메뉴 건너뛰기




Volumn 119, Issue SUPPL.1, 2011, Pages 234-240

Characterization of kallikrein-related peptidase 4 glycosylations

Author keywords

Enamel; Glycosylations; Kallikrein 4; Serine proteases; Sialic acid

Indexed keywords

ENAMEL PROTEIN; KALLIKREIN; KALLIKREIN 4; N ACETYLNEURAMINIC ACID; POLYSACCHARIDE; RECOMBINANT PROTEIN;

EID: 84862970062     PISSN: 09098836     EISSN: 16000722     Source Type: Journal    
DOI: 10.1111/j.1600-0722.2011.00863.x     Document Type: Article
Times cited : (13)

References (34)
  • 3
    • 84862972201 scopus 로고    scopus 로고
    • Expression of kallikrein 4 (Klk4) in dental and non-dental tissues
    • Simmer J, Richardson A, Smith C, Hu Y, Hu J-C. Expression of kallikrein 4 (Klk4) in dental and non-dental tissues. Eur J Oral Sci 2011; 119 (Suppl. 1): 226-233.
    • (2011) Eur J Oral Sci , vol.119 , Issue.SUPPL. 1 , pp. 226-233
    • Simmer, J.1    Richardson, A.2    Smith, C.3    Hu, Y.4    Hu, J.-C.5
  • 4
    • 67650529834 scopus 로고    scopus 로고
    • Hypomaturation enamel defects in Klk4 knockout/LacZ knockin mice
    • Simmer JP, Hu Y, Lertlam R, Yamakoshi Y, Hu JC. Hypomaturation enamel defects in Klk4 knockout/LacZ knockin mice. J Biol Chem 2009; 284: 19110-19121.
    • (2009) J Biol Chem , vol.284 , pp. 19110-19121
    • Simmer, J.P.1    Hu, Y.2    Lertlam, R.3    Yamakoshi, Y.4    Hu, J.C.5
  • 6
    • 79955962728 scopus 로고    scopus 로고
    • Effect of kallikrein 4 Loss on enamel mineralization: comparison with mice lacking matrix metalloproteinase 20
    • Smith CE, Richardson AS, Hu Y, Bartlett JD, Hu JC, Simmer JP. Effect of kallikrein 4 Loss on enamel mineralization: comparison with mice lacking matrix metalloproteinase 20. J Biol Chem 2011; 286: 18149-18160.
    • (2011) J Biol Chem , vol.286 , pp. 18149-18160
    • Smith, C.E.1    Richardson, A.S.2    Hu, Y.3    Bartlett, J.D.4    Hu, J.C.5    Simmer, J.P.6
  • 7
    • 80051801061 scopus 로고    scopus 로고
    • Why Does Enamel in Klk4 Null Mice Break Above the Dentino-Enamel Junction?
    • Simmer J, Hu Y, Richardson A, Bartlett J, Hu JC-C. Why Does Enamel in Klk4 Null Mice Break Above the Dentino-Enamel Junction? Cells Tissues Organs 2011; 194: 211-215.
    • (2011) Cells Tissues Organs , vol.194 , pp. 211-215
    • Simmer, J.1    Hu, Y.2    Richardson, A.3    Bartlett, J.4    Hu, J.-C.5
  • 11
    • 0033566020 scopus 로고    scopus 로고
    • Glycoproteins: glycan presentation and protein-fold stability
    • Wormald MR, Dwek RA. Glycoproteins: glycan presentation and protein-fold stability. Structure 1999; 7: R155-R160.
    • (1999) Structure , vol.7
    • Wormald, M.R.1    Dwek, R.A.2
  • 13
    • 78650401291 scopus 로고    scopus 로고
    • Congenital disorders of glycosylation
    • Jaeken J. Congenital disorders of glycosylation. Ann N Y Acad Sci 2010; 1214: 190-198.
    • (2010) Ann N Y Acad Sci , vol.1214 , pp. 190-198
    • Jaeken, J.1
  • 14
    • 79961171857 scopus 로고    scopus 로고
    • Mouse models for congenital disorders of glycosylation
    • Thiel C, Korner C. Mouse models for congenital disorders of glycosylation. J Inherit Metab Dis 2011; 34: 879-889.
    • (2011) J Inherit Metab Dis , vol.34 , pp. 879-889
    • Thiel, C.1    Korner, C.2
  • 17
    • 0024336222 scopus 로고
    • Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases
    • Maley F, Trimble RB, Tarentino AL, Plummer TH Jr. Characterization of glycoproteins and their associated oligosaccharides through the use of endoglycosidases. Anal Biochem 1989; 180: 195-204.
    • (1989) Anal Biochem , vol.180 , pp. 195-204
    • Maley, F.1    Trimble, R.B.2    Tarentino, A.L.3    Plummer Jr., T.H.4
  • 19
    • 0029079604 scopus 로고
    • Molecular mechanisms of dental enamel formation
    • Simmer JP, Fincham AG. Molecular mechanisms of dental enamel formation. Crit Rev Oral Biol Med 1995; 6: 84-108.
    • (1995) Crit Rev Oral Biol Med , vol.6 , pp. 84-108
    • Simmer, J.P.1    Fincham, A.G.2
  • 20
    • 0031968437 scopus 로고    scopus 로고
    • Cellular and chemical events during enamel maturation
    • Smith CE. Cellular and chemical events during enamel maturation. Crit Rev Oral Biol Med 1998; 9: 128-161.
    • (1998) Crit Rev Oral Biol Med , vol.9 , pp. 128-161
    • Smith, C.E.1
  • 21
    • 0033617953 scopus 로고    scopus 로고
    • The structural biology of the developing dental enamel matrix
    • Fincham AG, Moradian-Oldak J, Simmer JP. The structural biology of the developing dental enamel matrix. J Struct Biol 1999; 126: 270-299.
    • (1999) J Struct Biol , vol.126 , pp. 270-299
    • Fincham, A.G.1    Moradian-Oldak, J.2    Simmer, J.P.3
  • 25
    • 0034786105 scopus 로고    scopus 로고
    • Calcium binding of enamel proteins and their derivatives with emphasis on the calcium-binding domain of porcine sheathlin
    • Yamakoshi Y, Tanabe T, Oida S, Hu CC, Simmer JP, Fukae M. Calcium binding of enamel proteins and their derivatives with emphasis on the calcium-binding domain of porcine sheathlin. Arch Oral Biol 2001; 46: 1005-1014.
    • (2001) Arch Oral Biol , vol.46 , pp. 1005-1014
    • Yamakoshi, Y.1    Tanabe, T.2    Oida, S.3    Hu, C.C.4    Simmer, J.P.5    Fukae, M.6
  • 27
    • 0025176587 scopus 로고
    • Properties of phosphorylated 32 kd nonamelogenin proteins isolated from porcine secretory enamel
    • Tanabe T, Aoba T, Moreno EC, Fukae M, Shimizu M. Properties of phosphorylated 32 kd nonamelogenin proteins isolated from porcine secretory enamel. Calcif Tissue Int 1990; 46: 205-215.
    • (1990) Calcif Tissue Int , vol.46 , pp. 205-215
    • Tanabe, T.1    Aoba, T.2    Moreno, E.C.3    Fukae, M.4    Shimizu, M.5
  • 28
    • 77955931465 scopus 로고    scopus 로고
    • The enamelin genes in lizard, crocodile, and frog and the pseudogene in the chicken provide new insights on enamelin evolution in tetrapods
    • Al-Hashimi N, Lafont AG, Delgado S, Kawasaki K, Sire JY. The enamelin genes in lizard, crocodile, and frog and the pseudogene in the chicken provide new insights on enamelin evolution in tetrapods. Mol Biol Evol 2010; 27: 2078-2094.
    • (2010) Mol Biol Evol , vol.27 , pp. 2078-2094
    • Al-Hashimi, N.1    Lafont, A.G.2    Delgado, S.3    Kawasaki, K.4    Sire, J.Y.5
  • 29
    • 72449159548 scopus 로고    scopus 로고
    • Evolutionary analysis of mammalian enamelin, the largest enamel protein, supports a crucial role for the 32-kDa peptide and reveals selective adaptation in rodents and primates
    • Al-Hashimi N, Sire JY, Delgado S. Evolutionary analysis of mammalian enamelin, the largest enamel protein, supports a crucial role for the 32-kDa peptide and reveals selective adaptation in rodents and primates. J Mol Evol 2009; 69: 635-656.
    • (2009) J Mol Evol , vol.69 , pp. 635-656
    • Al-Hashimi, N.1    Sire, J.Y.2    Delgado, S.3
  • 30
    • 0028968674 scopus 로고
    • Carbohydrate moieties of porcine 32 kDa enamelin
    • Yamakoshi Y. Carbohydrate moieties of porcine 32 kDa enamelin. Calcif Tissue Int 1995; 56: 323-330.
    • (1995) Calcif Tissue Int , vol.56 , pp. 323-330
    • Yamakoshi, Y.1
  • 32
    • 0033593352 scopus 로고    scopus 로고
    • Tyrosyl motif in amelogenins binds N-acetyl-D-glucosamine
    • Ravindranath R, Moradian-Oldak J, Fincham A. Tyrosyl motif in amelogenins binds N-acetyl-D-glucosamine. J Biol Chem 1999; 274: 2464-2471.
    • (1999) J Biol Chem , vol.274 , pp. 2464-2471
    • Ravindranath, R.1    Moradian-Oldak, J.2    Fincham, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.