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Glaxo Smith rasmol molecular graphics visualisation tool
Rasmol Molecular Graphics Visualisation Tool, supplied by Glaxo Smith, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/graphical+visualisations/rasmol+program/pm21986542-294-1-12
Average 90 stars, based on 1 article reviews
rasmol molecular graphics visualisation tool - by Bioz Stars, 2026-09
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Article Title: Molecular characterization and expression analysis of major histocompatibility complex class IIA and IIB genes of Odontobutis potamophila
Article Snippet: The major histocompatibility complex (MHC) is a large genomic region in most vertebrates that encode MHC molecules and plays important roles in the immune response and autoimmunity.. MHC genes divide into two major classes, class I and class II, with an obvious difference in structure, peptide-binding specificity and the subsets of T cells that they can activate [1, 2].. MHC class I is found in all nucleated cells to provide peptides to cytotoxic T cells and plays an important role in the primary immune defense system.

Article Title: Induction of protective immunity by synthetic Vibrio cholerae hexasaccharide derived from V. cholerae O1 Ogawa lipopolysaccharide bound to a protein carrier.
Article Snippet: The RasMol program (Biomolecular Structure Department, Glaxo Wellcome Research and Development, Greenford, UK) was used to display and manipulate Brookhaven Protein Data Bank (available through the National Center for Biotechnology Information [http://www.ncbi.nlm.nih.gov]) file 1F4Y to generate this figure.

Article Title: Human CDR-grafted antibody and antibody fragment thereof
Article Snippet: The three-dimensional structure coordinates were prepared using a software AbM (manufactured by Oxford Molecular), and display of the three-dimensional structures using a software Pro-Explore (manufactured by Oxford Molecular) or RasMol (manufactured by Glaxo) according to the respective attached manufacture's instructions.

Article Title: Conformational stability of recombinant manganese superoxide dismutase from the filamentous fungus Trichoderma reesei.
Article Snippet: 30] R. Sayle, RasMol Molecular Graphics Visualisation Tool, Biomolecular Struc- tures Group, Glaxo Wellcome Research & Development, Hertfordshire, UK, 1998.

Article Title: The immune-modulator AS101 reduces anti-HLA antibodies in sera of sensitized patients: a structural approach.
Article Snippet: Abbreviations: aa, Amino acid; Ab, Antibody; CREG, cro leukocyte antigen; IVIg, Intra-venous Immuno-globulin; M sity; mg, miligram; mL, Milliliter; PP, Plasmapheresis; STD ⁎ Corresponding author at: Tissue Typing Laboratory, R campus), Zabotinski Rd., Petach-Tikva, 49100, Israel.. Te 7654607, +972 52 8654607(mobile); fax: +972 3 93767 E-mail addresses: israelimoshe@yahoo.com, mosheis 1 This work was conducted as part of the Ph.D. thesis at Bar-Ilan University.. 2 This author contributed equally to this study as the

Article Title: Induction of protective immunity by synthetic Vibrio cholerae hexasaccharide derived from V. cholerae O1 Ogawa lipopolysaccharide bound to a protein carrier.
Article Snippet: The Brookhaven Protein Data Bank (PDB; available through the National Center for Biotechnology at U niversity of M assachusetts M edical School on M arch 16, 2015 http://jid.oxfordjournals.org/ D ow nloaded from Information [http://www.ncbi.nlm.nih.gov]) file 1F4Y was manipulated with the RasMol program (R. Sayle and Biomolecular Structure Department, Glaxo Wellcome Research and Development, Greenford, UK) to generate figure 3.

Produced:

Article Title: Molecular cloning, functional expression, and mutagenesis of cDNA encoding rye (Secale cereale) seed chitinase-c.
Article Snippet: Taylor & Francis makes every effort to ensure the accuracy of all the information (the “Content”) contained in the publications on our platform.. However, Taylor & Francis, our agents, and our licensors make no representations or warranties whatsoever as to the accuracy, completeness, or suitability for any purpose of the Content.. Any opinions and views expressed in this publication are the opinions and views of the authors, and are not the views of or endorsed by Taylor & Francis.



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Active site of K69A T. brucei ODC in complex with DFMO. The figure was drawn based on the data of reference 7 using the RasMol 2.6 Molecular Graphics Visualisation tool (Glaxo Wellcome Research & Development Co., Stevenage, Herts., United Kingdom). In reference 7, the N terminus of recombinant T. brucei ODC corresponds to the 21st residue of intact ODC (Fig. ​(Fig.3).3). Residues (V62, T63, P64, D72, and T359) which correspond to the residues mutated in this study and were identified as functionally important for substrate specificity in S. ruminantium LDC are purple and violet. The atoms of PLP are yellow, the atoms of DFMO are green, A69 and C360 are orange, and Y389 and F397, which cradle the aliphatic portion of DFMO, are brown. R277, D332, and D361 are also shown, and nitrogen and oxygen atoms of these residues are blue and red, respectively. The asterisked residues belong to the other subunit of the dimer.
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Active site of K69A T. brucei ODC in complex with DFMO. The figure was drawn based on the data of reference 7 using the RasMol 2.6 Molecular Graphics Visualisation tool (Glaxo Wellcome Research & Development Co., Stevenage, Herts., United Kingdom). In reference 7, the N terminus of recombinant T. brucei ODC corresponds to the 21st residue of intact ODC (Fig. ​(Fig.3).3). Residues (V62, T63, P64, D72, and T359) which correspond to the residues mutated in this study and were identified as functionally important for substrate specificity in S. ruminantium LDC are purple and violet. The atoms of PLP are yellow, the atoms of DFMO are green, A69 and C360 are orange, and Y389 and F397, which cradle the aliphatic portion of DFMO, are brown. R277, D332, and D361 are also shown, and nitrogen and oxygen atoms of these residues are blue and red, respectively. The asterisked residues belong to the other subunit of the dimer.

Journal:

Article Title: Gene Cloning and Molecular Characterization of Lysine Decarboxylase from Selenomonas ruminantium Delineate Its Evolutionary Relationship to Ornithine Decarboxylases from Eukaryotes

doi:

Figure Lengend Snippet: Active site of K69A T. brucei ODC in complex with DFMO. The figure was drawn based on the data of reference 7 using the RasMol 2.6 Molecular Graphics Visualisation tool (Glaxo Wellcome Research & Development Co., Stevenage, Herts., United Kingdom). In reference 7, the N terminus of recombinant T. brucei ODC corresponds to the 21st residue of intact ODC (Fig. ​(Fig.3).3). Residues (V62, T63, P64, D72, and T359) which correspond to the residues mutated in this study and were identified as functionally important for substrate specificity in S. ruminantium LDC are purple and violet. The atoms of PLP are yellow, the atoms of DFMO are green, A69 and C360 are orange, and Y389 and F397, which cradle the aliphatic portion of DFMO, are brown. R277, D332, and D361 are also shown, and nitrogen and oxygen atoms of these residues are blue and red, respectively. The asterisked residues belong to the other subunit of the dimer.

Article Snippet: The figure was drawn based on the data of reference 7 using the RasMol 2.6 Molecular Graphics Visualisation tool (Glaxo Wellcome Research & Development Co., Stevenage, Herts., United Kingdom).

Techniques: Recombinant