Initial insight into the function of the lysosomal 66.3 kDa protein from mouse by means of X-ray crystallography

Lakomek K, Dickmanns A, Kettwig M, Urlaub H, Ficner R, Lübke T (2009)
BMC Structural Biology 9(1): 56-72.

Journal Article | Published | English

No fulltext has been uploaded

Author
; ; ; ; ;
Publishing Year
ISSN
PUB-ID

Cite this

Lakomek K, Dickmanns A, Kettwig M, Urlaub H, Ficner R, Lübke T. Initial insight into the function of the lysosomal 66.3 kDa protein from mouse by means of X-ray crystallography. BMC Structural Biology. 2009;9(1):56-72.
Lakomek, K., Dickmanns, A., Kettwig, M., Urlaub, H., Ficner, R., & Lübke, T. (2009). Initial insight into the function of the lysosomal 66.3 kDa protein from mouse by means of X-ray crystallography. BMC Structural Biology, 9(1), 56-72.
Lakomek, K., Dickmanns, A., Kettwig, M., Urlaub, H., Ficner, R., and Lübke, T. (2009). Initial insight into the function of the lysosomal 66.3 kDa protein from mouse by means of X-ray crystallography. BMC Structural Biology 9, 56-72.
Lakomek, K., et al., 2009. Initial insight into the function of the lysosomal 66.3 kDa protein from mouse by means of X-ray crystallography. BMC Structural Biology, 9(1), p 56-72.
K. Lakomek, et al., “Initial insight into the function of the lysosomal 66.3 kDa protein from mouse by means of X-ray crystallography”, BMC Structural Biology, vol. 9, 2009, pp. 56-72.
Lakomek, K., Dickmanns, A., Kettwig, M., Urlaub, H., Ficner, R., Lübke, T.: Initial insight into the function of the lysosomal 66.3 kDa protein from mouse by means of X-ray crystallography. BMC Structural Biology. 9, 56-72 (2009).
Lakomek, Kristina, Dickmanns, Achim, Kettwig, Matthias, Urlaub, Henning, Ficner, Ralf, and Lübke, Torben. “Initial insight into the function of the lysosomal 66.3 kDa protein from mouse by means of X-ray crystallography”. BMC Structural Biology 9.1 (2009): 56-72.
This data publication is cited in the following publications:
This publication cites the following data publications:

3 Citations in Europe PMC

Data provided by Europe PubMed Central.

More similar than different: Host cell protein production using three null CHO cell lines.
Yuk IH, Nishihara J, Walker D Jr, Huang E, Gunawan F, Subramanian J, Pynn AF, Yu XC, Zhu-Shimoni J, Vanderlaan M, Krawitz DC., Biotechnol. Bioeng. 112(10), 2015
PMID: 25894672
The proteome of lysosomes.
Schroder BA, Wrocklage C, Hasilik A, Saftig P., Proteomics 10(22), 2010
PMID: 20957757
Structures of an isopenicillin N converting Ntn-hydrolase reveal different catalytic roles for the active site residues of precursor and mature enzyme.
Bokhove M, Yoshida H, Hensgens CM, van der Laan JM, Sutherland JD, Dijkstra BW., Structure 18(3), 2010
PMID: 20223213

94 References

Data provided by Europe PubMed Central.

Endocannabinoid hydrolases.
Ueda N., Prostaglandins Other Lipid Mediat. 68-69(), 2002
PMID: 12432941
Fatty acid amide hydrolase, an enzyme with many bioactive substrates. Possible therapeutic implications.
Bisogno T, De Petrocellis L, Di Marzo V., Curr. Pharm. Des. 8(7), 2002
PMID: 11945157
Insight into autoproteolytic activation from the structure of cephalosporin acylase: a protein with two proteolytic chemistries.
Kim JK, Yang IS, Shin HJ, Cho KJ, Ryu EK, Kim SH, Park SS, Kim KH., Proc. Natl. Acad. Sci. U.S.A. 103(6), 2006
PMID: 16446446
In vivo post-translational processing and subunit reconstitution of cephalosporin acylase from Pseudomonas sp. 130.
Li Y, Chen J, Jiang W, Mao X, Zhao G, Wang E., Eur. J. Biochem. 262(3), 1999
PMID: 10411632
Compilation and analysis of intein sequences.
Perler FB, Olsen GJ, Adam E., Nucleic Acids Res. 25(6), 1997
PMID: 9092614
Structural insights into the mechanism of intramolecular proteolysis.
Xu Q, Buckley D, Guan C, Guo HC., Cell 98(5), 1999
PMID: 10490104
Crystal structure of plant asparaginase.
Michalska K, Bujacz G, Jaskolski M., J. Mol. Biol. 360(1), 2006
PMID: 16725155
Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease.
Ikonen E, Baumann M, Gron K, Syvanen AC, Enomaa N, Halila R, Aula P, Peltonen L., EMBO J. 10(1), 1991
PMID: 1703489
Monocyclic beta-lactam antibiotics produced by bacteria.
Sykes RB, Cimarusti CM, Bonner DP, Bush K, Floyd DM, Georgopapadakou NH, Koster WM, Liu WC, Parker WL, Principe PA, Rathnum ML, Slusarchyk WA, Trejo WH, Wells JS., Nature 291(5815), 1981
PMID: 7015152
A novel 7-β-(4-carboxybutanamido)-cephalosporanic acid acylase isolated from Pseudomonas strain C427 and its high-level production in
Ishii Y, Saito Y, Fujimura T, Isogai T, Kojo H, Yamashita M, Niwa M, Kohsaka M., 1994
The 2.0 A crystal structure of cephalosporin acylase.
Kim Y, Yoon K, Khang Y, Turley S, Hol WG., Structure 8(10), 2000
PMID: 11080627
The language of covalent histone modifications.
Strahl BD, Allis CD., Nature 403(6765), 2000
PMID: 10638745
Histone modifications in transcriptional regulation.
Berger SL., Curr. Opin. Genet. Dev. 12(2), 2002
PMID: 11893486
Translating the histone code.
Jenuwein T, Allis CD., Science 293(5532), 2001
PMID: 11498575

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 19706171
PubMed | Europe PMC

Search this title in

Google Scholar