نتائج البحث

Saturating representation of loop conformational fragments in structure databanks.

• Authors : Fernandez-Fuentes, Narcis¹ ; Fiser, András¹

• Source: BMC Structural Biology. 2006, Vol. 6, p15-12. 12p. 4 Charts, 6 Graphs.

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Quantification of the impact of PSI:Biology according to the annotations of the determined structures.

• Authors : DePietro PJ; Julfayev ES; McLaughlin WA

Subjects: Databases, Protein* ; Molecular Sequence Annotation*; Proteins/Proteins/Proteins/*chemistry

• Source: BMC structural biology [BMC Struct Biol] 2013 Oct 21; Vol. 13, pp. 24. Date of Electronic Publication: 2013 Oct 21.Publisher: BioMed Central Country of Publication: England NLM ID: 101088689 Publication Model: Electronic Cited Medium: Internet ISSN: 1472-6807

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A comprehensive update of the sequence and structure classification of kinases.

• Authors : Cheek S; Howard Hughes Medical Institute, University of Texas Southwestern Medical Center, 5323 Harry Hines Blvd, Dallas, Texas 75390, USA. ; Ginalski K

Subjects: Databases, Protein*; Phosphotransferases/Phosphotransferases/Phosphotransferases/*chemistry ; Phosphotransferases/Phosphotransferases/Phosphotransferases/*classification

• Source: BMC structural biology [BMC Struct Biol] 2005 Mar 16; Vol. 5, pp. 6. Date of Electronic Publication: 2005 Mar 16.Publisher: BioMed Central Country of Publication: England NLM ID: 101088689 Publication Model: Electronic Cited Medium: Internet ISSN: 1472-6807

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Functional region prediction with a set of appropriate homologous sequences--an index for sequence selection by integrating structure and sequence information with spatial statistics.

• Authors : Nemoto W; Computational Biology Research Center (CBRC), Advanced Industrial Science and Technology (AIST), AIST Tokyo Waterfront Bio-IT Research Building, 2-4-7 Aomi, Koto-ku, Tokyo 135-0064, Japan. ; Toh H

Subjects: Sequence Analysis, Protein* ; Sequence Homology, Amino Acid*; Computational Biology/Computational Biology/Computational Biology/*methods

• Source: BMC structural biology [BMC Struct Biol] 2012 May 29; Vol. 12, pp. 11. Date of Electronic Publication: 2012 May 29.Publisher: BioMed Central Country of Publication: England NLM ID: 101088689 Publication Model: Electronic Cited Medium: Internet ISSN: 1472-6807

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Improving protein structure similarity searches using domain boundaries based on conserved sequence information.

• Authors : Thompson KE; National Center for Biotechnology Information, National Library of Medicine, National Institutes of Health, Bethesda, MD, USA. ; Wang Y

Subjects: Amino Acid Sequence* ; Conserved Sequence*; Computational Biology/Computational Biology/Computational Biology/*methods

• Source: BMC structural biology [BMC Struct Biol] 2009 May 19; Vol. 9, pp. 33. Date of Electronic Publication: 2009 May 19.Publisher: BioMed Central Country of Publication: England NLM ID: 101088689 Publication Model: Electronic Cited Medium: Internet ISSN: 1472-6807

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Evolutionarily consistent families in SCOP: sequence, structure and function.

• Authors : Pethica RB; Department of Computer Science, University of Bristol, The Merchant Venturers Building, Room 3,16, Woodland Road, Bristol, UK. ; Levitt M

Subjects: Evolution, Molecular* ; Multigene Family* ; Sequence Analysis, Protein*

• Source: BMC structural biology [BMC Struct Biol] 2012 Oct 18; Vol. 12, pp. 27. Date of Electronic Publication: 2012 Oct 18.Publisher: BioMed Central Country of Publication: England NLM ID: 101088689 Publication Model: Electronic Cited Medium: Internet ISSN: 1472-6807

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Sequence analysis on the information of folding initiation segments in ferredoxin-like fold proteins.

• Authors : Matsuoka M; Kikuchi T; Department of Bioinformatics, College of Life Sciences, Ritsumeikan University, 1-1-1 Nojihigashi, Kusatsu, Shiga 525-8577, Japan. .

Subjects: Protein Folding*; Ferredoxins/Ferredoxins/Ferredoxins/*chemistry ; Proteins/Proteins/Proteins/*chemistry

• Source: BMC structural biology [BMC Struct Biol] 2014 May 23; Vol. 14, pp. 15. Date of Electronic Publication: 2014 May 23.Publisher: BioMed Central Country of Publication: England NLM ID: 101088689 Publication Model: Electronic Cited Medium: Internet ISSN: 1472-6807

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Fold-recognition and comparative modeling of human α2,3-sialyltransferases reveal their sequence and structural similarities to CstII from Campylobacter jejuni.

• Authors : Sujatha, M. S.¹ ; Balaji, Petety V.¹

• Source: BMC Structural Biology. 2006, Vol. 6, p1-15. 15p. 7 Diagrams, 2 Charts.

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Structural motif screening reveals a novel, conserved carbohydrate-binding surface in the pathogenesis-related protein PR-5d.

• Authors : Doxey AC; Department of Biology, University of Waterloo, 200 University Avenue West, Waterloo, Ontario N2L 3G1, Canada.; Cheng Z

Subjects: Carbohydrate Metabolism* ; Conserved Sequence*; Computational Biology/Computational Biology/Computational Biology/*methods

• Source: BMC structural biology [BMC Struct Biol] 2010 Aug 03; Vol. 10, pp. 23. Date of Electronic Publication: 2010 Aug 03.Publisher: BioMed Central Country of Publication: England NLM ID: 101088689 Publication Model: Electronic Cited Medium: Internet ISSN: 1472-6807

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Sequence and structural analysis of the Asp-box motif and Asp-box beta-propellers; a widespread propeller-type characteristic of the Vps10 domain family and several glycoside hydrolase families.

• Authors : Quistgaard EM; MIND Centre, Department of Molecular Biology, University of Aarhus, Gustav Wieds Vej 10C, DK 8000 Arhus C, Denmark. ; Thirup SS

Subjects: Glycoside Hydrolases/Glycoside Hydrolases/Glycoside Hydrolases/*chemistry ; Vesicular Transport Proteins/Vesicular Transport Proteins/Vesicular Transport Proteins/*chemistry; Amino Acid Motifs

• Source: BMC structural biology [BMC Struct Biol] 2009 Jul 13; Vol. 9, pp. 46. Date of Electronic Publication: 2009 Jul 13.Publisher: BioMed Central Country of Publication: England NLM ID: 101088689 Publication Model: Electronic Cited Medium: Internet ISSN: 1472-6807

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