporotic fractures in postmenopausal women.

PubMed ID: 9535665

DOI: 10.1056/nejm199804093381502

PubMed ID: 10408781

Title: Osteogenesis imperfecta: mosaicism and refinement of the genotype-phenotype map in OI type III.

PubMed ID: 10408781

DOI: 10.1002/(sici)1098-1004(1999)13:6<503::aid-humu11>3.0.co;2-l

PubMed ID: 10739762

Title: Classical Ehlers-Danlos syndrome caused by a mutation in type I collagen.

PubMed ID: 10739762

DOI: 10.1086/302859

PubMed ID: 8988177

Title: Deregulation of the platelet-derived growth factor B-chain gene via fusion with collagen gene COL1A1 in dermatofibrosarcoma protuberans and giant-cell fibroblastoma.

PubMed ID: 8988177

DOI: 10.1038/ng0197-95

PubMed ID: 12660034

Title: Dermatofibrosarcoma protuberans of breast.

PubMed ID: 12660034

DOI: 10.1016/s0165-4608(02)00844-0

PubMed ID: 15728585

Title: Mutations near amino end of alpha1(I) collagen cause combined osteogenesis imperfecta/Ehlers-Danlos syndrome by interference with N-propeptide processing.

PubMed ID: 15728585

DOI: 10.1074/jbc.m414698200

PubMed ID: 15864348

Title: A novel COL1A1 mutation in infantile cortical hyperostosis (Caffey disease) expands the spectrum of collagen-related disorders.

PubMed ID: 15864348

DOI: 10.1172/jci22760

PubMed ID: 16879195

Title: Osteogenesis imperfecta: clinical, biochemical and molecular findings.

PubMed ID: 16879195

DOI: 10.1111/j.1399-0004.2006.00646.x

PubMed ID: 16705691

Title: Mutational spectrum of type I collagen genes in Korean patients with osteogenesis imperfecta.

PubMed ID: 16705691

DOI: 10.1002/humu.9423

PubMed ID: 16786509

Title: Mutation analysis of COL1A1 and COL1A2 in patients diagnosed with osteogenesis imperfecta type I-IV.

PubMed ID: 16786509

DOI: 10.1002/humu.9430

PubMed ID: 16566045

Title: Prenatal diagnosis of type II osteogenesis imperfecta, describing a new mutation in the COL1A1 gene.

PubMed ID: 16566045

DOI: 10.1002/pd.1428

PubMed ID: 16638323

Title: A new mutation in COL1A1 gene in a family with osteogenesis imperfecta.

PubMed ID: 16638323

PubMed ID: 17078022

Title: Consortium for osteogenesis imperfecta mutations in the helical domain of type I collagen: regions rich in lethal mutations align with collagen binding sites for integrins and proteoglycans.

PubMed ID: 17078022

DOI: 10.1002/humu.20429

PubMed ID: 17211858

Title: Three arginine to cysteine substitutions in the pro-alpha (I)-collagen chain cause Ehlers-Danlos syndrome with a propensity to arterial rupture in early adulthood.

PubMed ID: 17211858

DOI: 10.1002/humu.20455

PubMed ID: 17206620

Title: Y-position cysteine substitution in type I collagen (alpha1(I) R888C/p.R1066C) is associated with osteogenesis imperfecta/Ehlers-Danlos syndrome phenotype.

PubMed ID: 17206620

DOI: 10.1002/humu.20456

PubMed ID: 17875077

Title: Mutations in type I collagen genes in Japanese osteogenesis imperfecta patients.

PubMed ID: 17875077

DOI: 10.1111/j.1442-200x.2007.02422.x

PubMed ID: 18272325

Title: Natural variation in four human collagen genes across an ethnically diverse population.

PubMed ID: 18272325

DOI: 10.1016/j.ygeno.2007.12.008

PubMed ID: 18670065

Title: Two novel COL1A1 mutations in patients with osteogenesis imperfecta (OI) affect the stability of the collagen type I triple-helix.

PubMed ID: 18670065

DOI: 10.1007/bf03195625

PubMed ID: 18996919

Title: Mutation and polymorphism spectrum in osteogenesis imperfecta type II: implications for genotype-phenotype relationships.

PubMed ID: 18996919

DOI: 10.1093/hmg/ddn374

PubMed ID: 21239989

Title: Recurrence of perinatal lethal osteogenesis imperfecta in sibships: parsing the risk between parental mosaicism for dominant mutations and autosomal recessive inheritance.

PubMed ID: 21239989

DOI: 10.1097/gim.0b013e318202e0f6

PubMed ID: 21344539

Title: COL1 C-propeptide cleavage site mutations cause high bone mass osteogenesis imperfecta.

PubMed ID: 21344539

DOI: 10.1002/humu.21475

PubMed ID: 23692737

Title: Helical mutations in type I collagen that affect the processing of the amino-propeptide result in an Osteogenesis Imperfecta/Ehlers-Danlos Syndrome overlap syndrome.

PubMed ID: 23692737

DOI: 10.1186/1750-1172-8-78

PubMed ID: 25086671

Title: Targeted sequencing of a pediatric metabolic bone gene panel using a desktop semiconductor next-generation sequencer.

PubMed ID: 25086671

DOI: 10.1007/s00223-014-9897-9

PubMed ID: 24682174

Title: A novel mild variant of osteogenesis imperfecta type I caused by a Gly1088Glu mutation in COL1A1.

PubMed ID: 24682174

DOI: 10.3892/mmr.2014.2084

PubMed ID: 25958000

Title: Whole-exome sequencing identifies de novo mutation in the COL1A1 gene to underlie the severe osteogenesis imperfecta.

PubMed ID: 25958000

DOI: 10.1186/s40246-015-0028-0

PubMed ID: 27509835

Title: DNA sequence analysis in 598 individuals with a clinical diagnosis of osteogenesis imperfecta: diagnostic yield and mutation spectrum.

PubMed ID: 27509835

DOI: 10.1007/s00198-016-3709-1

Sequence Information:

Length: 1464
Mass: 138911
Checksum: B0581DAD2809DDE8
Sequence:

MFSFVDLRLL LLLAATALLT HGQEEGQVEG QDEDIPPITC VQNGLRYHDR DVWKPEPCRI 
CVCDNGKVLC DDVICDETKN CPGAEVPEGE CCPVCPDGSE SPTDQETTGV EGPKGDTGPR 
GPRGPAGPPG RDGIPGQPGL PGPPGPPGPP GPPGLGGNFA PQLSYGYDEK STGGISVPGP 
MGPSGPRGLP GPPGAPGPQG FQGPPGEPGE PGASGPMGPR GPPGPPGKNG DDGEAGKPGR 
PGERGPPGPQ GARGLPGTAG LPGMKGHRGF SGLDGAKGDA GPAGPKGEPG SPGENGAPGQ 
MGPRGLPGER GRPGAPGPAG ARGNDGATGA AGPPGPTGPA GPPGFPGAVG AKGEAGPQGP 
RGSEGPQGVR GEPGPPGPAG AAGPAGNPGA DGQPGAKGAN GAPGIAGAPG FPGARGPSGP 
QGPGGPPGPK GNSGEPGAPG SKGDTGAKGE PGPVGVQGPP GPAGEEGKRG ARGEPGPTGL 
PGPPGERGGP GSRGFPGADG VAGPKGPAGE RGSPGPAGPK GSPGEAGRPG EAGLPGAKGL 
TGSPGSPGPD GKTGPPGPAG QDGRPGPPGP PGARGQAGVM GFPGPKGAAG EPGKAGERGV 
PGPPGAVGPA GKDGEAGAQG PPGPAGPAGE RGEQGPAGSP GFQGLPGPAG PPGEAGKPGE 
QGVPGDLGAP GPSGARGERG FPGERGVQGP PGPAGPRGAN GAPGNDGAKG DAGAPGAPGS 
QGAPGLQGMP GERGAAGLPG PKGDRGDAGP KGADGSPGKD GVRGLTGPIG PPGPAGAPGD 
KGESGPSGPA GPTGARGAPG DRGEPGPPGP AGFAGPPGAD GQPGAKGEPG DAGAKGDAGP 
PGPAGPAGPP GPIGNVGAPG AKGARGSAGP PGATGFPGAA GRVGPPGPSG NAGPPGPPGP 
AGKEGGKGPR GETGPAGRPG EVGPPGPPGP AGEKGSPGAD GPAGAPGTPG PQGIAGQRGV 
VGLPGQRGER GFPGLPGPSG EPGKQGPSGA SGERGPPGPM GPPGLAGPPG ESGREGAPGA 
EGSPGRDGSP GAKGDRGETG PAGPPGAPGA PGAPGPVGPA GKSGDRGETG PAGPAGPVGP 
VGARGPAGPQ GPRGDKGETG EQGDRGIKGH RGFSGLQGPP GPPGSPGEQG PSGASGPAGP 
RGPPGSAGAP GKDGLNGLPG PIGPPGPRGR TGDAGPVGPP GPPGPPGPPG PPSAGFDFSF 
LPQPPQEKAH DGGRYYRADD ANVVRDRDLE VDTTLKSLSQ QIENIRSPEG SRKNPARTCR 
DLKMCHSDWK SGEYWIDPNQ GCNLDAIKVF CNMETGETCV YPTQPSVAQK NWYISKNPKD 
KRHVWFGESM TDGFQFEYGG QGSDPADVAI QLTFLRLMST EASQNITYHC KNSVAYMDQQ 
TGNLKKALLL QGSNEIEIRA EGNSRFTYSV TVDGCTSHTG AWGKTVIEYK TTKTSRLPII 
DVAPLDVGAP DQEFGFDVGP VCFL

	Overall overall
	Acute kidney failure MONDO0002492
	Adrenal gland UBERON0002369
	Ascending colon UBERON0001156
	Atherosclerosis MONDO0005311
	Axilla UBERON0009472
	\|— Axilla Breast cancer UBERON0009472_MONDO0007254
	Basal cell carcinoma MONDO0020804
	Bipolar I disorder MONDO0001866
	Body of stomach UBERON0001161
	Breast UBERON0000310
	\|— Breast Breast cancer UBERON0000310_MONDO0007254
	\|— Breast Healthy UBERON0000310_PATO0000461
	\|— Breast cancer MONDO0007254
	Caudate lobe of liver UBERON0001117
	Cerebellum UBERON0002037
	\|— Cerebellum Healthy UBERON0002037_PATO0000461
	Cerebral cortex UBERON0000956
	\|— Cerebral cortex Healthy UBERON0000956_PATO0000461
	Colon UBERON0001155
	\|— Colon Healthy UBERON0001155_PATO0000461
	Colorectal cancer MONDO0005575
	Colorectum UBERON0012652
	Cortex of kidney UBERON0001225
	\|— Cortex of kidney Healthy UBERON0001225_PATO0000461
	COVID-19 MONDO0100096
	Crohn disease MONDO0005011
	Dementia MONDO0001627
	Dental pulp UBERON0001754
	Dorsolateral prefrontal cortex UBERON0009834
	\|— Dorsolateral prefrontal cortex Bipolar I disorder UBERON0009834_MONDO0001866
	\|— Dorsolateral prefrontal cortex Dementia UBERON0009834_MONDO0001627
	\|— Dorsolateral prefrontal cortex Healthy UBERON0009834_PATO0000461
	\|— Dorsolateral prefrontal cortex Schizophrenia UBERON0009834_MONDO0005090
	Duodenum UBERON0002114
	\|— Duodenum Healthy UBERON0002114_PATO0000461
	Fallopian tube UBERON0003889
	Glioblastoma MONDO0018177
	Healthy PATO0000461
	Heart left ventricle UBERON0002084
	\|— Heart left ventricle Healthy UBERON0002084_PATO0000461
	Heart right ventricle UBERON0002080
	\|— Heart right ventricle Healthy UBERON0002080_PATO0000461
	Hippocampal formation UBERON0002421
	\|— Hippocampal formation Healthy UBERON0002421_PATO0000461
	Hypothalamus UBERON0001898
	\|— Hypothalamus Healthy UBERON0001898_PATO0000461
	Ileum UBERON0002116
	\|— Ileum Healthy UBERON0002116_PATO0000461
	Interventricular septum UBERON0002094
	Islet of Langerhans UBERON0000006
	Kidney UBERON0002113
	\|— Kidney Healthy UBERON0002113_PATO0000461
	Liver UBERON0002107
	\|— Liver Healthy UBERON0002107_PATO0000461
	Lung UBERON0002048
	\|— Lung Healthy UBERON0002048_PATO0000461
	\|— Lung Renal cell carcinoma UBERON0002048_MONDO0005086
	\|— Lung adenocarcinoma MONDO0005061
	\|— Lung parenchyma UBERON0008946
	Lymph node UBERON0000029
	Malignant ovarian serous tumor MONDO0024885
	Midbrain UBERON0001891
	\|— Midbrain Healthy UBERON0001891_PATO0000461
	Neuroblastoma MONDO0005072
	Nonpapillary renal cell carcinoma MONDO0007763
	Ovary UBERON0000992
	\|— Ovary Healthy UBERON0000992_PATO0000461
	Parkinson disease MONDO0005180
	Placenta UBERON0001987
	Pleural effusion UBERON0000175
	Pons UBERON0000988
	\|— Pons Healthy UBERON0000988_PATO0000461
	Renal cell carcinoma MONDO0005086
	Renal medulla UBERON0000362
	Right atrium auricular region UBERON0006631
	Schizophrenia MONDO0005090
	Sigmoid colon UBERON0001159
	Skin of body UBERON0002097
	Small cell lung carcinoma MONDO0008433
	Small intestine UBERON0002108
	\|— Small intestine Healthy UBERON0002108_PATO0000461
	Stomach UBERON0000945
	\|— Stomach Healthy UBERON0000945_PATO0000461
	Thalamic complex UBERON0010225
	\|— Thalamic complex Healthy UBERON0010225_PATO0000461
	UBERON0005290 UBERON0005290
	\|— UBERON0005290 Healthy UBERON0005290_PATO0000461
	UBERON8440012 UBERON8440012
	\|— UBERON8440012 Healthy UBERON8440012_PATO0000461
	Upper lobe of left lung UBERON0008952

Details for: COL1A1

Cell Significance Landscape

Associated with

Significant Cells

Network Configuration

Legend:

Other Information

Analysis of the COL1A1 and COL1A2 genes by PCR amplification and scanning by conformation-sensitive gel electrophoresis identifies only COL1A1 mutations in 15 patients with osteogenesis imperfecta type I: identification of common sequences of null-allele mutations. PubMed ID: 9443882

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Complete nucleotide sequence of the region encompassing the first twenty-five exons of the human pro alpha 1(I) collagen gene (COL1A1). PubMed ID: 2843432

Structure of a full-length cDNA clone for the prepro alpha 1(I) chain of human type I procollagen. PubMed ID: 3178743

Human pro alpha 1(I) collagen gene structure reveals evolutionary conservation of a pattern of introns and exons. PubMed ID: 6462220

DNA sequences in the first intron of the human pro-alpha 1(I) collagen gene enhance transcription. PubMed ID: 2822714

Fine structural analysis of the human pro-alpha 1 (I) collagen gene. Promoter structure, AluI repeats, and polymorphic transcripts. PubMed ID: 2857713

Regulatory elements in the first intron contribute to transcriptional control of the human alpha 1(I) collagen gene. PubMed ID: 3480516

In vivo and in vitro noncovalent association of excised alpha 1 (I) amino-terminal propeptides with mutant pN alpha 2(I) collagen chains in native mutant collagen in a case of Ehlers-Danlos syndrome, type VII. PubMed ID: 2318855

A base substitution in the exon of a collagen gene causes alternative splicing and generates a structurally abnormal polypeptide in a patient with Ehlers-Danlos syndrome type VII. PubMed ID: 2767050

Isolation and characterization of the cyanogen bromide peptides from the alpha 1 and alpha 2 chains of human skin collagen. PubMed ID: 5529814

A critical crosslink region in human-bone-derived collagen type I. Specific cleavage site at residue Leu95. PubMed ID: 2169412

A comparative study of glycopeptides derived from selected vertebrate collagens. A possible role of the carbohydrate in fibril formation. PubMed ID: 4319110

Segmental amplification of the entire helical and telopeptide regions of the cDNA for human alpha 1 (I) collagen. PubMed ID: 2374517

Nucleotide sequences of complementary deoxyribonucleic acids for the pro alpha 1 chain of human type I procollagen. Statistical evaluation of structures that are conserved during evolution. PubMed ID: 6689127

Cloning and characterization of five overlapping cDNAs specific for the human pro alpha 1(I) collagen chain. PubMed ID: 6183642

Multiexon deletion in an osteogenesis imperfecta variant with increased type III collagen mRNA. PubMed ID: 2981843

Intron-mediated recombination may cause a deletion in an alpha 1 type I collagen chain in a lethal form of osteogenesis imperfecta. PubMed ID: 3857621

Variable expression of osteogenesis imperfecta in a nuclear family is explained by somatic mosaicism for a lethal point mutation in the alpha 1(I) gene (COL1A1) of type I collagen in a parent. PubMed ID: 2339700

Severe (type III) osteogenesis imperfecta due to glycine substitutions in the central domain of the collagen triple helix. PubMed ID: 7881420

Mutations in the carboxyl-terminal propeptide of the pro alpha 1(I) chain of type I collagen result in defective chain association and produce lethal osteogenesis imperfecta. PubMed ID: 8349697

Substitution of cysteine for glycine within the carboxyl-terminal telopeptide of the alpha 1 chain of type I collagen produces mild osteogenesis imperfecta. PubMed ID: 3170557

Human pro alpha 1(I) collagen: cDNA sequence for the C-propeptide domain. PubMed ID: 3340531

Frameshift mutation near the 3' end of the COL1A1 gene of type I collagen predicts an elongated Pro alpha 1(I) chain and results in osteogenesis imperfecta type I. PubMed ID: 2295701

Highly conserved sequences in the 3'-untranslated region of the COL1A1 gene bind cell-specific nuclear proteins. PubMed ID: 1995349

Mutations in collagen genes: causes of rare and some common diseases in humans. PubMed ID: 2010058

Ehlers-Danlos syndrome type VIIA and VIIB result from splice-junction mutations or genomic deletions that involve exon 6 in the COL1A1 and COL1A2 genes of type I collagen. PubMed ID: 9295084

Mutations in fibrillar collagens (types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels. PubMed ID: 9101290

Osteogenesis imperfecta: translation of mutation to phenotype. PubMed ID: 1895312

TRAM2 protein interacts with endoplasmic reticulum Ca2+ pump Serca2b and is necessary for collagen type I synthesis. PubMed ID: 14749390

The arthrochalasia type of Ehlers-Danlos syndrome (EDS VIIA and VIIB): the diagnostic value of collagen fibril ultrastructure. PubMed ID: 18409203

Resveratrol-induced changes of the human adipocyte secretion profile. PubMed ID: 22905912

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Lethal osteogenesis imperfecta resulting from a single nucleotide change in one human pro alpha 1(I) collagen allele. PubMed ID: 3016737

Lethal perinatal osteogenesis imperfecta due to the substitution of arginine for glycine at residue 391 of the alpha 1(I) chain of type I collagen. PubMed ID: 3108247

A point mutation in a type I procollagen gene converts glycine 748 of the alpha 1 chain to cysteine and destabilizes the triple helix in a lethal variant of osteogenesis imperfecta. PubMed ID: 3667599

Substitution of arginine for glycine 664 in the collagen alpha 1(I) chain in lethal perinatal osteogenesis imperfecta. Demonstration of the peptide defect by in vitro expression of the mutant cDNA. PubMed ID: 3403550

A cysteine for glycine substitution at position 1017 in an alpha 1(I) chain of type I collagen in a patient with mild dominantly inherited osteogenesis imperfecta. PubMed ID: 3244312

RNA sequence analysis of a perinatal lethal osteogenesis imperfecta mutation. PubMed ID: 2470760

Osteogenesis imperfecta type IV. Detection of a point mutation in one alpha 1(I) collagen allele (COL1A1) by RNA/RNA hybrid analysis. PubMed ID: 2745420

Characterization of point mutations in the collagen COL1A1 and COL1A2 genes causing lethal perinatal osteogenesis imperfecta. PubMed ID: 2777764

Substitution of serine for alpha 1(I)-glycine 844 in a severe variant of osteogenesis imperfecta minimally destabilizes the triple helix of type I procollagen. The effects of glycine substitutions on thermal stability are either position of amino acid specific. PubMed ID: 2511192

A lethal variant of osteogenesis imperfecta has a single base mutation that substitutes cysteine for glycine 904 of the alpha 1(I) chain of type I procollagen. The asymptomatic mother has an unidentified mutation producing an overmodified and unstable type I procollagen. PubMed ID: 2913053

Osteogenesis imperfecta. The position of substitution for glycine by cysteine in the triple helical domain of the pro alpha 1(I) chains of type I collagen determines the clinical phenotype. PubMed ID: 2794057

Mutations that substitute serine for glycine alpha 1-598 and glycine alpha 1-631 in type I procollagen. The effects on thermal unfolding of the triple helix are position-specific and demonstrate that the protein unfolds through a series of cooperative blocks. PubMed ID: 2116413

Substitution of arginine for glycine at position 847 in the triple-helical domain of the alpha 1 (I) chain of type I collagen produces lethal osteogenesis imperfecta. Molecules that contain one or two abnormal chains differ in stability and secretion. PubMed ID: 2211725

A single base mutation in type I procollagen (COL1A1) that converts glycine alpha 1-541 to aspartate in a lethal variant of osteogenesis imperfecta: detection of the mutation with a carbodiimide reaction of DNA heteroduplexes and direct sequencing of products of the PCR. PubMed ID: 2035536

Substitution of cysteine for glycine-alpha 1-691 in the pro alpha 1(I) chain of type I procollagen in a proband with lethal osteogenesis imperfecta destabilizes the triple helix at a site C-terminal to the substitution. PubMed ID: 1953667

A type I collagen with substitution of a cysteine for glycine-748 in the alpha 1(I) chain copolymerizes with normal type I collagen and can generate fractallike structures. PubMed ID: 2036375

Osteogenesis imperfecta due to recurrent point mutations at CpG dinucleotides in the COL1A1 gene of type I collagen. PubMed ID: 2037280

A de novo G to T transversion in a pro-alpha 1 (I) collagen gene for a moderate case of osteogenesis imperfecta. Substitution of cysteine for glycine 178 in the triple helical domain. PubMed ID: 1988452

Substitutions for glycine alpha 1-637 and glycine alpha 2-694 of type I procollagen in lethal osteogenesis imperfecta. The conformational strain on the triple helix introduced by a glycine substitution can be transmitted along the helix. PubMed ID: 1874719

The substitution of arginine for glycine 85 of the alpha 1(I) procollagen chain results in mild osteogenesis imperfecta. The mutation provides direct evidence for three discrete domains of cooperative melting of intact type I collagen. PubMed ID: 1718984

A 9-base pair deletion in COL1A1 in a lethal variant of osteogenesis imperfecta. PubMed ID: 1939261

Substitution of cysteine for glycine at residue 415 of one allele of the alpha 1(I) chain of type I procollagen in type III/IV osteogenesis imperfecta. PubMed ID: 1770532

G to A polymorphism in exon 45 of the COL1A1 gene. PubMed ID: 1870989

Characterization of three osteogenesis imperfecta collagen alpha 1(I) glycine to serine mutations demonstrating a position-dependent gradient of phenotypic severity. PubMed ID: 1445258

Type I procollagens containing substitutions of aspartate, arginine, and cysteine for glycine in the pro alpha 1 (I) chain are cleaved slowly by N-proteinase, but only the cysteine substitution introduces a kink in the molecule. PubMed ID: 1460046

Mild dominant osteogenesis imperfecta with intrafamilial variability: the cause is a serine for glycine alpha 1(I) 901 substitution in a type-I collagen gene. PubMed ID: 1634225

A dominant mutation in the COL1A1 gene that substitutes glycine for valine causes recurrent lethal osteogenesis imperfecta. PubMed ID: 1511982

A tripeptide deletion in the triple-helical domain of the pro alpha 1(I) chain of type I procollagen in a patient with lethal osteogenesis imperfecta does not alter cleavage of the molecule by N-proteinase. PubMed ID: 1460047

An osteopenic nonfracture syndrome with features of mild osteogenesis imperfecta associated with the substitution of a cysteine for glycine at triple helix position 43 in the pro alpha 1(I) chain of type I collagen. PubMed ID: 1737847

The clinicopathological features of three babies with osteogenesis imperfecta resulting from the substitution of glycine by valine in the pro alpha 1 (I) chain of type I procollagen. PubMed ID: 1613761

Chemical cleavage method for the detection of RNA base changes: experience in the application to collagen mutations in osteogenesis imperfecta. PubMed ID: 8456808

Moderately severe osteogenesis imperfecta associated with substitutions of serine for glycine in the alpha 1(I) chain of type I collagen. PubMed ID: 8456809

A cysteine for glycine substitution at position 175 in an alpha 1 (I) chain of type I collagen produces a clinically heterogeneous form of osteogenesis imperfecta. PubMed ID: 8339541

Osteogenesis imperfecta and type-I collagen mutations. A lethal variant caused by a Gly910--&gt;Ala substitution in the alpha 1 (I) chain. PubMed ID: 7679635

Gly85 to Val substitution in pro alpha 1(I) chain causes mild osteogenesis imperfecta and introduces a susceptibility to protease digestion. PubMed ID: 8223589

SSCP detection of a Gly565Val substitution in the pro alpha 1(I) collagen chain resulting in osteogenesis imperfecta type II. PubMed ID: 8100209

An RT-PCR-SSCP screening strategy for detection of mutations in the gene encoding the alpha 1 chain of type I collagen: application to four patients with osteogenesis imperfecta. PubMed ID: 7691343

Paternal mosaicism for a COL1A1 dominant mutation (alpha 1 Ser-415) causes recurrent osteogenesis imperfecta. PubMed ID: 8364588

Serine for glycine substitutions in type I collagen in two cases of type IV osteogenesis imperfecta (OI). Additional evidence for a regional model of OI pathophysiology. PubMed ID: 8094076

BiP binds type I procollagen pro alpha chains with mutations in the carboxyl-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta. PubMed ID: 8349698