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Chymosin (English Wikipedia)

Analysis of information sources in references of the Wikipedia article "Chymosin" in English language version.

refsWebsite
Global rank English rank
11nih.gov
4th place
4th place
10doi.org
2nd place
2nd place
2rcsb.org
8,838th place
8,783rd place
2books.google.com
3rd place
3rd place
1oup.com
485th place
440th place
1semanticscholar.org
11th place
8th place
1omim.org
4,380th place
4,305th place
1researchgate.net
120th place
125th place
1harvard.edu
18th place
17th place
1web.archive.org
1st place
1st place
1gmo-compass.org
low place
low place
1wiley.com
222nd place
297th place
1state.gov
264th place
249th place

books.google.com

doi.org

  • PDB: 1CZI​; Groves MR, Dhanaraj V, Badasso M, Nugent P, Pitts JE, Hoover DJ, Blundell TL (October 1998). "A 2.3 A resolution structure of chymosin complexed with a reduced bond inhibitor shows that the active site beta-hairpin flap is rearranged when compared with the native crystal structure" (PDF). Protein Engineering. 11 (10): 833–40. doi:10.1093/protein/11.10.833. PMID 9862200.
  • Lopes-Marques M, Ruivo R, Fonseca E, Teixeira A, Castro LF (November 2017). "Unusual loss of chymosin in mammalian lineages parallels neo-natal immune transfer strategies". Molecular Phylogenetics and Evolution. 116: 78–86. doi:10.1016/j.ympev.2017.08.014. PMID 28851538.
  • Kitamura N, Tanimoto A, Hondo E, Andrén A, Cottrell DF, Sasaki M, Yamada J (August 2001). "Immunohistochemical study of the ontogeny of prochymosin--and pepsinogen-producing cells in the abomasum of sheep". Anatomia, Histologia, Embryologia. 30 (4): 231–5. doi:10.1046/j.1439-0264.2001.00326.x. PMID 11534329. S2CID 7552821.
  • Henschel MJ, Newport MJ, Parmar V (1987). "Gastric proteases in the human infant". Biology of the Neonate. 52 (5): 268–72. doi:10.1159/000242719. PMID 3118972.
  • Szecsi PB, Harboe M (2013). "Chapter 5: Chymosin". In Rawlings ND, Salvesen G (eds.). Handbook of Proteolytic Enzymes. Vol. 1. pp. 37–42. doi:10.1016/B978-0-12-382219-2.00005-3.
  • Gilliland GL, Oliva MT, Dill J (1991). "Functional Implications of the Three-Dimensional Structure of Bovine Chymosin". Structure and Function of the Aspartic Proteinases. Advances in Experimental Medicine and Biology. Vol. 306. pp. 23–37. doi:10.1007/978-1-4684-6012-4_3. ISBN 978-1-4684-6014-8. PMID 1812710.
  • PDB: 4CMS​; Newman M, Safro M, Frazao C, Khan G, Zdanov A, Tickle IJ, et al. (October 1991). "X-ray analyses of aspartic proteinases. IV. Structure and refinement at 2.2 A resolution of bovine chymosin". Journal of Molecular Biology. 221 (4): 1295–309. doi:10.1016/0022-2836(91)90934-X. PMID 1942052.
  • Emtage JS, Angal S, Doel MT, Harris TJ, Jenkins B, Lilley G, Lowe PA (June 1983). "Synthesis of calf prochymosin (prorennin) in Escherichia coli". Proceedings of the National Academy of Sciences of the United States of America. 80 (12): 3671–5. Bibcode:1983PNAS...80.3671E. doi:10.1073/pnas.80.12.3671. PMC 394112. PMID 6304731.
  • Harris TJ, Lowe PA, Lyons A, Thomas PG, Eaton MA, Millican TA, et al. (April 1982). "Molecular cloning and nucleotide sequence of cDNA coding for calf preprochymosin". Nucleic Acids Research. 10 (7): 2177–87. doi:10.1093/nar/10.7.2177. PMC 320601. PMID 6283469.
  • Johnson ME, Lucey JA (April 2006). "Major technological advances and trends in cheese". Journal of Dairy Science. 89 (4): 1174–8. doi:10.3168/jds.S0022-0302(06)72186-5. PMID 16537950.

gmo-compass.org

harvard.edu

ui.adsabs.harvard.edu

nih.gov

pubmed.ncbi.nlm.nih.gov

  • PDB: 1CZI​; Groves MR, Dhanaraj V, Badasso M, Nugent P, Pitts JE, Hoover DJ, Blundell TL (October 1998). "A 2.3 A resolution structure of chymosin complexed with a reduced bond inhibitor shows that the active site beta-hairpin flap is rearranged when compared with the native crystal structure" (PDF). Protein Engineering. 11 (10): 833–40. doi:10.1093/protein/11.10.833. PMID 9862200.
  • Lopes-Marques M, Ruivo R, Fonseca E, Teixeira A, Castro LF (November 2017). "Unusual loss of chymosin in mammalian lineages parallels neo-natal immune transfer strategies". Molecular Phylogenetics and Evolution. 116: 78–86. doi:10.1016/j.ympev.2017.08.014. PMID 28851538.
  • Kitamura N, Tanimoto A, Hondo E, Andrén A, Cottrell DF, Sasaki M, Yamada J (August 2001). "Immunohistochemical study of the ontogeny of prochymosin--and pepsinogen-producing cells in the abomasum of sheep". Anatomia, Histologia, Embryologia. 30 (4): 231–5. doi:10.1046/j.1439-0264.2001.00326.x. PMID 11534329. S2CID 7552821.
  • Henschel MJ, Newport MJ, Parmar V (1987). "Gastric proteases in the human infant". Biology of the Neonate. 52 (5): 268–72. doi:10.1159/000242719. PMID 3118972.
  • Gilliland GL, Oliva MT, Dill J (1991). "Functional Implications of the Three-Dimensional Structure of Bovine Chymosin". Structure and Function of the Aspartic Proteinases. Advances in Experimental Medicine and Biology. Vol. 306. pp. 23–37. doi:10.1007/978-1-4684-6012-4_3. ISBN 978-1-4684-6014-8. PMID 1812710.
  • PDB: 4CMS​; Newman M, Safro M, Frazao C, Khan G, Zdanov A, Tickle IJ, et al. (October 1991). "X-ray analyses of aspartic proteinases. IV. Structure and refinement at 2.2 A resolution of bovine chymosin". Journal of Molecular Biology. 221 (4): 1295–309. doi:10.1016/0022-2836(91)90934-X. PMID 1942052.
  • Emtage JS, Angal S, Doel MT, Harris TJ, Jenkins B, Lilley G, Lowe PA (June 1983). "Synthesis of calf prochymosin (prorennin) in Escherichia coli". Proceedings of the National Academy of Sciences of the United States of America. 80 (12): 3671–5. Bibcode:1983PNAS...80.3671E. doi:10.1073/pnas.80.12.3671. PMC 394112. PMID 6304731.
  • Harris TJ, Lowe PA, Lyons A, Thomas PG, Eaton MA, Millican TA, et al. (April 1982). "Molecular cloning and nucleotide sequence of cDNA coding for calf preprochymosin". Nucleic Acids Research. 10 (7): 2177–87. doi:10.1093/nar/10.7.2177. PMC 320601. PMID 6283469.
  • Johnson ME, Lucey JA (April 2006). "Major technological advances and trends in cheese". Journal of Dairy Science. 89 (4): 1174–8. doi:10.3168/jds.S0022-0302(06)72186-5. PMID 16537950.

ncbi.nlm.nih.gov

omim.org

oup.com

academic.oup.com

  • PDB: 1CZI​; Groves MR, Dhanaraj V, Badasso M, Nugent P, Pitts JE, Hoover DJ, Blundell TL (October 1998). "A 2.3 A resolution structure of chymosin complexed with a reduced bond inhibitor shows that the active site beta-hairpin flap is rearranged when compared with the native crystal structure" (PDF). Protein Engineering. 11 (10): 833–40. doi:10.1093/protein/11.10.833. PMID 9862200.

rcsb.org

  • PDB: 1CZI​; Groves MR, Dhanaraj V, Badasso M, Nugent P, Pitts JE, Hoover DJ, Blundell TL (October 1998). "A 2.3 A resolution structure of chymosin complexed with a reduced bond inhibitor shows that the active site beta-hairpin flap is rearranged when compared with the native crystal structure" (PDF). Protein Engineering. 11 (10): 833–40. doi:10.1093/protein/11.10.833. PMID 9862200.
  • PDB: 4CMS​; Newman M, Safro M, Frazao C, Khan G, Zdanov A, Tickle IJ, et al. (October 1991). "X-ray analyses of aspartic proteinases. IV. Structure and refinement at 2.2 A resolution of bovine chymosin". Journal of Molecular Biology. 221 (4): 1295–309. doi:10.1016/0022-2836(91)90934-X. PMID 1942052.

researchgate.net

semanticscholar.org

api.semanticscholar.org

  • Kitamura N, Tanimoto A, Hondo E, Andrén A, Cottrell DF, Sasaki M, Yamada J (August 2001). "Immunohistochemical study of the ontogeny of prochymosin--and pepsinogen-producing cells in the abomasum of sheep". Anatomia, Histologia, Embryologia. 30 (4): 231–5. doi:10.1046/j.1439-0264.2001.00326.x. PMID 11534329. S2CID 7552821.

state.gov

fpc.state.gov

web.archive.org

wiley.com

eu.wiley.com