scholarly article | Q13442814 |
P356 | DOI | 10.1016/S0141-8130(00)00120-3 |
P698 | PubMed publication ID | 10828365 |
P50 | author | Janusz Bujnicki | Q11720088 |
P2860 | cites work | Circular Permutations in the Molecular Evolution of DNA Methyltransferases | Q21045391 |
The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools | Q24248165 | ||
Gapped BLAST and PSI-BLAST: a new generation of protein database search programs | Q24545170 | ||
Three-dimensional structure of the adenine-specific DNA methyltransferase M.Taq I in complex with the cofactor S-adenosylmethionine | Q24562671 | ||
The DNA (cytosine-5) methyltransferases | Q24614934 | ||
Alw26I, Eco31I and Esp3I--type IIs methyltransferases modifying cytosine and adenine in complementary strands of the target DNA | Q24629662 | ||
Hydrophobic folding units derived from dissimilar monomer structures and their interactions | Q24673675 | ||
The crystal structure of Haelll methyltransferase covalently complexed to DNA: An extrahelical cytosine and rearranged base pairing | Q27729758 | ||
Crystal structure of the HhaI DNA methyltransferase complexed with S-adenosyl-L-methionine | Q27731970 | ||
Structure of pvu II DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment | Q27739964 | ||
Crystal structure of the DpnM DNA adenine methyltransferase from the DpnII restriction system of streptococcus pneumoniae bound to S-adenosylmethionine | Q27766381 | ||
SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling | Q27860614 | ||
Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features | Q27860675 | ||
Errors in protein structures | Q27860776 | ||
Comparative protein modelling by satisfaction of spatial restraints | Q27860866 | ||
Three-dimensional domain duplication, swapping and stealing | Q28242376 | ||
Recognition of errors in three-dimensional structures of proteins | Q28249658 | ||
JPred: a consensus secondary structure prediction server | Q29614378 | ||
Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches | Q29622868 | ||
Alignment of beta-barrels in (beta/alpha)8 proteins using hydrogen-bonding pattern | Q30193889 | ||
Seeking significance in three-dimensional protein structure comparisons. | Q30417187 | ||
Structural features can be unconserved in proteins with similar folds. An analysis of side-chain to side-chain contacts secondary structure and accessibility. | Q30420113 | ||
Autonomous subdomains in protein folding | Q30420417 | ||
How far divergent evolution goes in proteins | Q30431003 | ||
A case of convergent evolution of nucleic acid binding modules | Q34411103 | ||
Intermediate sequences increase the detection of homology between sequences | Q34446157 | ||
Agmenellum quadruplicatum M.AquI, a novel modification methylase | Q36156622 | ||
Cloning and analysis of the genes encoding the type IIS restriction-modification system HphI from Haemophilus parahaemolyticus | Q39716944 | ||
Cloning of the BssHII restriction-modification system in Escherichia coli : BssHII methyltransferase contains circularly permuted cytosine-5 methyltransferase motifs | Q39721447 | ||
A bacterial methyltransferase M.EcoHK311 requires two proteins for in vitro methylation. | Q40392566 | ||
The multiplicity of domains in proteins | Q40422007 | ||
Predictive motifs derived from cytosine methyltransferases | Q40448394 | ||
Circularly permuted DNA, RNA and proteins — a review | Q40485844 | ||
Cloning and sequence analysis of the StsI restriction-modification gene: presence of homology to FokI restriction-modification enzymes | Q40533662 | ||
Construction and use of chimeric SPR/phi 3T DNA methyltransferases in the definition of sequence recognizing enzyme regions. | Q41354942 | ||
Circular permutations of natural protein sequences: structural evidence | Q41515840 | ||
M.(phi)BssHII, a novel cytosine-C5-DNA-methyltransferase with target-recognizing domains at separated locations of the enzyme | Q42283657 | ||
Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes | Q42605575 | ||
Sequence comparison of the EcoHK31I and EaeI restriction-modification systems suggests an intergenic transfer of genetic material | Q42679217 | ||
Conserved sequence motifs in plant S-adenosyl-L-methionine-dependent methyltransferases | Q47755068 | ||
Structure-guided analysis reveals nine sequence motifs conserved among DNA amino-methyltransferases, and suggests a catalytic mechanism for these enzymes | Q48069333 | ||
Nucleotide sequence of the FokI restriction-modification system: separate strand-specificity domains in the methyltransferase | Q48289621 | ||
The DNA recognition subunit of a DNA methyltransferase is predominantly a molten globule in the absence of DNA. | Q52212933 | ||
Universal catalytic domain structure of AdoMet-dependent methyltransferases. | Q53012595 | ||
Amino acid sequence arrangements of DNA-methyltransferases | Q53753431 | ||
Recognition of analogous and homologous protein folds: analysis of sequence and structure conservation 1 1Edited by F. E. Cohen | Q57881402 | ||
Structural modelling of a type I DNA methyltransferase | Q71726980 | ||
Structure-based sequence alignment of three AdoMet-dependent DNA methyltransferases | Q71866459 | ||
Structural characterization of two tandemly arranged DNA methyltransferase genes from Neisseria gonorrhoeae MS11: N4-cytosine specific M.NgoMXV and nonfunctional 5-cytosine-type M.NgoMorf2P | Q73393627 | ||
Is the HemK family of putative S-adenosylmethionine-dependent methyltransferases a "missing" zeta subfamily of adenine methyltransferases? A hypothesis | Q73483490 | ||
Structural studies of EcoRII methylase: exploring similarities among methylases | Q74445735 | ||
P433 | issue | 3 | |
P304 | page(s) | 195-204 | |
P577 | publication date | 2000-06-01 | |
P1433 | published in | International Journal of Biological Macromolecules | Q6051322 |
P1476 | title | Homology modelling of the DNA 5mC methyltransferase M.BssHII. Is permutation of functional subdomains common to all subfamilies of DNA methyltransferases? | |
P478 | volume | 27 |
Q55023866 | Circularly permuted variants of two CG-specific prokaryotic DNA methyltransferases. |
Q47233097 | Genome-wide analysis of restriction-modification system in unicellular and filamentous cyanobacteria |
Q43208461 | Homology modeling and molecular dynamics simulations of HgiDII methyltransferase in complex with DNA and S-adenosyl-methionine: catalytic mechanism and interactions with DNA. |
Q21045389 | Sequence permutations in the molecular evolution of DNA methyltransferases |
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