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CHEMISTRY (602 journals)                  1 2 3 4 | Last

Showing 1 - 200 of 735 Journals sorted alphabetically
2D Materials     Hybrid Journal   (Followers: 5)
Accreditation and Quality Assurance: Journal for Quality, Comparability and Reliability in Chemical Measurement     Hybrid Journal   (Followers: 25)
ACS Catalysis     Full-text available via subscription   (Followers: 26)
ACS Chemical Neuroscience     Full-text available via subscription   (Followers: 15)
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ACS Photonics     Full-text available via subscription   (Followers: 6)
ACS Synthetic Biology     Full-text available via subscription   (Followers: 16)
Acta Chemica Iasi     Open Access  
Acta Chimica Sinica     Full-text available via subscription  
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Acta Chromatographica     Full-text available via subscription   (Followers: 8)
Acta Facultatis Medicae Naissensis     Open Access  
Acta Metallurgica Sinica (English Letters)     Hybrid Journal   (Followers: 4)
Acta Scientifica Naturalis     Open Access  
adhäsion KLEBEN & DICHTEN     Hybrid Journal   (Followers: 5)
Adhesion Adhesives & Sealants     Hybrid Journal   (Followers: 6)
Adsorption Science & Technology     Full-text available via subscription   (Followers: 4)
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African Journal of Bacteriology Research     Open Access  
African Journal of Chemical Education     Open Access   (Followers: 2)
African Journal of Pure and Applied Chemistry     Open Access   (Followers: 6)
Agrokémia és Talajtan     Full-text available via subscription   (Followers: 2)
Alchemy : Jurnal Penelitian Kimia     Open Access  
Alkaloids: Chemical and Biological Perspectives     Full-text available via subscription   (Followers: 3)
AMB Express     Open Access   (Followers: 1)
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American Journal of Biochemistry and Biotechnology     Open Access   (Followers: 61)
American Journal of Biochemistry and Molecular Biology     Open Access   (Followers: 13)
American Journal of Chemistry     Open Access   (Followers: 23)
American Journal of Plant Physiology     Open Access   (Followers: 12)
American Mineralogist     Full-text available via subscription   (Followers: 8)
Anadolu University Journal of Science and Technology     Open Access  
Analyst     Full-text available via subscription   (Followers: 41)
Angewandte Chemie     Hybrid Journal   (Followers: 119)
Angewandte Chemie International Edition     Hybrid Journal   (Followers: 167)
Annales UMCS, Chemia     Open Access   (Followers: 1)
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Annual Review of Chemical and Biomolecular Engineering     Full-text available via subscription   (Followers: 9)
Annual Review of Food Science and Technology     Full-text available via subscription   (Followers: 13)
Anti-Infective Agents     Hybrid Journal   (Followers: 3)
Antiviral Chemistry and Chemotherapy     Full-text available via subscription  
Applied Organometallic Chemistry     Hybrid Journal   (Followers: 5)
Applied Spectroscopy     Full-text available via subscription   (Followers: 23)
Applied Surface Science     Hybrid Journal   (Followers: 22)
Arabian Journal of Chemistry     Open Access   (Followers: 6)
ARKIVOC     Open Access   (Followers: 2)
Asian Journal of Biochemistry     Open Access   (Followers: 1)
Atomization and Sprays     Full-text available via subscription   (Followers: 3)
Australian Journal of Chemistry     Hybrid Journal   (Followers: 4)
Autophagy     Hybrid Journal   (Followers: 2)
Avances en Quimica     Open Access   (Followers: 1)
Biochemical Pharmacology     Hybrid Journal   (Followers: 7)
Biochemistry     Full-text available via subscription   (Followers: 220)
Biochemistry Insights     Open Access   (Followers: 4)
Biochemistry Research International     Open Access   (Followers: 5)
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Bioinspired Materials     Open Access   (Followers: 2)
Biointerface Research in Applied Chemistry     Open Access   (Followers: 1)
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Biomacromolecules     Full-text available via subscription   (Followers: 17)
Biomass Conversion and Biorefinery     Partially Free   (Followers: 11)
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Biomolecular NMR Assignments     Hybrid Journal   (Followers: 2)
BioNanoScience     Partially Free   (Followers: 4)
Bioorganic & Medicinal Chemistry     Hybrid Journal   (Followers: 92)
Bioorganic & Medicinal Chemistry Letters     Hybrid Journal   (Followers: 83)
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Bitácora Digital     Open Access  
Boletin de la Sociedad Chilena de Quimica     Open Access  
Bulletin of the Chemical Society of Ethiopia     Open Access   (Followers: 3)
Bulletin of the Chemical Society of Japan     Full-text available via subscription   (Followers: 25)
Bulletin of the Korean Chemical Society     Hybrid Journal  
C - Journal of Carbon Research     Open Access   (Followers: 2)
Canadian Association of Radiologists Journal     Full-text available via subscription   (Followers: 2)
Canadian Journal of Chemistry     Full-text available via subscription   (Followers: 6)
Canadian Mineralogist     Full-text available via subscription   (Followers: 3)
Carbohydrate Research     Hybrid Journal   (Followers: 27)
Carbon     Hybrid Journal   (Followers: 65)
Catalysis for Sustainable Energy     Open Access   (Followers: 5)
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Catalysis Science and Technology     Free   (Followers: 5)
Catalysis Surveys from Asia     Hybrid Journal   (Followers: 3)
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Chemical and Engineering News     Free   (Followers: 11)
Chemical Bulletin of Kazakh National University     Open Access  
Chemical Communications     Full-text available via subscription   (Followers: 63)
Chemical Engineering Research and Design     Hybrid Journal   (Followers: 21)
Chemical Research in Chinese Universities     Hybrid Journal   (Followers: 3)
Chemical Research in Toxicology     Full-text available via subscription   (Followers: 17)
Chemical Reviews     Full-text available via subscription   (Followers: 125)
Chemical Science     Open Access   (Followers: 18)
Chemical Technology     Open Access   (Followers: 11)
Chemical Vapor Deposition     Hybrid Journal   (Followers: 4)
Chemical Week     Full-text available via subscription   (Followers: 7)
Chemie in Unserer Zeit     Hybrid Journal   (Followers: 52)
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Chemistry - A European Journal     Hybrid Journal   (Followers: 115)
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Chemistry and Materials Research     Open Access   (Followers: 15)
Chemistry Central Journal     Open Access   (Followers: 5)
Chemistry Education Research and Practice     Free   (Followers: 4)
Chemistry in Education     Open Access   (Followers: 2)
Chemistry International     Hybrid Journal   (Followers: 1)
Chemistry Letters     Full-text available via subscription   (Followers: 43)
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Chemoecology     Hybrid Journal   (Followers: 2)
Chemometrics and Intelligent Laboratory Systems     Hybrid Journal   (Followers: 15)
Chemosensors     Open Access  
ChemPhysChem     Hybrid Journal   (Followers: 6)
ChemTexts     Hybrid Journal  
CHIMIA International Journal for Chemistry     Full-text available via subscription   (Followers: 3)
Chinese Journal of Chemistry     Hybrid Journal   (Followers: 6)
Chinese Journal of Polymer Science     Hybrid Journal   (Followers: 10)
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Clay Minerals     Full-text available via subscription   (Followers: 9)
Cogent Chemistry     Open Access  
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Colloid and Polymer Science     Hybrid Journal   (Followers: 8)
Colloids and Surfaces B: Biointerfaces     Hybrid Journal   (Followers: 6)
Combinatorial Chemistry & High Throughput Screening     Hybrid Journal   (Followers: 4)
Combustion Science and Technology     Hybrid Journal   (Followers: 19)
Comments on Inorganic Chemistry: A Journal of Critical Discussion of the Current Literature     Hybrid Journal   (Followers: 1)
Composite Interfaces     Hybrid Journal   (Followers: 3)
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        1 2 3 4 | Last

Journal Cover Biomolecular NMR Assignments
  [SJR: 0.325]   [H-I: 10]   [2 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  [2335 journals]
  • 1 H, 13 C, and 15 N resonance assignments and secondary structure
           information for Methylobacterium extorquens PqqD and the complex of PqqD
           with PqqA
    • Authors: Robert L. Evans; John A. Latham; Judith P. Klinman; Carrie M. Wilmot; Youlin Xia
      Abstract: Abstract The ribosomally synthesized and post-translationally modified peptide (RiPP), pyrroloquinoline quinone (PQQ), is a dehydrogenase cofactor synthesized by, but not exclusively used by, certain prokaryotes. RiPPs represent a rapidly expanding and diverse class of natural products—many of which have therapeutic potential—and the biosynthetic pathways for these are gaining attention. Five gene products from the pqq operon (PqqA, PqqB, PqqC, PqqD, and PqqE) are essential for PQQ biosynthesis. The substrate is the peptide PqqA, which is presented to the radical SAM enzyme PqqE by the small protein PqqD. PqqA is unstructured in solution, and only binds to PqqE when in complex with PqqD. PqqD is a member of a growing family of RiPP chaperone proteins (or domains in most cases) that present their associated peptide substrates to the initial RiPP biosynthesis enzymes. An X-ray crystal structure exists for dimeric Xanthomonas campestris PqqD (PDB ID: 3G2B), but PqqD is now known to act as a monomer under physiological conditions. In this study, the PqqD truncation from naturally fused Methylobacterium extorquens (Mex) PqqCD was overexpressed in Escherichia coli and MexPqqA was chemically synthesized. Solution NMR 1H-,15N-HSQC chemical shift studies have identified the PqqD residues involved in binding PqqA, and 1H, 13C, and 15N peak assignments for PqqD alone and for PqqD bound to PqqA are reported herein.
      PubDate: 2016-09-16
      DOI: 10.1007/s12104-016-9705-8
  • NMR study of Met-1 human Angiogenin: 1 H, 13 C, 15 N backbone and
           side-chain resonance assignment
    • Authors: Aikaterini C. Tsika; Demetra S. M. Chatzileontiadou; Demetres D. Leonidas; Georgios A. Spyroulias
      Abstract: Abstract Here, we report the high yield expression and preliminary structural analysis via solution hetero-nuclear NMR spectroscopy of the recombinant Met-1 human Angiogenin. The analysis reveals a well folded as well as, a monomeric polypeptide. Τhe sequence-specific assignment of its 1H, 15N and 13C resonances at high percentage was obtained. Also, using TALOS+ its secondary structure elements were determined.
      PubDate: 2016-09-13
      DOI: 10.1007/s12104-016-9704-9
  • 1 H, 13 C, 15 N backbone and side-chain resonance assignment of Nostoc sp.
           C139A variant of the heme–nitric oxide/oxygen binding (H-NOX) domain
    • Authors: Ioannis I. Alexandropoulos; Aikaterini I. Argyriou; Kostas D. Marousis; Stavros Topouzis; Andreas Papapetropoulos; Georgios A. Spyroulias
      Abstract: Abstract The H-NOX (Heme-nitric oxide/oxygen binding) domain is conserved across eukaryotes and bacteria. In human soluble guanylyl cyclase (sGC) the H-NOX domain functions as a sensor for the gaseous signaling agent nitric oxide (NO). sGC contains the heme-binding H-NOX domain at its N-terminus, which regulates the catalytic site contained within the C-terminal end of the enzyme catalyzing the conversion of GTP (guanosine 5′-triphosphate) to GMP (guanylyl monophosphate). Here, we present the backbone and side-chain assignments of the 1H, 13C and 15N resonances of the 183-residue H-NOX domain from Nostoc sp. through solution NMR.
      PubDate: 2016-09-10
      DOI: 10.1007/s12104-016-9707-6
  • Chemical shift assignments of nsp7α from porcine reproductive and
           respiratory syndrome virus
    • Authors: Jiaping Chen; Xiaodong Xu; Hu Tao; Yuanyuan Wang; Hongying Chen
      Abstract: Abstract Porcine reproductive and respiratory syndrome virus (PRRSV) is the causative agent of porcine reproductive and respiratory syndrome, a destructive disease of swine. PRRSV has a single strand positive-sense RNA genome which contains at least ten open reading frames, of these, ORF1a and ORF1b encode polyproteins pp1a and pp1ab. Subsequently, pp1a is cleaved into ten nonstructural proteins, including nonstructural protein 7α and 7β (nsp7α and 7β), the internal cleavage products of a conserved nonstructural protein nsp7. Nsp7 plays a role in provoking the humoral immune system into producing anti-nsp7 antibodies which can be highly and persistently expressed in PRRSV-infected swine. However, the functions of nsp7α and 7β remain unknown. Western blot and radioimmunoprecipitation analysis of the two proteins showed that only cleaved nsp7α was detectable and cleaved nsp7β was not detected in the infected cells. Here, we reported the 1H, 13C and 15N resonance assignment of nsp7α from PRRSV as a basis for further structural and functional studies.
      PubDate: 2016-09-09
      DOI: 10.1007/s12104-016-9706-7
  • Chemical shift assignment of the intrinsically disordered N-terminus and
           the rubredoxin domain in the folded metal bound and unfolded oxidized
           state of mycobacterial protein kinase G
    • Authors: Matthias Wittwer; Sonja A. Dames
      Abstract: Abstract Mycobacterium tuberculosis protein kinase G (PknG) is a 82 kDa multidomain eukaryotic-like serine/threonine kinase mediating the survival of pathogenic mycobacteria within host macrophages. The N-terminal sequence preceding the catalytic kinase domain contains an approximately 75 residues long tail, which was predicted to show no regulatory secondary structure (1–75 = NORS) but harbors the major in vivo phosphorylation site (T63), and a rubredoxin-like metal binding motif (74–147 = RD). In the reduced rubredoxin motif, four conserved cysteine residues that are present as two C-X-X-C-G motifs coordinate a metal ion. The cysteines are further involved in sensing the redox environment to regulate PknG catalytic activity. Here, we report the 1H, 13C, and 15N resonance assignments of the highly dynamic unstructured N-terminal region NORS and the RD in the reduced, metal bound, presumably folded and the oxidized, presumably unfolded state. Chemical shifts have been deposited at the BioMagResBank under the BMRB accession numbers 26,028 for the His-PknG1–147 with the RD in reduced, metal bound state, 26,027 for His-PknG1–75, and 26,030 and 26,029 for PknG74–147 either in the reduced, metal bound or oxidized state, respectively. The presented chemical shift assignments pave the route for the structural characterization of the regulation of PknG by redox changes and posttranslational modifications (phosphorylation).
      PubDate: 2016-09-08
      DOI: 10.1007/s12104-016-9708-5
  • Secondary structure and 1 H, 13 C and 15 N resonance assignments of
           Skint-1: a selecting ligand for a murine γδ T cell subset implicated in
           tumour suppression
    • Authors: M. Salim; C. R. Willcox; F. Mohammed; A. C. Hayday; M. Overduin; B. E. Willcox; T. J. Knowles
      Abstract: Abstract A study describing the 1H, 13C and 15N backbone and side chain chemical shift assignments and secondary structure of Skint-1 a prototypic member of a family of mouse genes, of which Skint-1 is involved in the development of the dendritic epidermal T cell (DETC) subset of γδ T cells.
      PubDate: 2016-08-04
      DOI: 10.1007/s12104-016-9700-0
  • 1 H, 13 C and 15 N resonance assignments for the response regulator CheY 3
           from Rhodobacter sphaeroides
    • Authors: Lorena Varela; Christian H. Bell; Judith P. Armitage; Christina Redfield
      Abstract: Abstract Rhodobacter sphaeroides has emerged as a model system for studies of the complex chemotaxis pathways that are a hallmark of many non-enteric bacteria. The genome of R. sphaeroides encodes two sets of flagellar genes, fla1 and fla2, that are controlled by three different operons. Each operon encodes homologues of most of the proteins required for the well-studied E. coli chemotaxis pathway. R. sphaeroides has six homologues of the response regulator CheY that are localized to and are regulated by different clusters of chemosensory proteins in the cell and have different effects on chemotaxis. CheY6 is the major CheY stopping the fla1 flagellar motor and associated with a cytoplasmically localised chemosensory pathway. CheY3 and CheY4 are associated with a membrane localised polar chemosensory cluster, and can bind to but not stop the motor. CheY6 and either CheY3 or CheY4 are required for chemotaxis. We are using NMR spectroscopy to characterise and compare the structure and dynamics of CheY3 and CheY6 in solution. We are interested in defining the conformational changes that occur upon activation of these two proteins and to identify differences in their properties that can explain the different functions they play in chemotaxis in R. sphaeroides. Here we present the 1H, 13C and 15N assignments for CheY3 in its active, inactive and Mg2+-free apo form. These assignments provide the starting point for detailed investigations of the structure and function of CheY3.
      PubDate: 2016-07-29
      DOI: 10.1007/s12104-016-9703-x
  • 1 H, 15 N and 13 C resonance assignments of the C-terminal domain of
           Vibrio cholerae TolA protein
    • Authors: Romain Navarro; Olivier Bornet; Laetitia Houot; Roland Lloubes; Françoise Guerlesquin; Matthieu Nouailler
      Abstract: Abstract Vibrio cholerae is the bacterial causative agent of the human disease cholera. Non-pathogenic bacterium can be converted to pathogenic following infection by a filamentous phage, CTXΦ, that carries the cholera toxin encoding genes. A crucial step during phage infection requires a direct interaction between the CTXΦ minor coat protein (pIIICTX) and the C-terminal domain of V. cholerae TolA protein (TolAIIIvc). In order to get a better understanding of TolA function during the infection process, we have initiated a study of the V. cholerae TolAIII domain by 2D and 3D heteronuclear NMR. With the exception of the His-tag (H123–H128), 97 % of backbone 1H, 15N and 13C resonances were assigned and the side chain assignments for 92 % of the protein were obtained (BMRB deposit with accession number 25689).
      PubDate: 2016-07-19
      DOI: 10.1007/s12104-016-9690-y
  • 1 H, 15 N, 13 C resonance assignments for pyrazinoic acid binding domain
           of ribosomal protein S1 from Mycobacterium tuberculosis
    • Authors: Biling Huang; Jinglin Fu; Chenyun Guo; Xueji Wu; Donghai Lin; Xinli Liao
      Abstract: Abstract Ribosomal protein S1 of Mycobacterium tuberculosis (MtRpsA) binds to ribosome and mRNA, and plays significant role in the regulation of translation initiation, conventional protein synthesis and transfer-messenger RNA (tmRNA) mediated trans-translation. It has been identified as the target of pyrazinoic acid (POA), a bactericidal moiety from hydrolysis of pyrazinamide, which is a mainstay of combination therapy for tuberculosis. POA prevented the interactions between the C-terminal S1 domain of MtRpsA (residues 280–368, MtRpsACTD_S1) and tmRNA; so that POA can inhibit the trans-translation, which is a key component of multiple quality control pathways in bacteria. However, the details of molecular mechanism and dynamic characteristics for MtRpsACTD_S1 interactions with POA, tmRNA or mRNA are still unclear. Here we present the 1H, 15N, 13C resonance assignments of MtRpsACTD_S1 as well as the secondary structure information based on backbone chemical shifts, which lay foundation for further solution structure determination, dynamic properties characterization and interactions investigation between MtRpsACTD_S1 and tmRNA, RNA or POA.
      PubDate: 2016-07-13
      DOI: 10.1007/s12104-016-9692-9
  • 1 H, 13 C and 15 N backbone resonance assignments and dynamic properties
           of the PDZ tandem of Whirlin
    • Authors: Florent Delhommel; Nicolas Wolff; Florence Cordier
      Abstract: Abstract Mammals perceive sounds thanks to mechanosensory hair cells located in the inner ear. The stereocilia of these cells are tightly bound together in bundles by a network of cadherins and scaffolding proteins. Stereocilia deflection induces stretching of this network and is responsible for hair cell depolarization that triggers the neuronal message, transducing the mechanical signal into an electric signal transmissible to the brain. Nearly all proteins involved in this mechano-electrical transduction network contain short C-terminal motifs of interaction with PDZ domains (PSD-95, Discs Large, ZO-1). Interestingly only two of these proteins encompass PDZ domains: Harmonin and Whirlin. As our first step towards a comprehensive structural study of Whirlin, we have assigned the 1H, 13C and 15N backbone resonances of a tandem formed by the first two PDZ domains of Whirlin, reported the secondary structure elements of this tandem as predicted by the TALOS+ server and evaluated its dynamics from 15N relaxation measurements.
      PubDate: 2016-07-09
      DOI: 10.1007/s12104-016-9701-z
  • Backbone and side chain assignments of human cell cycle regulatory protein
           S-phase kinase-associated protein 1
    • Authors: Nitin Nathubhai Kachariya; Sarath Chandra Dantu; Ashutosh Kumar
      Abstract: Abstract Ubiquitination of proteins is required to regulate several cellular mechanisms in cells. Skp1-Cullin-1-F-box (SCF), the largest family of the RING E3 ligases, recognizes and carries out the poly-ubiquitination of many substrate proteins. SCF E3 ligase is a multi-component protein complex, and the human S-phase kinase-associated protein 1 (Skp1) is the adapter protein, which binds and presents the substrate binding protein F-box (FBP) to the rest of the E3 ligase. Several crystallographic studies have solved the partial structure of Skp1 in complex with various FBPs, but there is no structure of standalone Skp1. Understanding the conformational and structural properties of Skp1 with and without FBPs is required to understand the complete mechanism of poly-ubiquitination. Here, we report ~90 % backbone and 64 % side chain 1H, 13C, 15N assignments of Skp1 protein using various double and triple resonance NMR experiments.
      PubDate: 2016-07-09
      DOI: 10.1007/s12104-016-9699-2
  • Resonance assignments of a VapC family toxin from Clostridium thermocellum
    • Authors: Chen Wang; Jinsong Xuan; Qiu Cui; Yingang Feng
      Abstract: Abstract Toxin–antitoxin (TA) systems widely exist in bacterial plasmids, phages, and chromosomes and play important roles in growth persistence and host-pathogen interaction. Virulence associated protein BC (VapBC) family TAs are the most abundant TAs in bacteria and many pathogens contain a large number of vapBC loci in the genome which have been extensively studied. Clostridium thermocellum, a cellulolytic anaerobic gram-positive bacterium with promising applications in biofuel production, also contains a VapBC TA in the genome. Despite the structures of several VapBC family TAs have been determined, the toxin and anti-toxin components of C. thermocellum VapBC have very low sequence identity to the proteins in PDB. Therefore, the structure and functional mechanism of this TA is largely unknown. Here we reported the NMR resonance assignments of the VapC toxin from C. thermocellum as a basis for further structural and functional studies.
      PubDate: 2016-07-08
      DOI: 10.1007/s12104-016-9702-y
  • 1 H, 13 C and 15 N backbone resonance assignment for the 40.5 kDa
           catalytic domain of Ubiquitin Specific Protease 7 (USP7)
    • Authors: Paola Di Lello; Lionel Rougé; Borlan Pan; Till Maurer
      Abstract: Abstract The deubiquitinase Ubiquitin Specific Protease 7 (USP7) is part of the regulatory cascade of proteins that modulates the activity of the tumor suppressor protein p53. Deubiquitination of its target Murine Double Minute 2 (MDM2) leads to increased proteosomal degradation of p53. Consequently, USP7 has emerged as an attractive oncology target because its inhibition stabilizes p53, thereby promoting p53-dependent apoptosis in cancer cells. Here we report the backbone resonance assignment for the 40.5 kDa catalytic domain of USP7.
      PubDate: 2016-07-08
      DOI: 10.1007/s12104-016-9698-3
  • Chemical shift assignments of the homodimer protein SP_0782 (7–79) from
           Streptococcus pneumoniae
    • Authors: Shuangli Li; Theresa A. Ramelot; Michael A. Kennedy; Maili Liu; Yunhuang Yang
      Abstract: Abstract The protein SP_0782 from Streptococcus pneumonia is a small homodimeric protein that belongs to a protein family containing representative members with single-stranded DNA (ssDNA) binding functions. The ssDNA binding of the homolog YdbC from Lactococcus lactis was previously characterized when bound to a 20-mer of pyridine-rich ssDNA, sharing an overall similar structural fold with the human transcription coactivator PC4. We report that SP_0782 exhibits distinct differences in ssDNA binding properties from YdbC as revealed by NMR titration experiments. Unlike the binding of the ssDNA dT19G1 to PC4 and YdbC, SP_0782 resulted in aggregation. In addition, SP_0782 exhibits favorable binding to shorter ssDNA such as dT6. The reason is unclear, and the SP_0782 structure–function relationship remains to be elucidated. Here, we report the complete 1H, 13C, and 15N backbone and side chain NMR assignments of SP_0782, residues 7–79.
      PubDate: 2016-07-07
      DOI: 10.1007/s12104-016-9697-4
  • 1 H, 15 N, and 13 C resonance assignments of Staphylococcus aureus
           extracellular adherence protein domain 4
    • Authors: Jordan L. Woehl; Daisuke Takahashi; Alvaro I. Herrera; Brian V. Geisbrecht; Om Prakash
      Abstract: Abstract The pathogenic bacterium Staphylococcus aureus has evolved to actively evade many aspects of the human innate immune system by expressing a series of secreted inhibitory proteins. Among these, the extracellular adherence protein (Eap) has been shown to inhibit the classical and lectin pathways of the complement system. By binding to complement component C4b, Eap is able to inhibit formation of the CP/LP C3 pro-convertase. Secreted full-length, mature Eap consists of four ~98 residue domains, all of which adopt a similar beta-grasp fold, and are connected through a short linker region. Through multiple biochemical approaches, it has been determined that the third and fourth domains of Eap are responsible for C4b binding. Here we report the backbone and side-chain resonance assignments of the 11.3 kDa fourth domain of Eap. The assignment data has been deposited in the BMRB database under the accession number 26726.
      PubDate: 2016-07-02
      DOI: 10.1007/s12104-016-9688-5
  • Backbone resonance assignments for the SET domain of the human
           methyltransferase NSD2
    • Authors: Romel Bobby; Karolina Peciak; Alexander G. Milbradt
      Abstract: Abstract Aberrant NSD2 methyltransferase activity is implicated as the oncogenic driver in multiple myeloma, suggesting opportunities for novel therapeutic intervention. The methyltransferase activity of NSD2 resides in its catalytic SET domain, which is conserved among most lysine methyltransferases. Here we report the backbone \(\hbox {H}^{\mathrm{N}}\) , N, C \(^{\prime }\) , \(\hbox {C}^\alpha\) and side-chain \(\hbox {C}^\beta\) assignments of a 25 kDa NSD2 SET domain construct, spanning residues 991–1203. A chemical shift analysis of C \(^{\prime }\) , \(\hbox {C}^\alpha\) and \(\hbox {C}^\beta\) resonances predicts a secondary structural pattern that is in agreement with homology models.
      PubDate: 2016-07-01
      DOI: 10.1007/s12104-016-9689-4
  • NMR backbone resonance assignment and solution secondary structure
           determination of human NSD1 and NSD2
    • Authors: Nader Amin; Daniel Nietlispach; Seema Qamar; Joe Coyle; Elisabetta Chiarparin; Glyn Williams
      Abstract: Abstract Proteins of the NSD family are histone-methyl transferases with critical functions in the regulation of chromatin structure and function. NSD1 and NSD2 are homologous proteins that function as epigenetic regulators of transcription through their abilities to catalyse histone methylation. Misregulation of NSD1 and NSD2 expression or mutations in their genes are linked to a number of human diseases such as Sotos syndrome, and cancers including acute myeloid leukemia, multiple myeloma, and lung cancer. The catalytic domain of both proteins contains a conserved SET domain which is involved in histone methylation. Here we report the backbone resonance assignments and secondary structure information of the catalytic domains of human NSD1 and NSD2.
      PubDate: 2016-06-29
      DOI: 10.1007/s12104-016-9691-x
  • Chemical shift assignments and secondary structure prediction for Q4DY78,
           a conserved kinetoplastid-specific protein from Trypanosoma cruzi
    • Authors: Éverton Dias D’Andréa; Anne Diehl; Peter Schmieder; Hartmut Oschkinat; José Ricardo Pires
      Abstract: Abstract Trypanosoma cruzi, Trypanosma brucei and Leishmania spp. are kinetoplastid protozoa causative agents of Chagas disease, sleeping sickness and leishmaniasis, respectively, neglected tropical diseases estimated to infect millions of people worldwide. Their genome sequencing has revealed approximately 50 % of genes encoding hypothetical proteins of unknown function, opening possibilities for novel target identification and drug discovery. Q4DY78 is a putative essential protein from T. cruzi conserved in the related kinetoplastids and divergent from mammalian host proteins. Here we report the 1H, 15N, and 13C chemical shift assignments and secondary structure analysis of the Q4DY78 protein as basis for NMR structure determination, functional analysis and drug screening.
      PubDate: 2016-06-29
      DOI: 10.1007/s12104-016-9693-8
  • 1 H, 13 C, and 15 N resonance assignments for the pro-inflammatory
           cytokine interleukin-36α
    • Authors: Nishit Goradia; Amelie Wißbrock; Christoph Wiedemann; Frank Bordusa; Ramadurai Ramachandran; Diana Imhof; Oliver Ohlenschläger
      Abstract: Abstract Interleukin-36α (IL-36α) is a recently characterised member of the interleukin-1 superfamily. It is involved in the pathogenesis of inflammatory arthritis in one third of psoriasis patients. By binding of IL-36α to its receptor IL-36R via the NF-κB pathway other cytokines involved in inflammatory and apoptotic cascade are activated. The efficacy of complex formation is controlled by N-terminal processing. To obtain a more detailed view on the structure function relationship we performed a heteronuclear multidimensional NMR investigation and here report the 1H, 13C, and 15N resonance assignments for the backbone and side chain nuclei of the pro-inflammatory cytokine interleukin-36α.
      PubDate: 2016-06-28
      DOI: 10.1007/s12104-016-9694-7
  • 1 H N , 13 C, and 15 N resonance assignments of the CDTb-interacting
           domain (CDTaBID) from the Clostridium difficile binary toxin catalytic
           component (CDTa, residues 1–221)
    • Authors: Braden M. Roth; Kristen M. Varney; Richard R. Rustandi; David J. Weber
      Abstract: Abstract Once considered a relatively harmless bacterium, Clostridium difficile has become a major concern for healthcare facilities, now the most commonly reported hospital-acquired pathogen. C. difficile infection (CDI) is usually contracted when the normal gut microbiome is compromised by antibiotic therapy, allowing the opportunistic pathogen to grow and produce its toxins. The severity of infection ranges from watery diarrhea and abdominal cramping to pseudomembranous colitis, sepsis, or death. The past decade has seen a marked increase in the frequency and severity of CDI among industrialized nations owing directly to the emergence of a highly virulent C. difficile strain, NAP1. Along with the large Clostridial toxins expressed by non-epidemic strains, C. difficile NAP1 produces a binary toxin, C. difficile transferase (CDT). As the name suggests, CDT is a two-component toxin comprised of an ADP-ribosyltransferase (ART) component (CDTa) and a cell-binding/translocation component (CDTb) that function to destabilize the host cytoskeleton by covalent modification of actin monomers. Central to the mechanism of binary toxin-induced pathogenicity is the formation of CDTa/CDTb complexes at the cell surface. From the perspective of CDTa, this interaction is mediated by the N-terminal domain (residues 1–215) and is spatially and functionally independent of ART activity, which is located in the C-terminal domain (residues 216–420). Here we report the 1HN, 13C, and 15N backbone resonance assignments of a 221 amino acid, ~26 kDa N-terminal CDTb-interacting domain (CDTaBID) construct by heteronuclear NMR spectroscopy. These NMR assignments represent the first component coordination domain for a family of Clostridium or Bacillus species harboring ART activity. Our assignments lay the foundation for detailed solution state characterization of structure–function relationships, toxin complex formation, and NMR-based drug discovery efforts.
      PubDate: 2016-06-28
      DOI: 10.1007/s12104-016-9695-6
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