for Journals by Title or ISSN
for Articles by Keywords
help
  Subjects -> CHEMISTRY (Total: 762 journals)
    - ANALYTICAL CHEMISTRY (45 journals)
    - CHEMISTRY (527 journals)
    - CRYSTALLOGRAPHY (22 journals)
    - ELECTROCHEMISTRY (24 journals)
    - INORGANIC CHEMISTRY (40 journals)
    - ORGANIC CHEMISTRY (40 journals)
    - PHYSICAL CHEMISTRY (64 journals)

CHEMISTRY (527 journals)                  1 2 3 4 5 6 | Last

Accreditation and Quality Assurance: Journal for Quality, Comparability and Reliability in Chemical Measurement     Hybrid Journal   (30 followers)
ACS Catalysis     Full-text available via subscription   (21 followers)
ACS Chemical Neuroscience     Full-text available via subscription   (10 followers)
ACS Combinatorial Science     Full-text available via subscription   (6 followers)
ACS Macro Letters     Full-text available via subscription   (16 followers)
ACS Medicinal Chemistry Letters     Full-text available via subscription   (16 followers)
ACS Nano     Full-text available via subscription   (154 followers)
ACS Photonics     Full-text available via subscription   (1 follower)
ACS Synthetic Biology     Full-text available via subscription   (7 followers)
Acta Chemica Iasi     Open Access  
Acta Chimica Slovaca     Open Access   (5 followers)
Acta Chromatographica     Full-text available via subscription   (9 followers)
Acta Facultatis Medicae Naissensis     Open Access   (1 follower)
Acta Metallurgica Sinica (English Letters)     Hybrid Journal   (2 followers)
adhäsion KLEBEN & DICHTEN     Hybrid Journal   (1 follower)
Adhesion Adhesives & Sealants     Hybrid Journal   (3 followers)
Adsorption Science & Technology     Full-text available via subscription   (5 followers)
Advanced Functional Materials     Hybrid Journal   (29 followers)
Advances in Chemical Engineering and Science     Open Access   (19 followers)
Advances in Chemical Science     Open Access   (6 followers)
Advances in Colloid and Interface Science     Full-text available via subscription   (12 followers)
Advances in Drug Research     Full-text available via subscription   (13 followers)
Advances in Fluorine Science     Full-text available via subscription   (6 followers)
Advances in Fuel Cells     Full-text available via subscription   (10 followers)
Advances in Heterocyclic Chemistry     Full-text available via subscription   (6 followers)
Advances in Materials Physics and Chemistry     Open Access   (7 followers)
Advances in Nanoparticles     Open Access   (9 followers)
Advances in Organometallic Chemistry     Full-text available via subscription   (7 followers)
Advances in Polymer Science     Hybrid Journal   (35 followers)
Advances in Protein Chemistry     Full-text available via subscription   (4 followers)
Advances in Protein Chemistry and Structural Biology     Full-text available via subscription   (8 followers)
Advances in Quantum Chemistry     Full-text available via subscription   (3 followers)
African Journal of Chemical Education     Open Access  
African Journal of Pure and Applied Chemistry     Open Access  
Afrique Science : Revue Internationale des Sciences et Technologie     Open Access  
Agrokémia és Talajtan     Full-text available via subscription   (2 followers)
Alchemy     Open Access   (2 followers)
Alkaloids: Chemical and Biological Perspectives     Full-text available via subscription   (3 followers)
AMB Express     Open Access   (1 follower)
Ambix     Hybrid Journal   (3 followers)
American Journal of Applied Sciences     Open Access   (27 followers)
American Journal of Biochemistry and Biotechnology     Open Access   (79 followers)
American Journal of Biochemistry and Molecular Biology     Open Access   (7 followers)
American Journal of Chemistry     Open Access   (14 followers)
American Journal of Plant Physiology     Open Access   (9 followers)
American Mineralogist     Full-text available via subscription   (2 followers)
Analyst     Full-text available via subscription   (33 followers)
Angewandte Chemie     Hybrid Journal   (12 followers)
Angewandte Chemie International Edition     Hybrid Journal   (142 followers)
Annales UMCS, Chemia     Open Access   (2 followers)
Annual Reports in Computational Chemistry     Full-text available via subscription   (1 follower)
Annual Reports Section A (Inorganic Chemistry)     Full-text available via subscription   (2 followers)
Annual Reports Section B (Organic Chemistry)     Full-text available via subscription   (4 followers)
Annual Review of Chemical and Biomolecular Engineering     Full-text available via subscription   (8 followers)
Annual Review of Food Science and Technology     Full-text available via subscription   (11 followers)
Anti-Infective Agents     Hybrid Journal   (1 follower)
Applied Organometallic Chemistry     Hybrid Journal   (3 followers)
Applied Spectroscopy     Full-text available via subscription   (11 followers)
Applied Surface Science     Hybrid Journal   (13 followers)
Arabian Journal of Chemistry     Full-text available via subscription   (5 followers)
ARKIVOC     Open Access   (1 follower)
Asian Journal of Biochemistry     Open Access   (1 follower)
Australian Journal of Chemistry     Hybrid Journal   (4 followers)
Autophagy     Full-text available via subscription  
Avances en Quimica     Open Access   (1 follower)
Biocell     Open Access  
Biochemical Pharmacology     Hybrid Journal   (5 followers)
Biochemistry     Full-text available via subscription   (120 followers)
Biochemistry Insights     Open Access   (3 followers)
Biochemistry Research International     Open Access   (3 followers)
BioChip Journal     Hybrid Journal   (1 follower)
Bioinorganic Chemistry and Applications     Open Access   (4 followers)
Biointerface Research in Applied Chemistry     Open Access   (1 follower)
Biointerphases     Open Access  
Biomacromolecules     Full-text available via subscription   (16 followers)
Biomass Conversion and Biorefinery     Partially Free   (5 followers)
Biomedical Chromatography     Hybrid Journal   (7 followers)
Biomolecular NMR Assignments     Hybrid Journal   (2 followers)
BioNanoScience     Partially Free   (4 followers)
Bioorganic & Medicinal Chemistry     Hybrid Journal   (26 followers)
Bioorganic & Medicinal Chemistry Letters     Hybrid Journal   (20 followers)
Bioorganic Chemistry     Hybrid Journal   (5 followers)
Biopolymers     Hybrid Journal   (12 followers)
Biosensors     Open Access   (3 followers)
Biotechnic and Histochemistry     Hybrid Journal   (1 follower)
Boletin de la Sociedad Chilena de Quimica     Open Access  
Bulletin of the Chemical Society of Ethiopia     Open Access   (1 follower)
Bulletin of the Chemical Society of Japan     Full-text available via subscription   (11 followers)
Canadian Association of Radiologists Journal     Full-text available via subscription   (3 followers)
Canadian Journal of Chemistry     Full-text available via subscription   (6 followers)
Canadian Mineralogist     Full-text available via subscription   (1 follower)
Carbohydrate Research     Hybrid Journal   (10 followers)
Carbon     Hybrid Journal   (33 followers)
Catalysis for Sustainable Energy     Open Access   (1 follower)
Catalysis Reviews: Science and Engineering     Hybrid Journal   (3 followers)
Catalysis Science and Technology     Free   (3 followers)
Catalysis Surveys from Asia     Hybrid Journal   (3 followers)
Catalysts     Open Access   (5 followers)
Cellulose     Hybrid Journal   (4 followers)
Central European Journal of Chemistry     Hybrid Journal   (5 followers)

        1 2 3 4 5 6 | Last

Biomolecular NMR Assignments    [4 followers]  Follow    
  Hybrid Journal Hybrid journal (It can contain Open Access articles)
     ISSN (Print) 1874-270X - ISSN (Online) 1874-2718
     Published by Springer-Verlag Homepage  [2187 journals]   [SJR: 0.402]   [H-I: 7]
  • Polypeptide backbone, C       class="a-plus-plus">β and methyl group
           resonance assignments of the 24 kDa plectin repeat domain 6 from
           human protein plectin
    • Abstract: Abstract The 500 kDa protein plectin is essential for the cytoskeletal organization of most mammalian cells and it is up-regulated in some types of cancer. Here, we report nearly complete sequence-specific polypeptide backbone, 13Cβ and methyl group resonance assignments for 24 kDa human plectin(4403–4606) containing the C-terminal plectin repeat domain 6.
      PubDate: 2014-04-11
       
  • NMR backbone resonance assignments of the N, P domains of CopA, a
           copper-transporting ATPase, in the apo and ligand bound states
    • Abstract: Abstract Copper-transporting ATPase, a member of P-type ATPase family, plays a key role in the homeostasis of cellular copper levels. Here, the backbone assignments of the directly connected N and P domains (292 residues, 31 kDa) of Cu-transporting ATPase in the ligand free and the AMPPCP-bound states are reported in solution. The NMR assignments pave the way for binding and dynamics studies of this enzyme to better understand its function.
      PubDate: 2014-04-05
       
  • 13C,        class="a-plus-plus">15N and        class="a-plus-plus">1H resonance assignments of
           receiver domain of ethylene receptor ETR1
    • Abstract: Abstract Ethylene plays versatile functions in regulating plant physiology. Although the high affinity ethylene receptor and its downstream regulators have been identified, the molecular recognition of the receptor interacting domains remains to be established. It has been speculated that the cytoplasmic signaling of the ethylene receptor is a two-component regulatory system involving the conserved receiver domain (RD). Here, we report the NMR chemical shift assignments for RD from Arabidopsis thaliana ethylene receptor ETR1. Nearly complete backbone and side-chain assignments were achieved at pH 6.0 and 25 °C. The assignments and backbone dynamics revealed the secondary structure and showed that ETR1-RD is a monomer in solution. These results will make it possible to monitor downstream binding partners and elucidates our understanding of phosphotransfer in the plant two-component regulatory system in the ethylene signaling pathway.
      PubDate: 2014-04-03
       
  • Solution NMR assignment of LpoB, an outer-membrane anchored
           Penicillin-Binding Protein activator from        class="a-plus-plus">Escherichia coli
    • Abstract: Abstract Bacteria surround their cytoplasmic membrane with the essential heteropolymer peptidoglycan (PG), which is made of glycan chains cross-linked by short peptides, to maintain osmotic stability and cell shape. PG is assembled from lipid II precursor by glycosyltransferase and transpeptidase reactions catalyzed by PG synthases, which are anchored to the cytoplasmic membrane and are controlled from inside the cell by cytoskeletal elements. Recently, two lipoproteins, LpoA and LpoB, were shown to be required in Escherichia coli for activating the main peptidoglycan synthases, Penicillin-Binding Proteins 1A and 1B, from the outer membrane. Here we present the backbone and side-chain assignment of the 1H, 13C and 15N resonances of LpoB from E. coli. We also provide evidence for a two-domain organization of LpoB and a largely disordered, 64 amino acid-long N-terminal domain.
      PubDate: 2014-04-02
       
  • Sequence-specific backbone        class="a-plus-plus">1H,        class="a-plus-plus">13C and        class="a-plus-plus">15N assignments of the
           catalytic domain of the        class="a-plus-plus">Escherichia coli protein
           tyrosine kinase, Wzc
    • Abstract: Abstract Protein tyrosine kinases in bacteria are structurally and functionally distinct from their eukaryotic counterparts. The largest family of bacterial tyrosine kinases, the BY-kinase family, is highly conserved in Gram-negative and Gram-positive species, and plays a central role in biofilm and capsule formation. In Escherichia coli the BY-kinase, Wzc, is a critical component of the machinery responsible for the synthesis and export of the exo-polysaccharide colanic acid, a key constituent of biofilms. Here we present the main-chain 1HN, 15N, 13C′ and 13Cα, side-chain 13Cβ resonance assignments for a construct that encodes the entire 274-residue cytosolic catalytic domain of Wzc.
      PubDate: 2014-04-01
       
  • 1H,        class="a-plus-plus">13C, and        class="a-plus-plus">15N chemical shift
           assignments of the phosphotyrosine binding domain 2 (PTB2) of human FE65
    • Abstract: Abstract Phosphotyrosine binding domains (PTB) are protein–protein interaction domains that play important roles in various cellular signal transduction pathways. The second phosphotyrosine binding domain (PTB2) of the human scaffolding protein FE65 interacts with the C-terminal part of the Amyloid Precursor Protein (APP) involved in Alzheimer’s disease. The structure of PTB2 in complex with a 32 amino acid fragment of APP has been solved previously by X-ray crystallography. Here, we report the NMR spectral assignments of the free FE65 PTB2. This provides the basis for further investigation of the interactions of PTB2 with peptides and small organic ligands with the aim of disrupting the PTB2-APP interaction.
      PubDate: 2014-04-01
       
  • Backbone 1H,        class="a-plus-plus">13C and        class="a-plus-plus">15N resonance assignments of
           human vaccinia-related kinase 1 (VRK1)
    • Abstract: Abstract Vaccinia-related kinase 1 (VRK1) is one of the mitotic kinases which play key roles in cell cycle control and chromatin modifications. To understand the biological role of the kinase and gain insights into its catalytic mechanism, we performed NMR assignments of catalytically active form of VRK1 with 361 amino acids residues. Here, we present the backbone NMR resonance assignments of the kinase.
      PubDate: 2014-04-01
       
  • 1H,        class="a-plus-plus">13C and        class="a-plus-plus">15N resonance assignments of
           an N-terminal domain of CHD4
    • Abstract: Abstract Chromatin-remodeling proteins have a pivotal role in normal cell function and development, catalyzing conformational changes in DNA that ultimately result in changes in gene expression patterns. Chromodomain helicase DNA-binding protein 4 (CHD4), the defining subunit of the nucleosome remodeling and deacetylase (NuRD) complex, is a nucleosome-remodeling protein of the SNF2/ISWI2 family, members of which contain two chromo domains and an ATP-dependent helicase module. CHD3, CHD4 and CHD5 also contain two contiguous PHD domains and have an extended N-terminal region that has not previously been characterized. We have identified a stable domain in the N-terminal region of CHD4 and report here the backbone and side chain resonance assignments for this domain at pH 7.5 and 25 °C (BMRB No. 18906).
      PubDate: 2014-04-01
       
  • 1H,        class="a-plus-plus">15N,        class="a-plus-plus">13C assignment and secondary
           structure determination of two domains of La protein from        class="a-plus-plus">D. discoideum
    • Abstract: Abstract Biosynthesis of RNA polymerase III transcripts requires binding of the La protein at their 3′ end. La is an abundant nuclear RNA-binding protein which protects the nascent transcripts from 3′ exonuclease degradation. Here, we report the high yield expression and preliminary structural analysis through NMR spectroscopy of two recombinant RNA binding domains (La motif and NRRM) from the La protein of Dictyostelium discoideum. Both recombinant protein constructs were well-folded and allowed for an almost complete sequence-specific assignment of the 15N and 13C labeled domains and their secondary structure prediction using PECAN online tool.
      PubDate: 2014-04-01
       
  • Chemical shift assignments and secondary structure prediction of the
           master biofilm regulator, SinR, from        class="a-plus-plus">Bacillus subtilis
    • Abstract: Abstract Bacillus subtilis is a soil-dwelling Gram-positive bacterial species that has been extensively studied as a model of biofilm formation and stress-induced cellular differentiation. The tetrameric protein, SinR, has been identified as a master regulator for biofilm formation and linked to the regulation of the early transition states during cellular stress response, such as motility and biofilm-linked biosynthetic genes. SinR is a 111-residue protein that is active as a dimer of dimers, composed of two distinct domains, a DNA-binding helix-turn-helix N-terminus domain and a C-terminal multimerization domain. In order for biofilm formation to proceed, the antagonist, SinI, must inactivate SinR. This interaction results in a dramatic structural rearrangement of both proteins. Here we report the full-length backbone and side chain chemical shift values in addition to the experimentally derived secondary structure predictions as the first step towards directly studying the complex interaction dynamics between SinR and SinI.
      PubDate: 2014-04-01
       
  • Solid-state NMR sequential assignments of the C-terminal oligomerization
           domain of human C4b-binding protein
    • Abstract: Abstract The complement 4 binding protein (C4bp) plays a crucial role in the inhibition of the complement cascade. It has an extraordinary seven-arm octopus-like structure with 7 tentacle-like identical chains, held together at their C-terminal end. The C-terminal domain does oligomerize in isolation, and is necessary and sufficient to oligomerize full-length C4bp. It is predicted to form a seven-helix coiled coil, and its multimerization properties make it a promising vaccine adjuvant, probably by enhancing the structural stability and binding affinity of the presented antigen. Here, we present the solid-state NMR resonance assignment of the human C4bp C-terminal oligomerization Domain, hC4pbOD, and the corresponding secondary chemical shifts.
      PubDate: 2014-04-01
       
  • Protein chemical shift assignments of the unbound and RNA-bound forms of
           the alternative splicing factor SUP-12 from        class="a-plus-plus">C. elegans
    • Abstract: Abstract The splicing factor SUP-12 from Caenorhabditis elegans binds to regulatory RNA elements in pre-mRNA in order to generate tissue-specific alternative splicing for genes such as the fibroblast growth factor receptor egl-15. In nematode muscle cells, SUP-12 promotes the use of a mutually exclusive exon to impart variant binding specificity to the EGL-15 extracellular protein domain. Here we report the side chain and backbone 1H, 13C and 15N chemical shift assignments for the bacterially expressed RNA recognition motif domain from SUP-12, both in isolation as well as bound to a short RNA derived from the intron sequence between exon 4 and exon 5B of egl-15. Comparison of protein chemical shift values for both the backbone and side chain nuclei, coupled with secondary chemical shift analysis, reveal initial details of the RNA recognition.
      PubDate: 2014-04-01
       
  • Resonance assignments for latherin, a natural surfactant protein from
           horse sweat
    • Abstract: Abstract Latherin is an intrinsically surfactant protein of ~23 kDa found in the sweat and saliva of horses. Its function is probably to enhance the translocation of sweat water from the skin to the surface of the pelt for evaporative cooling. Its role in saliva may be to enhance the wetting, softening and maceration of the dry, fibrous food for which equines are adapted. Latherin is unusual in its relatively high content of aliphatic amino acids (~25 % leucines) that might contribute to its surfactant properties. Latherin is related to the palate, lung, and nasal epithelium carcinoma-associated proteins (PLUNCs) of mammals, at least one of which is now known to exhibit similar surfactant activity to latherin. No structures of any PLUNC protein are currently available. 15N,13C-labelled recombinant latherin was produced in Escherichia coli, and essentially all of the resonances were assigned despite the signal overlap due to the preponderance of leucines. The most notable exceptions include a number of residues located in an apparently dynamic loop region between residues 145 and 154. The assignments have been deposited with BMRB accession number 19067.
      PubDate: 2014-04-01
       
  • Chemical shift assignments and secondary structure prediction of the
           phosphorelay protein VanU from        class="a-plus-plus">Vibrio anguillarum
    • Abstract: Abstract Vibrio anguillarum is a biofilm forming Gram-negative bacterium that survives prolonged periods in seawater and causes vibriosis in marine life. A quorum-sensing signal transduction pathway initiates biofilm formation in response to environmental stresses. The phosphotransferase protein VanU is the focal point of the quorum-sensing pathway and facilitates the regulation between independent phosphorelay systems that activate or repress biofilm formation. Here we report the 1H, 13C, and 15N backbone and side chain resonance assignments and secondary structure prediction for VanU from V. anguillarum.
      PubDate: 2014-04-01
       
  • 1H,        class="a-plus-plus">13C,        class="a-plus-plus">15N resonance assignments of
           murine hepatitis virus nonstructural protein 3a
    • Abstract: Abstract Nonstructural protein (nsp) 3 is the largest of 16 nsps translated from the murine hepatitis virus (MHV) genome. The N-terminal most domain of nsp3, nsp3a, has been identified by reverse genetics as a likely binding partner of MHV nucleocapsid protein. Here we report the backbone and side chain resonance assignments of MHV nsp3a (residues 1-114).
      PubDate: 2014-04-01
       
  • Backbone and partial side chain assignment of the microtubule binding
           domain of the MAP1B light chain
    • Abstract: Abstract Microtubule-associated protein 1B (MAP1B) is a classical high molecular mass microtubule-associated protein expressed at high levels in the brain. It confers specific properties to neuronal microtubules and is essential for neuronal differentiation, brain development and synapse maturation. Misexpression of the protein contributes to the development of brain disorders in humans. However, despite numerous reports demonstrating the importance of MAP1B in regulation of the neuronal cytoskeleton during neurite extension and axon guidance, its mechanism of action is still elusive. Here we focus on the intrinsically disordered microtubule binding domain of the light chain of MAP1B. In order to obtain more detailed structural information about this domain we assigned NMR chemical shifts of backbone and aliphatic side chain atoms.
      PubDate: 2014-04-01
       
  • 1H,        class="a-plus-plus">13C and        class="a-plus-plus">15N resonance assignments of
           S114A mutant of UVI31+ from        class="a-plus-plus">Chlamydomonas reinhardtii
    • Abstract: Abstract Almost complete sequence specific 1H, 13C and 15N resonance assignments of S114A mutant of UVI31+ from Chlamydomonas reinhardtii are reported. The cDNA of S114A mutant of UVI31+ was cloned from a eukaryotic green algae (C. reinhardtii) and overexpressed in E.coli from where the protein was purified to homogeneity. The point mutation S114A in UVI31+ reduces its DNA endonuclease activity substantially as compared with its wild type. As a prelude to the structural characterization of S114A mutant of UVI31+, we report here complete sequence-specific 1H, 13C and 15N NMR assignments.
      PubDate: 2014-04-01
       
  • Backbone and ILV methyl resonance assignments of        class="a-plus-plus">E. coli thymidylate synthase
           bound to cofactor and a nucleotide analogue
    • Abstract: Abstract Thymidylate synthase (TSase) is a 62 kDa homodimeric enzyme required for de novo synthesis of thymidine monophosphate in most organisms. This makes the enzyme an excellent target for anticancer and microbial antibiotic drugs. In addition, TSase has been shown to exhibit negative cooperativity and half-the-sites reactivity. For these collective reasons, TSase is widely studied, and much is known about its kinetics and structure as it progresses through a multi-step catalytic cycle. Recently, nuclear magnetic resonance spin relaxation has been instrumental in demonstrating the critical role of dynamics in enzyme function in small model systems. These studies raise questions about how dynamics affect function in larger enzymes with more complex reaction coordinates. TSase is an ideal candidate given its size, oligomeric state, cooperativity, and status as a drug target. Here, as a pre-requisite to spin relaxation studies, we present the backbone and ILV methyl resonance assignments of TSase from Escherichia coli bound to a substrate analogue and cofactor.
      PubDate: 2014-04-01
       
  • Backbone resonance assignment of the HEAT1-domain of the human eukaryotic
           translation initiation factor 4GI
    • Abstract: Abstract Controlling translation during protein synthesis is crucial for cell proliferation and differentiation. Protein translation is orchestrated by an assembly of various protein components at the ribosomal subunits. The eukaryotic translation initiation factor 4G (eIF4G) plays an important role in the formation of the translation initiation complex eIF4F consisting of eIF4G, the ATP dependent RNA helicase eIF4A and the cap binding protein eIF4E. One of the functions of eIF4G is the enhancement of the activity of eIF4A facilitated mainly through binding to the HEAT1 domain of eIF4G. In order to understand the interaction of HEAT1 with eIF4A and other components during translation initiation backbone assignment is essential. Here we report the 1H, 13C and 15N backbone assignment for the HEAT1 domain of human eIF4G isoform I (eIF4GI-HEAT1), the first of three HEAT domains of eIF4G (29 kDa) as a basis for the elucidation of its structure and interactions with its binding partners, necessary for understanding the mechanism of its biological function.
      PubDate: 2014-04-01
       
  • Backbone 1H,        class="a-plus-plus">13C,        class="a-plus-plus">15N NMR assignments of yeast
           OMP synthase in unliganded form and in complex with orotidine
           5′-monophosphate
    • Abstract: Abstract The type I phosphoribosyltransferase OMP synthase (EC 2.4.2.10) is involved in de novo synthesis of pyrimidine nucleotides forming the UMP precursor orotidine 5′-monophosphate (OMP). The homodimeric enzyme has a Rossman α/β core topped by a base-enclosing “hood” domain and a flexible domain-swapped catalytic loop. High-resolution X-ray structures of the homologous Salmonella typhimurium and yeast enzymes show that a general compacting of the core as well as movement of the hood and a major disorder-to-order transition of the loop occur upon binding of ligands MgPRPP and orotate. Here we present backbone NMR assignments for the unliganded yeast enzyme (49 kDa) and its complex with product OMP. We were able to assign 212–213 of the 225 non-proline backbone 15N and amide proton resonances. Significant difference in chemical shifts of the amide cross peaks occur in regions of the structure that undergo movement upon ligand occupancy in the S. typhimurium enzyme.
      PubDate: 2014-04-01
       
 
 
JournalTOCs
School of Mathematical and Computer Sciences
Heriot-Watt University
Edinburgh, EH14 4AS, UK
Email: journaltocs@hw.ac.uk
Tel: +00 44 (0)131 4513762
Fax: +00 44 (0)131 4513327
 
About JournalTOCs
API
Help
News (blog, publications)
JournalTOCs on Twitter   JournalTOCs on Facebook

JournalTOCs © 2009-2014