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Table representation of search results timeline featuring number of search results per year.

Year Number of Results
1902 2
1914 1
1923 1
1925 1
1928 1
1929 1
1931 2
1932 3
1933 2
1938 2
1940 2
1942 1
1944 1
1945 9
1946 1
1947 14
1948 15
1949 24
1950 46
1951 76
1952 82
1953 110
1954 96
1955 138
1956 153
1957 165
1958 174
1959 144
1960 176
1961 228
1962 242
1963 410
1964 595
1965 507
1966 542
1967 666
1968 829
1969 915
1970 1027
1971 1080
1972 1237
1973 1171
1974 1340
1975 1539
1976 1455
1977 1427
1978 1503
1979 1552
1980 1741
1981 1777
1982 1803
1983 2003
1984 2264
1985 2308
1986 2514
1987 2407
1988 2729
1989 3105
1990 3312
1991 3522
1992 3610
1993 3669
1994 3814
1995 3930
1996 4110
1997 4148
1998 4214
1999 4382
2000 4655
2001 4862
2002 5131
2003 5455
2004 6008
2005 6586
2006 6810
2007 7209
2008 7679
2009 7962
2010 8522
2011 9343
2012 9733
2013 10295
2014 10364
2015 10670
2016 10504
2017 10739
2018 10877
2019 11128
2020 11810
2021 12410
2022 11844
2023 11455
2024 4410

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271,078 results

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The following term was not found in PubMed: PG-hydrolyzed
Page 1
Collagen glycosylation.
Hennet T. Hennet T. Curr Opin Struct Biol. 2019 Jun;56:131-138. doi: 10.1016/j.sbi.2019.01.015. Epub 2019 Feb 26. Curr Opin Struct Biol. 2019. PMID: 30822656 Review.
The extent of collagen glycosylation varies by the types of collagen, with basement membrane collagen type IV being more glycosylated than fibrillar collagens. Beyond true collagens, proteins including collagen domains such as the complem …
The extent of collagen glycosylation varies by the types of collagen, with basement membrane collagen type IV being mor …
The collagen family.
Ricard-Blum S. Ricard-Blum S. Cold Spring Harb Perspect Biol. 2011 Jan 1;3(1):a004978. doi: 10.1101/cshperspect.a004978. Cold Spring Harb Perspect Biol. 2011. PMID: 21421911 Free PMC article. Review.
Collagens are the most abundant proteins in mammals. The collagen family comprises 28 members that contain at least one triple-helical domain. Collagens are deposited in the extracellular matrix where most of them form supramolecular assemblies. ...
Collagens are the most abundant proteins in mammals. The collagen family comprises 28 members that contain at least one triple …
The Collagen Suprafamily: From Biosynthesis to Advanced Biomaterial Development.
Sorushanova A, Delgado LM, Wu Z, Shologu N, Kshirsagar A, Raghunath R, Mullen AM, Bayon Y, Pandit A, Raghunath M, Zeugolis DI. Sorushanova A, et al. Adv Mater. 2019 Jan;31(1):e1801651. doi: 10.1002/adma.201801651. Epub 2018 Aug 20. Adv Mater. 2019. PMID: 30126066 Review.
First, an overview of the family of collagens and their respective structures, conformation, and biosynthesis is provided. The advances and shortfalls of various collagen preparations (e.g., mammalian/marine extracted collagen, cell-produced collagens, …
First, an overview of the family of collagens and their respective structures, conformation, and biosynthesis is provided. The advanc …
Collagens--structure, function, and biosynthesis.
Gelse K, Pöschl E, Aigner T. Gelse K, et al. Adv Drug Deliv Rev. 2003 Nov 28;55(12):1531-46. doi: 10.1016/j.addr.2003.08.002. Adv Drug Deliv Rev. 2003. PMID: 14623400 Review.
The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified so …
The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and variou …
Mechanochemistry of collagen.
Siadat SM, Ruberti JW. Siadat SM, et al. Acta Biomater. 2023 Jun;163:50-62. doi: 10.1016/j.actbio.2023.01.025. Epub 2023 Jan 17. Acta Biomater. 2023. PMID: 36669548 Review.
In animals, cells produce fibril-forming collagen molecules that self-assemble into larger structures known as collagen fibrils. ...In this perspective, we examine the known role of mechanical force on the formation and development of collagenous structure. W …
In animals, cells produce fibril-forming collagen molecules that self-assemble into larger structures known as collagen fibril …
Collagen for bone tissue regeneration.
Ferreira AM, Gentile P, Chiono V, Ciardelli G. Ferreira AM, et al. Acta Biomater. 2012 Sep;8(9):3191-200. doi: 10.1016/j.actbio.2012.06.014. Epub 2012 Jun 15. Acta Biomater. 2012. PMID: 22705634 Review.
In the last decades, increased knowledge about the organization, structure and properties of collagen (particularly concerning interactions between cells and collagen-based materials) has inspired scientists and engineers to design innovative collagen-based b …
In the last decades, increased knowledge about the organization, structure and properties of collagen (particularly concerning intera …
Collagens.
Gordon MK, Hahn RA. Gordon MK, et al. Cell Tissue Res. 2010 Jan;339(1):247-57. doi: 10.1007/s00441-009-0844-4. Epub 2009 Aug 20. Cell Tissue Res. 2010. PMID: 19693541 Free PMC article. Review.
The collagens represent a family of trimeric extracellular matrix molecules used by cells for structural integrity and other functions. ...This review highlights some of the structural characteristics of collagen types I-XXVIII....
The collagens represent a family of trimeric extracellular matrix molecules used by cells for structural integrity and other function …
[An overview of the beneficial effects of hydrolysed collagen intake on joint and bone health and on skin ageing].
Figueres Juher T, Basés Pérez E. Figueres Juher T, et al. Nutr Hosp. 2015 Jul 18;32 Suppl 1:62-6. doi: 10.3305/nh.2015.32.sup1.9482. Nutr Hosp. 2015. PMID: 26267777 Free article. Review. Spanish.
INTRODUCTION: Hydrolysate Collagen (HC) consists of small peptides with a molecular weight lower than 5.000 Da. produced from gelatinization and subsequent enzymatic hydrolysis of native collagen which is found in rich collagenic animal tissues. ...CONCLUSION …
INTRODUCTION: Hydrolysate Collagen (HC) consists of small peptides with a molecular weight lower than 5.000 Da. produced from gelatin …
Structure, physiology, and biochemistry of collagens.
Mienaltowski MJ, Birk DE. Mienaltowski MJ, et al. Adv Exp Med Biol. 2014;802:5-29. doi: 10.1007/978-94-007-7893-1_2. Adv Exp Med Biol. 2014. PMID: 24443018 Review.
The hierarchical structure of tendon and its functional properties are determined by the collagens present, as well as their supramolecular organization. There are 28 different types of collagen that assemble into a variety of supramolecular structures. ...The gener …
The hierarchical structure of tendon and its functional properties are determined by the collagens present, as well as their supramol …
Molecular structure of the collagen triple helix.
Brodsky B, Persikov AV. Brodsky B, et al. Adv Protein Chem. 2005;70:301-39. doi: 10.1016/S0065-3233(05)70009-7. Adv Protein Chem. 2005. PMID: 15837519 Review.
The molecular conformation of the collagen triple helix confers strict amino acid sequence constraints, requiring a (Gly-X-Y)(n) repeating pattern and a high content of imino acids. The increasing family of collagens and proteins with collagenous domains show …
The molecular conformation of the collagen triple helix confers strict amino acid sequence constraints, requiring a (Gly-X-Y)(n) repe …
271,078 results
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