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

Year Number of Results
1953 1
1954 1
1964 2
1966 6
1967 2
1968 4
1969 5
1970 4
1971 3
1972 6
1973 7
1974 4
1975 4
1976 7
1977 7
1978 4
1979 5
1980 10
1981 4
1982 13
1983 21
1984 13
1985 10
1986 8
1987 20
1988 16
1989 10
1990 16
1991 15
1992 20
1993 22
1994 33
1995 20
1996 30
1997 20
1998 20
1999 32
2000 24
2001 24
2002 20
2003 31
2004 23
2005 37
2006 39
2007 33
2008 33
2009 31
2010 32
2011 30
2012 44
2013 34
2014 36
2015 39
2016 46
2017 51
2018 66
2019 65
2020 53
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2022 37
2023 31
2024 8

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1,230 results

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Page 1
Endo-N-acetyl-beta-D-glucosaminidases and their potential substrates: structure/function relationships.
Karamanos Y. Karamanos Y. Res Microbiol. 1997 Nov;148(8):661-71. doi: 10.1016/S0923-2508(99)80065-5. Res Microbiol. 1997. PMID: 9765851 Free article. Review.
Endo-N-acetyl-beta-D-glucosaminidases (ENGases) have been defined as the enzymes that hydrolyse the glycosidic bond between an N-acetyl-beta-D-glucosamine residue and the adjacent (partner) monosaccharide within an oligosaccharide chain. ...
Endo-N-acetyl-beta-D-glucosaminidases (ENGases) have been defined as the enzymes that hydrolyse the glycosidic bond between an …
Are there biological functions for bacterial endo-N-acetyl-beta-D-glucosaminidases?
Karamanos Y, Bourgerie S, Barreaud JP, Julien R. Karamanos Y, et al. Res Microbiol. 1995 Jul-Aug;146(6):437-43. doi: 10.1016/0923-2508(96)80289-0. Res Microbiol. 1995. PMID: 8525060 Free article. Review.
The endo-N-acetyl-beta-D-glucosaminidases (ENGase) acting on the N-N'-diacetylchitobiosyl core of N-glycosylproteins are essential reagents for the investigation of the structure and the functions of glycoproteins. ...
The endo-N-acetyl-beta-D-glucosaminidases (ENGase) acting on the N-N'-diacetylchitobiosyl core of N-glycosylproteins are essen …
Endo-N-acetylneuraminidase associated with bacteriophage particles.
Kwiatkowski B, Boschek B, Thiele H, Stirm S. Kwiatkowski B, et al. J Virol. 1982 Aug;43(2):697-704. doi: 10.1128/JVI.43.2.697-704.1982. J Virol. 1982. PMID: 7109038 Free PMC article.
By analogy to other virus particles with host capsule depolymerase activity, it is probable that the phi 1.2 endo-N-acetylneuraminidase activity is associated with these spikes....
By analogy to other virus particles with host capsule depolymerase activity, it is probable that the phi 1.2 endo-N-acetylneur …
Complete nucleotide sequence of the bacteriophage K1F tail gene encoding endo-N-acylneuraminidase (endo-N) and comparison to an endo-N homolog in bacteriophage PK1E.
Petter JG, Vimr ER. Petter JG, et al. J Bacteriol. 1993 Jul;175(14):4354-63. doi: 10.1128/jb.175.14.4354-4363.1993. J Bacteriol. 1993. PMID: 8331067 Free PMC article.
Endo-N-acylneuraminidase (endo-N) is a phage-encoded depolymerase that degrades the alpha (2-8)-linked polysialic acid chains of K1 serotypes of Escherichia coli and vertebrate neural cell adhesion molecules. ...The endo-N amino-terminal …
Endo-N-acylneuraminidase (endo-N) is a phage-encoded depolymerase that degrades the alpha (2-8)-linked polysiali …
High resolution crystal structure of the endo-N-Acetyl-beta-D-glucosaminidase responsible for the deglycosylation of Hypocrea jecorina cellulases.
Stals I, Karkehabadi S, Kim S, Ward M, Van Landschoot A, Devreese B, Sandgren M. Stals I, et al. PLoS One. 2012;7(7):e40854. doi: 10.1371/journal.pone.0040854. Epub 2012 Jul 30. PLoS One. 2012. PMID: 22859955 Free PMC article.
The endo-N-acetyl-beta-D-glucosaminidases classified into glycoside hydrolase family 18 are small, bacterial proteins with different substrate specificities. ...This is the first three-dimensional structure of a eukaryotic endo-N-acetyl-beta-D-glucosam …
The endo-N-acetyl-beta-D-glucosaminidases classified into glycoside hydrolase family 18 are small, bacterial proteins with dif …
Substrate specificity of two bacteriophage-associated endo-N-acetylneuraminidases.
Kwiatkowski B, Boschek B, Thiele H, Stirm S. Kwiatkowski B, et al. J Virol. 1983 Jan;45(1):367-74. doi: 10.1128/JVI.45.1.367-374.1983. J Virol. 1983. PMID: 6401818 Free PMC article.
Virol. 43:697-704, 1982), which grows on E. coli K235 (O1:K1:H-), depolymerizes colominic acid, and belongs to morphology group C. The specificity of the phi 1.2- and phi 92-associated endo-N-acetylneuraminidases has been studied with respect to the following substr …
Virol. 43:697-704, 1982), which grows on E. coli K235 (O1:K1:H-), depolymerizes colominic acid, and belongs to morphology group C. The speci …
Purification and properties of a bacteriophage-induced endo-N-acetylneuraminidase specific for poly-alpha-2,8-sialosyl carbohydrate units.
Hallenbeck PC, Vimr ER, Yu F, Bassler B, Troy FA. Hallenbeck PC, et al. J Biol Chem. 1987 Mar 15;262(8):3553-61. J Biol Chem. 1987. PMID: 3546309 Free article.
The soluble form of a bacteriophage-induced endo-N-acetylneuraminidase (Endo-N) specific for hydrolyzing oligo- or poly-alpha-2,8-linked sialosyl units in sources as disparate as bacterial and neural membrane glycoconjugates was purified approximately …
The soluble form of a bacteriophage-induced endo-N-acetylneuraminidase (Endo-N) specific for hydrolyzing oligo- …
Endo-N-acetyl-beta-D-glucosaminidase and peptide-N4-(N-acetyl-glucosaminyl) asparagine amidase activities during germination of Raphanus sativus.
Berger S, Menudier A, Julien R, Karamanos Y. Berger S, et al. Phytochemistry. 1995 Jun;39(3):481-7. doi: 10.1016/0031-9422(95)00001-n. Phytochemistry. 1995. PMID: 7576449
Endo-N-acetyl-beta-D-glucosaminidase (ENGase, EC 3.2.1.96) and peptide-N4-(N-acetyl-beta-D-glucosaminyl) asparagine amidase (PNGase, EC 3.5.1.52) activities were monitored during germination and postgerminative development in Raphanus sativus. ...
Endo-N-acetyl-beta-D-glucosaminidase (ENGase, EC 3.2.1.96) and peptide-N4-(N-acetyl-beta-D-glucosaminyl) asparagine amidase (P …
1,230 results