scholarly article | Q13442814 |
P50 | author | Janusz Bujnicki | Q11720088 |
P2093 | author name string | Keith Firman | |
Marcin Feder | |||
Eva Sisáková | |||
Marie Weiserová | |||
Alex Blundell | |||
Agnieszka Obarska | |||
Stepánka Vejsadová | |||
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Three-dimensional structure of the adenine-specific DNA methyltransferase M.Taq I in complex with the cofactor S-adenosylmethionine | Q24562671 | ||
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Biology of DNA restriction | Q24634671 | ||
DNA bending by M.EcoKI methyltransferase is coupled to nucleotide flipping. | Q24810294 | ||
Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors | Q26778475 | ||
Understanding the immutability of restriction enzymes: crystal structure of BglII and its DNA substrate at 1.5 A resolution | Q27621185 | ||
Structure of the N6-adenine DNA methyltransferase M.TaqI in complex with DNA and a cofactor analog | Q27629529 | ||
Structure of Ocr from bacteriophage T7, a protein that mimics B-form DNA | Q27637438 | ||
The PSIPRED protein structure prediction server | Q27860953 | ||
FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties | Q28203085 | ||
Assessment of protein models with three-dimensional profiles | Q28283805 | ||
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Enhanced genome annotation using structural profiles in the program 3D-PSSM | Q29547847 | ||
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Pcons: a neural-network-based consensus predictor that improves fold recognition. | Q30328734 | ||
GeneSilico protein structure prediction meta-server. | Q30333042 | ||
Combining local-structure, fold-recognition, and new fold methods for protein structure prediction. | Q30336231 | ||
COLORADO3D, a web server for the visual analysis of protein structures. | Q30341998 | ||
Accurate prediction of solvent accessibility using neural networks-based regression. | Q30342423 | ||
??? | Q94305684 | ||
FRankenstein becomes a cyborg: the automatic recombination and realignment of fold recognition models in CASP6. | Q30351469 | ||
Families of restriction enzymes: an analysis prompted by molecular and genetic data for type ID restriction and modification systems | Q30662423 | ||
Unusual 2-aminopurine fluorescence from a complex of DNA and the EcoKI methyltransferase | Q30925018 | ||
KpnBI is the prototype of a new family (IE) of bacterial type I restriction-modification system | Q30969015 | ||
Tracking EcoKI and DNA fifty years on: a golden story full of surprises | Q31030715 | ||
Crystal structure of DNA sequence specificity subunit of a type I restriction-modification enzyme and its functional implications | Q33858629 | ||
Structural homologies among type I restriction-modification systems | Q33927977 | ||
Organization of restriction-modification systems | Q34111928 | ||
S-Adenosyl-L-methionine-dependent restriction enzymes | Q34317912 | ||
Conservation of organization in the specificity polypeptides of two families of type I restriction enzymes | Q35597794 | ||
Generation of new DNA binding specificity by truncation of the type IC EcoDXXI hsdS gene | Q35908207 | ||
Coupled prediction of protein secondary and tertiary structure | Q36348400 | ||
Genetic recombination can generate altered restriction specificity | Q37570816 | ||
Purification and biochemical characterisation of theEcoR124 type I modification methylase | Q38330901 | ||
The specificity of sty SKI, a type I restriction enzyme, implies a structure with rotational symmetry | Q39719811 | ||
A deletion mutant of the type IC restriction endonuclease EcoR1241 expressing a novel DNA specificity | Q40415571 | ||
A ?FRankenstein's monster? approach to comparative modeling: Merging the finest fragments of Fold-Recognition models and iterative model refinement aided by 3D structure evaluation | Q40553690 | ||
A symmetrical model for the domain structure of type I DNA methyltransferases | Q40636115 | ||
DNA-binding induces a major structural transition in a type I methyltransferase. | Q40794101 | ||
Initiation of translocation by Type I restriction-modification enzymes is associated with a short DNA extrusion | Q40938302 | ||
Finding a basis for flipping bases. | Q41111081 | ||
Comparison of sequence profiles. Strategies for structural predictions using sequence information | Q41724734 | ||
The location of the genes for host-controlled modification and restriction in Escherichia coli K-12 | Q41967863 | ||
Basis for changes in DNA recognition by the EcoR124 and EcoR124/3 type I DNA restriction and modification enzymes | Q41994610 | ||
Cascaded multiple classifiers for secondary structure prediction | Q42847666 | ||
Chemical modification of lysine by reductive methylation. A probe for residues involved in DNA binding | Q43611425 | ||
Conservation of complex DNA recognition domains between families of restriction enzymes | Q44918995 | ||
Single-body residue-level knowledge-based energy score combined with sequence-profile and secondary structure information for fold recognition | Q47596351 | ||
Isolation of a non-classical mutant of the DNA recognition subunit of the type I restriction endonuclease R.EcoR124I. | Q47969886 | ||
Reassortment of DNA recognition domains and the evolution of new specificities | Q48342551 | ||
Hybrid fold recognition: combining sequence derived properties with evolutionary information. | Q52076382 | ||
Complementation analysis of temperature-sensitive host specificity mutations in Escherichia coli | Q53770636 | ||
Purification and characterization of the methyltransferase from the type 1 restriction and modification system of Escherichia coli K12. | Q54655712 | ||
R124, an fi+ R Factor of a New Compatibility Class | Q54657952 | ||
High-level expression of the cloned genes encoding the subunits of and intact DNA methyltransferase, M.EcoR124 | Q68079186 | ||
Genetics of host-controlled restriction and modification in Escherichia coli | Q69882355 | ||
Functional analysis of host-specificity mutants inEscherichia coli | Q69921483 | ||
Surface labelling of the type I methyltransferase M.EcoR124I reveals lysine residues critical for DNA binding | Q71039730 | ||
Structural modelling of a type I DNA methyltransferase | Q71726980 | ||
A novel mutant of the type I restriction-modification enzyme EcoR124I is altered at a key stage of the subunit assembly pathway | Q73220618 | ||
Theory and applications of the generalized Born solvation model in macromolecular simulations | Q77381573 | ||
Crystal structure of a putative type I restriction-modification S subunit from Mycoplasma genitalium | Q80415317 | ||
P433 | issue | 7 | |
P304 | page(s) | 1992-2005 | |
P577 | publication date | 2006-04-13 | |
P1433 | published in | Nucleic Acids Research | Q135122 |
P1476 | title | Structural model for the multisubunit Type IC restriction-modification DNA methyltransferase M.EcoR124I in complex with DNA. | |
P478 | volume | 34 |
Q36930943 | Crystallization and preliminary X-ray diffraction analysis of the HsdR subunit of a putative type I restriction enzyme from Vibrio vulnificus YJ016 |
Q42002446 | DNA looping and translocation provide an optimal cleavage mechanism for the type III restriction enzymes |
Q37698622 | Diversity of DNA methyltransferases that recognize asymmetric target sequences |
Q37183920 | EcoR124I: from plasmid-encoded restriction-modification system to nanodevice |
Q42965698 | Functional analysis of MmeI from methanol utilizer Methylophilus methylotrophus, a subtype IIC restriction-modification enzyme related to type I enzymes |
Q37810510 | General and molecular microbiology and microbial genetics in the IM CAS |
Q36802930 | Genome-wide survey of codons under diversifying selection in a highly recombining bacterial species, Helicobacter pylori |
Q33885645 | HsdR subunit of the type I restriction-modification enzyme EcoR124I: biophysical characterisation and structural modelling |
Q40817110 | Shape and subunit organisation of the DNA methyltransferase M.AhdI by small-angle neutron scattering |
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