메뉴 건너뛰기




Volumn 8, Issue 8, 1999, Pages 1714-1719

A superfamily of archaeal, bacterial, and eukaryotic proteins homologous to animal transglutaminases

Author keywords

Catalytic triad; Evolution of enzymes; Iterative database search; Thiol protease; Transglutaminase

Indexed keywords

ASPARTIC ACID; BACTERIAL PROTEIN; BLOOD CLOTTING FACTOR 13A; CELL PROTEIN; CYSTEINE; HISTIDINE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE;

EID: 0032800014     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.8.1714     Document Type: Article
Times cited : (148)

References (35)
  • 1
    • 0028946284 scopus 로고
    • Transglutaminase-catalyzed matrix cross-linking in differentiating cartilage: Identification of osteonectin as a major glutaminyl substrate
    • Aeschlimann D, Kaupp O, Paulsson M. 1995. Transglutaminase-catalyzed matrix cross-linking in differentiating cartilage: Identification of osteonectin as a major glutaminyl substrate. J Cell Biol 129:881-892.
    • (1995) J Cell Biol , vol.129 , pp. 881-892
    • Aeschlimann, D.1    Kaupp, O.2    Paulsson, M.3
  • 4
    • 0032509302 scopus 로고    scopus 로고
    • Genome sequence of the nematode C. elegans: A platform for investigating biology
    • The C. elegans Sequencing Consortium. 1998. Genome sequence of the nematode C. elegans: A platform for investigating biology. Science 282:2012-2028.
    • (1998) Science , vol.282 , pp. 2012-2028
  • 5
    • 0030976452 scopus 로고    scopus 로고
    • A new transglutaminase-like from ascidian Ciona intestinalis
    • Cariello L, Risloratore F, Zanetti L. 1997. A new transglutaminase-like from ascidian Ciona intestinalis. FEBS Lett 408:171-176.
    • (1997) FEBS Lett , vol.408 , pp. 171-176
    • Cariello, L.1    Risloratore, F.2    Zanetti, L.3
  • 6
    • 0027288548 scopus 로고
    • Human erythrocyte membrane protein band 4.2 (pallidin)
    • Cohen CM, Dotimas E, Korsgren C. 1993. Human erythrocyte membrane protein band 4.2 (pallidin). Semin Hematol 30:119-137.
    • (1993) Semin Hematol , vol.30 , pp. 119-137
    • Cohen, C.M.1    Dotimas, E.2    Korsgren, C.3
  • 8
    • 0027938296 scopus 로고
    • Analysis of the catalytic activity of human factor XIIIa by site-directed mutagenesis
    • Hettasch JM, Greenberg CS. 1994. Analysis of the catalytic activity of human factor XIIIa by site-directed mutagenesis. J Biol Chem 269:28309-28313.
    • (1994) J Biol Chem , vol.269 , pp. 28309-28313
    • Hettasch, J.M.1    Greenberg, C.S.2
  • 10
    • 0030611230 scopus 로고    scopus 로고
    • Bordetella bronchiseptica dermonecrotizing toxin induces reorganization of actin stress fibers through deamidation of Gln-63 of the GTP-binding protein Rho
    • Horiguchi Y, Inoue N, Masuda M, Kashimoto T, Katahira J, Sugimoto N, Matsuda M. 1997. Bordetella bronchiseptica dermonecrotizing toxin induces reorganization of actin stress fibers through deamidation of Gln-63 of the GTP-binding protein Rho. Proc Natl Acad Sci USA 94:11623-11626.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11623-11626
    • Horiguchi, Y.1    Inoue, N.2    Masuda, M.3    Kashimoto, T.4    Katahira, J.5    Sugimoto, N.6    Matsuda, M.7
  • 12
    • 0029076150 scopus 로고
    • Highly active soluble processed forms of the transglutaminase 1 enzyme in epidermal keratinocytes
    • Kim SY, Chung SI, Steinert PM. 1995. Highly active soluble processed forms of the transglutaminase 1 enzyme in epidermal keratinocytes. J Biol Chem 270:18026-18035.
    • (1995) J Biol Chem , vol.270 , pp. 18026-18035
    • Kim, S.Y.1    Chung, S.I.2    Steinert, P.M.3
  • 13
    • 0001339532 scopus 로고
    • A program to produce both detailed and schematic plots of proteins
    • Kraulis P. 1991 A program to produce both detailed and schematic plots of proteins. J Appl Crystallogr 24:946-950.
    • (1991) J Appl Crystallogr , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 15
    • 0032080312 scopus 로고    scopus 로고
    • Biochemical characterization and localization of transglutaminase in wild-type and cell-death mutants of the nematode Caenorhabditis elegans
    • Madi A, Punyiczki M, di Rao M, Piacentini M, Fesus L. 1998. Biochemical characterization and localization of transglutaminase in wild-type and cell-death mutants of the nematode Caenorhabditis elegans. Eur J Biochem 253:583-590.
    • (1998) Eur J Biochem , vol.253 , pp. 583-590
    • Madi, A.1    Punyiczki, M.2    Di Rao, M.3    Piacentini, M.4    Fesus, L.5
  • 17
    • 0028289723 scopus 로고
    • Role of histidine 373 in catalytic activity of coagulation factor XIII
    • Micanovic R, Procyk R, Lin W, Matsueda CR. 1994. Role of histidine 373 in catalytic activity of coagulation factor XIII. J Biol Chem 269:9190-9194.
    • (1994) J Biol Chem , vol.269 , pp. 9190-9194
    • Micanovic, R.1    Procyk, R.2    Lin, W.3    Matsueda, C.R.4
  • 18
    • 0030825124 scopus 로고    scopus 로고
    • Glycoproteins in prokaryotes
    • Moens S, Vanderleyden J. 1997. Glycoproteins in prokaryotes. Arch Microbiol 168:169-175.
    • (1997) Arch Microbiol , vol.168 , pp. 169-175
    • Moens, S.1    Vanderleyden, J.2
  • 19
    • 0029847710 scopus 로고    scopus 로고
    • Novel aspects of blood coagulation factor XIII. I. Structure, distribution, activation, and function
    • Muszbek L, Adany R, Mikkola H. 1996. Novel aspects of blood coagulation factor XIII. I. Structure, distribution, activation, and function. Crit Rev Clin Lab Sci 33:351-421.
    • (1996) Crit Rev Clin Lab Sci , vol.33 , pp. 351-421
    • Muszbek, L.1    Adany, R.2    Mikkola, H.3
  • 21
  • 22
    • 0030053370 scopus 로고    scopus 로고
    • ProMod and Swiss-model: Internet-based tools for automated comparative protein modelling
    • Peitsch MC. 1996. ProMod and Swiss-Model: Internet-based tools for automated comparative protein modelling. Biochem Sue Trans 24:274-279.
    • (1996) Biochem Sue Trans , vol.24 , pp. 274-279
    • Peitsch, M.C.1
  • 24
    • 0032577588 scopus 로고    scopus 로고
    • Thr Rho-deamidating Cytotoxic Necrotizing Factor 1 from Escherichia coli possesses transglutaminase activity
    • Schmidt G, Selzer J, Lerm M, Aktories K. 1998. Thr Rho-deamidating Cytotoxic Necrotizing Factor 1 from Escherichia coli possesses transglutaminase activity. J. Biol Chem 273:13669-13674.
    • (1998) J. Biol Chem , vol.273 , pp. 13669-13674
    • Schmidt, G.1    Selzer, J.2    Lerm, M.3    Aktories, K.4
  • 26
    • 0029364939 scopus 로고
    • Multiple alignment of biopolymer sequences, based on the search for statistically significant common segments
    • Seledtsov IA, Vul'f IuI, Makarova KS. 1995. Multiple alignment of biopolymer sequences, based on the search for statistically significant common segments. Mol Biol (Mosk) 29:1023-1039.
    • (1995) Mol Biol (Mosk) , vol.29 , pp. 1023-1039
    • Seledtsov, I.A.1    Vul'f, Iu.I.2    Makarova, K.S.3
  • 28
    • 0343145679 scopus 로고    scopus 로고
    • Bacterial and archaeal S-layer proteins: Structure-function relationships and their biotechnological applications
    • Sleytr UB, Sara M. 1997. Bacterial and archaeal S-layer proteins: Structure-function relationships and their biotechnological applications. Trends Biotechnol 15:20-26.
    • (1997) Trends Biotechnol , vol.15 , pp. 20-26
    • Sleytr, U.B.1    Sara, M.2
  • 29
    • 0029050246 scopus 로고
    • The proteins elafin, filaggrin, keratin intermediate filaments, loricrin, and small proline-rich proteins 1 and 2 are isodipeptide cross-linked components of the human epidermal cornified cell envelope
    • Steinert PM, Marekov LN. 1995. The proteins elafin, filaggrin, keratin intermediate filaments, loricrin, and small proline-rich proteins 1 and 2 are isodipeptide cross-linked components of the human epidermal cornified cell envelope. J Biol Chem 270:17702-17711.
    • (1995) J Biol Chem , vol.270 , pp. 17702-17711
    • Steinert, P.M.1    Marekov, L.N.2
  • 30
    • 0027439684 scopus 로고
    • Limulus hemocyte transglutaminase. cDNA cloning, amino acid sequence, and tissue localization
    • Tokunaga F, Muta T, Iwanaga S, Ichinose A, Davie EW, Kuma K, Miyata T. 1993. Limulus hemocyte transglutaminase. cDNA cloning, amino acid sequence, and tissue localization. J Biol Chem 268:262-268.
    • (1993) J Biol Chem , vol.268 , pp. 262-268
    • Tokunaga, F.1    Muta, T.2    Iwanaga, S.3    Ichinose, A.4    Davie, E.W.5    Kuma, K.6    Miyata, T.7
  • 31
  • 33
    • 0028501914 scopus 로고
    • Non-globular domains in protein sequences: Automated segmentation using complexity measures
    • Wootton JC. 1994. Non-globular domains in protein sequences: Automated segmentation using complexity measures. Comput Chem 18:269-285.
    • (1994) Comput Chem , vol.18 , pp. 269-285
    • Wootton, J.C.1
  • 34
    • 0029901640 scopus 로고    scopus 로고
    • Analysis of compositionally biased regions in sequence databases
    • Wootton JC, Federhen S. 1996. Analysis of compositionally biased regions in sequence databases. Methods Enzymol 266:554-571.
    • (1996) Methods Enzymol , vol.266 , pp. 554-571
    • Wootton, J.C.1    Federhen, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.