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  Subjects -> CHEMISTRY (Total: 871 journals)
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CHEMISTRY (610 journals)                  1 2 3 4 | Last

Showing 1 - 200 of 735 Journals sorted alphabetically
2D Materials     Hybrid Journal   (Followers: 13)
Accreditation and Quality Assurance: Journal for Quality, Comparability and Reliability in Chemical Measurement     Hybrid Journal   (Followers: 26)
ACS Catalysis     Full-text available via subscription   (Followers: 42)
ACS Chemical Neuroscience     Full-text available via subscription   (Followers: 20)
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Acta Chemica Iasi     Open Access   (Followers: 2)
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Acta Facultatis Medicae Naissensis     Open Access  
Acta Metallurgica Sinica (English Letters)     Hybrid Journal   (Followers: 6)
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adhäsion KLEBEN & DICHTEN     Hybrid Journal   (Followers: 5)
Adhesion Adhesives & Sealants     Hybrid Journal   (Followers: 8)
Adsorption Science & Technology     Full-text available via subscription   (Followers: 5)
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African Journal of Bacteriology Research     Open Access  
African Journal of Chemical Education     Open Access   (Followers: 3)
African Journal of Pure and Applied Chemistry     Open Access   (Followers: 7)
Agrokémia és Talajtan     Full-text available via subscription   (Followers: 2)
Al-Kimia : Jurnal Penelitian Sains Kimia     Open Access  
Alkaloids: Chemical and Biological Perspectives     Full-text available via subscription   (Followers: 2)
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American Journal of Biochemistry and Biotechnology     Open Access   (Followers: 61)
American Journal of Biochemistry and Molecular Biology     Open Access   (Followers: 15)
American Journal of Chemistry     Open Access   (Followers: 29)
American Journal of Plant Physiology     Open Access   (Followers: 11)
American Mineralogist     Hybrid Journal   (Followers: 15)
Analyst     Full-text available via subscription   (Followers: 38)
Angewandte Chemie     Hybrid Journal   (Followers: 164)
Angewandte Chemie International Edition     Hybrid Journal   (Followers: 235)
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Annual Review of Chemical and Biomolecular Engineering     Full-text available via subscription   (Followers: 12)
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Anti-Infective Agents     Hybrid Journal   (Followers: 3)
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Applied Organometallic Chemistry     Hybrid Journal   (Followers: 8)
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Arabian Journal of Chemistry     Open Access   (Followers: 5)
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Atomization and Sprays     Full-text available via subscription   (Followers: 4)
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Autophagy     Hybrid Journal   (Followers: 2)
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Biomass Conversion and Biorefinery     Partially Free   (Followers: 10)
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Biomolecular NMR Assignments     Hybrid Journal   (Followers: 3)
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Bioorganic & Medicinal Chemistry Letters     Hybrid Journal   (Followers: 84)
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Bitácora Digital     Open Access  
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Bulletin of the Chemical Society of Ethiopia     Open Access   (Followers: 2)
Bulletin of the Chemical Society of Japan     Full-text available via subscription   (Followers: 24)
Bulletin of the Korean Chemical Society     Hybrid Journal   (Followers: 1)
C - Journal of Carbon Research     Open Access   (Followers: 3)
Cakra Kimia (Indonesian E-Journal of Applied Chemistry)     Open Access  
Canadian Association of Radiologists Journal     Full-text available via subscription   (Followers: 2)
Canadian Journal of Chemistry     Hybrid Journal   (Followers: 10)
Canadian Mineralogist     Full-text available via subscription   (Followers: 6)
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Catalysis for Sustainable Energy     Open Access   (Followers: 7)
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ChemBioEng Reviews     Full-text available via subscription   (Followers: 1)
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Chemical Research in Chinese Universities     Hybrid Journal   (Followers: 3)
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Chemistry & Industry     Hybrid Journal   (Followers: 6)
Chemistry - A European Journal     Hybrid Journal   (Followers: 151)
Chemistry - An Asian Journal     Hybrid Journal   (Followers: 16)
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Chemistry Central Journal     Open Access   (Followers: 4)
Chemistry Education Research and Practice     Free   (Followers: 5)
Chemistry in Education     Open Access   (Followers: 9)
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Chemistry Letters     Full-text available via subscription   (Followers: 44)
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Chemistry of Natural Compounds     Hybrid Journal   (Followers: 9)
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Chemoecology     Hybrid Journal   (Followers: 4)
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ChemTexts     Hybrid Journal  
CHIMIA International Journal for Chemistry     Full-text available via subscription   (Followers: 2)
Chinese Journal of Chemistry     Hybrid Journal   (Followers: 6)
Chinese Journal of Polymer Science     Hybrid Journal   (Followers: 11)
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Clay Minerals     Full-text available via subscription   (Followers: 10)
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Colloids and Surfaces B: Biointerfaces     Hybrid Journal   (Followers: 6)
Combinatorial Chemistry & High Throughput Screening     Hybrid Journal   (Followers: 5)
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Detection     Open Access   (Followers: 2)
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Doklady Chemistry     Hybrid Journal  

        1 2 3 4 | Last

Journal Cover Biomolecular NMR Assignments
  [SJR: 0.325]   [H-I: 10]   [3 followers]  Follow
    
   Hybrid Journal Hybrid journal (It can contain Open Access articles)
   ISSN (Print) 1874-2718 - ISSN (Online) 1874-270X
   Published by Springer-Verlag Homepage  [2352 journals]
  • Resonance assignments of an α-synuclein fibril prepared in Tris buffer at
           moderate ionic strength
    • Authors: Alexander M. Barclay; Dhruva D. Dhavale; Joseph M. Courtney; Paul T. Kotzbauer; Chad M. Rienstra
      Abstract: Fibrils of the protein α-synuclein (α-syn) are implicated in the pathogenesis of Parkinson’s disease and related neurodegenerative disorders. We have reported a high-resolution structure (PDB 2N0A) of an α-syn fibril form prepared by in vitro incubation of monomeric protein in 50 mM sodium phosphate buffer pH 7.4 with 0.1 mM EDTA and 0.01% sodium azide. In parallel with this structure determination, ongoing studies of small molecule ligands binding to α-syn fibrils, prepared in 2-amino-2-(hydroxymethyl)-1,3-propanediol (Tris) buffer, have been in progress, and it is therefore of interest to determine the structural similarity of these forms. Here we report the 13C and 15N resonance assignments for α-syn fibrils prepared with Tris–HCl buffer (pH 7.7 at 37 °C) and 100 mM NaCl. These fibrillization conditions yield a form with fibril core chemical shifts highly similar to those we reported (BMRB 16939) in the course of determining the high-resolution 2N0A structure, with the exception of some small perturbations from T44 to V55, including two sets of peaks observed for residues T44–V48. Additional differences occur in the patterns of observed residues in the primarily unstructured N-terminus. These results demonstrate a common fold of the fibril core for α-syn fibrils prepared in phosphate or Tris–HCl buffer at moderate ionic strength.
      PubDate: 2018-02-23
      DOI: 10.1007/s12104-018-9808-5
       
  • 1 H, 13 C, and 15 N resonance assignments of CW domain of the N
           -methyltransferase ASHH2 free and bound to the mono-, di- and
           tri-methylated histone H3 tail peptides
    • Authors: Olena Dobrovolska; Maxim Bril’kov; Øyvind Ødegård-Fougner; Rein Aasland; Øyvind Halskau
      Abstract: The ASHH2 CW domain is responsible for recognizing the methylation state at lysine 4 of histone 3 N-terminal tails and implicated in the recruitment of the ASHH2 methyltransferase enzyme correctly to the histones. The ASHH2 CW domain binds H3 lysine motifs that can be either mono-, di-, or tri-methylated [ARTK(meX)QTAR, where X denotes the number of methylations], but binds strongest to monomethylated instances (Kd values reported in the range of 1 µm to 500 nM). Hoppmann et al. published the uncomplexed NMR structure of an ASHH2 CW domain in 2011. Here we document the assignment of a shortened ASHH2 CW construct, CW42, with similar binding affinity and better expression yields than the one used to solve the uncomplexed structure. We also perform 1H–15N HSQC-monitored titrations that document at which protein–peptide ratios the complex is saturated. Backbone resonance assignments are presented for this shortened ASHH2 CW domain alone and bound to an H3 histone tail mimicking peptide monomethylated on lysine 4 (ARTK(me1)QTAR). Likewise, the assignment was also performed for the protein in complex with the dimethylated (ARTK(me2)QTAR) and trimethylated (ARTK(me3)QTAR) peptide. Overall, these two latter situations displayed a similar perturbation of shifts as the mono-methylated instance. In the case of the monomethylated histone tail mimic, side-chain assignment of CW42 in this complex was performed and reported in addition to backbone assignment, in preparation of a future solution structure determination and dynamics characterization of the CW42–ARTK(me1)QTAR complex.
      PubDate: 2018-02-16
      DOI: 10.1007/s12104-018-9811-x
       
  • Backbone 1 H, 13 C, and 15 N assignments of the extracellular region of
           human Fcγ receptor IIIb
    • Authors: Rina Yogo; Saeko Yanaka; Koichi Kato
      Abstract: Fcγ receptor (FcγR) promotes various immune responses through interactions with the Fc portion of immunoglobulin G (IgG). FcγRIIIb is a glycosylphosphatidylinositol-linked protein expressed on neutrophils and triggers degranulation and opsonic phagocytosis. The extracellular region of FcγR is composed of two Ig-fold domains and can be cleaved as a soluble form (sFcγRIIIb), which is also reactive with complement receptor type 3. Although structure and Fc interaction of sFcγRIIIb have been characterized by X-ray crystallography, little has been known about its structure in solution. We herein report the backbone NMR assignments of human sFcγRIIIb to gain basic understanding of functional IgG–FcγRIII interactions of immunological and biopharmaceutical interest regarding the structural investigation.
      PubDate: 2018-02-16
      DOI: 10.1007/s12104-018-9809-4
       
  • Solid-state [ 13 C– 15 N] NMR resonance assignment of hepatitis B
           virus core protein
    • Authors: Lauriane Lecoq; Shishan Wang; Thomas Wiegand; Stéphane Bressanelli; Michael Nassal; Beat H. Meier; Anja Böckmann
      Abstract: Each year, nearly 900,000 deaths are due to serious liver diseases caused by chronic hepatitis B virus infection. The viral particle is composed of an outer envelope and an inner icosahedral nucleocapsid formed by multiple dimers of a ~ 20 kDa self-assembling core protein (Cp). Here we report the solid-state 13C and 15N resonance assignments of the assembly domain, Cp149, of the core protein in its capsid form. A secondary chemical shift analysis of the 140 visible residues suggests an overall alpha-helical three-dimensional fold matching that derived for Cp149 from the X-ray crystallography of the capsid, and from solution-state NMR of the Cp149 dimer. Interestingly, however, at three distinct regions the chemical shifts in solution differ significantly between core proteins in the capsid state versus in the dimer state, strongly suggesting the respective residues to be involved in capsid assembly.
      PubDate: 2018-02-16
      DOI: 10.1007/s12104-018-9810-y
       
  • NMR resonance assignments of RNase P protein from Thermotoga maritima
    • Authors: Danyun Zeng; Benjamin P. Brown; Markus W. Voehler; Sheng Cai; Nicholas J. Reiter
      Abstract: Ribonuclase P (RNase P) is an essential metallo-endonuclease that catalyzes 5′ precursor-tRNA (ptRNA) processing and exists as an RNA-based enzyme in bacteria, archaea, and eukaryotes. In bacteria, a large catalytic RNA and a small protein component assemble to recognize and accurately cleave ptRNA and tRNA-like molecular scaffolds. Substrate recognition of ptRNA by bacterial RNase P requires RNA–RNA shape complementarity, intermolecular base pairing, and a dynamic protein–ptRNA binding interface. To gain insight into the binding specificity and dynamics of the bacterial protein–ptRNA interface, we report the backbone and side chain 1H, 13C, and 15N resonance assignments of the hyperthermophilic Thermatoga maritima RNase P protein in solution at 318 K. Our data confirm the formation of a stable RNA recognition motif (RRM) with intrinsic heterogeneity at both the N- and C-terminus of the protein, consistent with available structural information. Comprehensive resonance assignments of the bacterial RNase P protein serve as an important first step in understanding how coupled RNA binding and protein–RNA conformational changes give rise to ribonucleoprotein function.
      PubDate: 2018-02-15
      DOI: 10.1007/s12104-018-9806-7
       
  • 1 H, 13 C and 15 N resonance assignment of domain 1 of trans-activation
           response element (TAR) RNA binding protein isoform 1 (TRBP2) and its
           comparison with that of isoform 2 (TRBP1)
    • Authors: Harshad Paithankar; Pankaj V. Jadhav; Amit S. Naglekar; Shilpy Sharma; Jeetender Chugh
      Abstract: TAR RNA binding protein (TRBP) is a double-stranded RNA binding protein involved in various biological processes like cell growth, development, death, etc. The protein exists as two isoforms TRBP2 and TRBP1. TRBP2 contains additional 21 amino acids at its N-terminus, which are proposed to be involved in its membrane localization, when compared to TRBP1. The resonance assignment (19–228) of the double-stranded RNA binding domains (dsRBD 1 and 2) of TRBP2 has been reported earlier. Here, we report 1H, 13C and 15N resonance assignment for dsRBD1 of TRBP2 (1–105) containing the additional N-terminal residues. This assignment will provide deeper insights to understand the effect of these residues on the structure and dynamics of TRBP2 and would therefore help in further elucidating the differences in the role of these isoforms.
      PubDate: 2018-02-14
      DOI: 10.1007/s12104-018-9807-6
       
  • 1 H, 13 C, 15 N resonance assignment of human YAP 50–171 fragment
    • Authors: Michael Feichtinger; Tomáš Sára; Gerald Platzer; Borja Mateos; Fedir Bokhovchuk; Patrick Chène; Robert Konrat
      Abstract: Yes associated protein (YAP) is an intrinsically disordered protein that plays a major role in the Hippo pathway, regulating organ size, cell proliferation, apoptosis, and is associated with cancer development. Therefore, the binding between YAP and TEAD is an interesting target for cancer therapy. The TEAD binding domain of YAP was mapped to protein residues 50–171. To obtain further structural insights into this 12 kDa segment of YAP, we report a backbone and a partial sidechain assignment of recombinant YAP 50–171.
      PubDate: 2018-01-25
      DOI: 10.1007/s12104-018-9805-8
       
  • 1 H, 15 N, and 13 C resonance assignments of the third domain from the S.
           aureus innate immune evasion protein Eap
    • Authors: Alvaro I. Herrera; Nicoleta T. Ploscariu; Brian V. Geisbrecht; Om Prakash
      Abstract: Staphylococcus aureus is a widespread and persistent pathogen of humans and livestock. The bacterium expresses a wide variety of virulence proteins, many of which serve to disrupt the host’s innate immune system from recognizing and clearing bacteria with optimal efficiency. The extracellular adherence protein (Eap) is a multidomain protein that participates in various protein–protein interactions that inhibit the innate immune response, including both the complement system (Woehl et al in J Immunol 193:6161–6171, 2014) and Neutrophil Serine Proteases (NSPs) (Stapels et al in Proc Natl Acad Sci USA 111:13187–13192, 2014). The third domain of Eap, Eap3, is an ~ 11 kDa protein that was recently shown to bind complement component C4b (Woehl et al in Protein Sci 26:1595–1608, 2017) and therefore play an essential role in inhibiting the classical and lectin pathways of complement (Woehl et al in J Immunol 193:6161–6171, 2014). Since structural characterization of Eap3 is still incomplete, we acquired a series of 2D and 3D NMR spectra of Eap3 in solution. Here we report the backbone and side-chain 1H, 15N, and 13C resonance assignments of Eap3 and its predicted secondary structure via the TALOS-N server. The assignment data have been deposited in the BMRB data bank under accession number 27087.
      PubDate: 2018-01-25
      DOI: 10.1007/s12104-018-9804-9
       
  • 1 H, 13 C and 15 N NMR assignments of cyclophilin LRT2 (OsCYP2) from rice
    • Authors: Lucila Andrea Acevedo; Linda K. Nicholson
      Abstract: Cyclophilins are enzymes that catalyze the isomerization of a prolyl–peptide bond and are found in both prokaryotes and eukaryotes. LRT2 (also known as OsCYP2) is a cyclophilin in rice (Oryza sativa), that has importance in lateral root development and stress tolerance. LRT2 is 172 amino acids long and has a molecular weight of 18.3 kDa. Here, we report the backbone and sidechain resonance assignments of 1H, 13C, 15N in the LRT2 protein using several 2D and 3D heteronuclear NMR experiments at pH 6.7 and 298 K. Our chemical shift data analysis predicts a secondary structure like the cytosolic wheat cyclophilin TaCypA-1 with 87.7% sequence identity. These assignments will be useful for further analysis in the NMR studies for function and structure of this enzyme.
      PubDate: 2018-01-20
      DOI: 10.1007/s12104-018-9803-x
       
  • 1 H, 15 N, and 13 C chemical shift assignments of the micelle immersed FAT
           C-terminal (FATC) domains of the human protein kinases
           ataxia-telangiectasia mutated (ATM) and DNA-dependent protein kinase
           catalytic subunit (DNA-PKcs) fused to the B1 domain of streptococcal
           protein G (GB1)
    • Authors: Munirah S. Abd Rahim; Lisa A. M. Sommer; Anja Wacker; Martin Schaad; Sonja A. Dames
      Abstract: FAT C-terminal (FATC) is a circa 33 residue-long domain. It controls the kinase functionality in phosphatidylinositol-3 kinase-related kinases (PIKKs). Recent NMR- and CD-monitored interaction studies indicated that the FATC domains of all PIKKs can interact with membrane mimetics albeit with different preferences for membrane properties such as surface charge and curvature. Thus they may generally act as membrane anchoring unit. Here, we present the 1H, 15N, and 13C chemical shift assignments of the DPC micelle immersed FATC domains of the human PIKKs ataxia-telangiectasia mutated (ATM, residues 3024–3056) and DNA protein kinase catalytic subunit (DNA-PKcs, residues 4096–4128), both fused to the 56 residue long B1 domain of Streptococcal protein G (GB1). Each fusion protein is 100 amino acids long and contains in the linking region between the GB1 tag and the FATC region a thrombin (LVPRGS) and an enterokinase (DDDDK) protease site. The assignments pave the route for the detailed structural characterization of the membrane mimetic bound states, which will help to better understand the role of the proper cellular localization at membranes for the function and regulation of PIKKs. The chemical shift assignment of the GB1 tag is useful for NMR spectroscopists developing new experiments or using GB1 otherwise for case studies in the field of in-cell NMR spectroscopy or protein folding. Moreover it is often used as purification tag. Earlier we showed already that GB1 does not interact with membrane mimetics and thus does not disturb the NMR monitoring of membrane mimetic interactions of attached proteins.
      PubDate: 2018-01-18
      DOI: 10.1007/s12104-018-9798-3
       
  • Backbone chemical shift assignments of the glycine cleavage complex H
           protein of Escherichia coli
    • Authors: Usha Yadav; Monica Sundd
      Abstract: Glycine cleavage complex H protein (GcvH) is one of the four components that form the glycine cleavage complex (GCS), essential for the synthesis of C1 (one-carbon units) for cell metabolism, by the oxidative cleavage of glycine. The activity of this complex is induced in the presence of exogenous glycine, and is repressed by purines. GCS, in cooperation with GCA (serine hydroxymethyltransferase) regulates the endogenous levels of glycine and C1 units in the cell. GcvH, the lipoamide containing component of the complex, plays an indispensable role in this reaction, as its prosthetic group shuttles between the active site of the three other components of the GCS complex sequentially. In environments rich in exogenous lipoic acid, GcvH is converted to lipoyl-GcvH by Lipoate protein ligase (LplA), by the salvage pathway. When exogenous lipoic acid is deficient, it is post-translationally modified to lipoyl-GcvH by the consecutive action of two enzymes, (a) Lipoate protein ligase B (LipB) and (b) Lipoyl synthase (LipA). Although, the crystal structure has been determined for Escherichia coli GcvH, no information exists for its interaction with LipB or LipA. Therefore, we plan to study its interactions with the aforementioned enzymes. As a first step, we have carried out the complete backbone chemical shift assignments of the E. coli glycine cleavage complex H protein in its apo-form, as well as its C8- intermediate.
      PubDate: 2018-01-15
      DOI: 10.1007/s12104-018-9801-z
       
  • 1 H, 13 C and 15 N backbone and partial side-chain resonance assignments
           of the C-terminal domain of HIV-1 Pr55 Gag encompassed in NCp15
    • Authors: Valéry Larue; Marjorie Catala; Anissa Belfetmi; Loussiné Zargarian; Olivier Mauffret; Carine Tisné
      Abstract: During HIV-1 assembly, the Pr55Gag polyprotein precursor (Gag) interacts with the genomic RNA, with lipids of the plasma membrane, with host proteins (ALIX, TSG101) through the ESCRT complex, with the viral protein Vpr and are involved in intermolecular interactions with other Pr55Gag proteins. This network of interactions is responsible for the formation of the viral particle, the selection of genomic RNA and the packaging of Vpr. The C-terminal domain of Gag encompassed in NCp15 is involved in the majority of these interactions, either by its nucleocapsid or its p6 domains. We study the NCp15 protein as a model of the C-terminal domain of Gag to better understand the role of this domain in the assembly and budding of HIV-1. Here, we report the 1H, 13C and 15N chemical shift assignments of NCp15 obtained by heteronuclear multidimensional NMR spectroscopy as well as the analysis of its secondary structure in solution. These assignments of NCp15 pave the way for interaction studies with its numerous partners.
      PubDate: 2018-01-13
      DOI: 10.1007/s12104-017-9796-x
       
  • Chemical shift assignments of retinal degeneration 3 protein (RD3)
    • Authors: Sunghyuk Lim; Diana Cudia; Qinhong Yu; Igor Peshenko; Alexander M. Dizhoor; James B. Ames
      Abstract: Retinal degeneration 3 protein (RD3) binds to retinal membrane guanylyl cyclase (RetGC) and suppresses the basal activity of RetGC in photoreceptor cells that opposes the allosteric activation of the cyclase by GCAP proteins. Mutations in RD3 that disrupt its inhibition of RetGC are implicated in human retinal degenerative disorders. Here we report both backbone and sidechain NMR assignments for the RD3 protein (BMRB accession no. 27305).
      PubDate: 2018-01-11
      DOI: 10.1007/s12104-018-9802-y
       
  • 1 H, 13 C and 15 N resonance assignments of NEDD8 from Trypanosoma brucei
    • Authors: Rui Wang; Jiahai Zhang; Shanhui Liao; Xiaoming Tu
      Abstract: Neural precursor cell-expressed, developmently downregulated 8 (NEDD8) is a small ubiquitin-like modifier, which plays important roles in many cellular processes. Although it has been well studied in many eukaryotes, NEDD8 is still uncharacterized in some unicellular parasites, such as Trypanosoma brucei (T. brucei). Here we report the resonance assignments of NEDD8 from T. brucei.
      PubDate: 2018-01-11
      DOI: 10.1007/s12104-018-9800-0
       
  • Chemical shift assignments of CHU_1110: an AHSA1-like protein from
           Cytophaga hutchinsonii
    • Authors: Chunjie Liang; Ting He; Tao Li; Yunhuang Yang; Jiang Zhu; Maili Liu
      Abstract: AHSA1 protein family is one of the four largest families in the Bet v1-like protein superfamily. The functions and structures of proteins in AHSA1 family are still largely unknown. CHU_1110 with 167 amino acids and a molecular weight of 19.2 kDa is a member of the AHSA1 family from Cytophaga hutchinsonii, a soil bacterium known for its ability to digest crystalline cellulose. Here we report the complete 1H, 13C and 15N chemical shift assignments of CHU_1110. The secondary structural elements of CGL2373 are consistent with the canonical AHSA1 structure. However the sequence identity of CHU_1110 with other members of AHSA1 family with functional and structural reports, such as RHE_CH02687 from Rhizobium etli, Aha1 from Homo sapiens and Yndb from Bacillus subtilis, are very low, which may suggest a different function of CHU_1110. Our chemical shift assignments of CHU_1110 are essential for the following structural and functional research of CHU_1110.
      PubDate: 2018-01-09
      DOI: 10.1007/s12104-018-9799-2
       
  • Backbone and side-chain chemical shift assignments of the kringle domain
           of human receptor tyrosine kinase-like orphan receptor 1 (ROR1)
    • Authors: Xiaofang Ma; Yingying Zhang; Bin Liu; Jiahui Yang; Kaifeng Hu
      Abstract: Receptor tyrosine kinase-like orphan receptor 1 (ROR1) expresses at high level in many cancers and has been suggested as a potential therapeutic target. It was reported that the Kringle (KNG) domain of ROR1 extracellular region is involved in ROR1/ROR2 heterooligomerization. Monoantibodies that target KNG domain of ROR1 could induce apoptosis of chronic lymphocytic leukemia cells. Here we present the backbone and side chain assignments of KNG domain of ROR1, which lays a foundation for its further structural and function research.
      PubDate: 2018-01-08
      DOI: 10.1007/s12104-017-9797-9
       
  • Backbone resonance assignment of the response regulator protein PhoB N
           F20D from Escherichia coli
    • Authors: Xinhui Kou; Xinghong Liu; Yixiang Liu; Conggang Li; Maili Liu; Ling Jiang
      Abstract: PhoB is a response regulator of the PhoR/PhoB two-component signal transduction system that is involved in the regulation of the phosphate (Pho) regulon of Escherichia coli. PhoB has two domains, receiver domain and effector domain. The receiver domain can be phosphorylated by its cognate histidine kinase PhoR and the phosphorylation induces conformational changes of the full length protein of PhoB that promote the DNA binding and transcription. Three-dimensional crystal structures of PhoB receiver domain (PhoBN) have been solved under apo or BeF3− (a phosphoryl analog) binding forms and it has been found that PhoBN is dimerized in both situations. However, we have found that the apo form of PhoBN has multiple conformational changes in solution that is hard to be distinguished by using NMR spectroscopy, while the mutagenesis of F20D PhoBN gives homogeneous dispersed signals in HSQC spectrum indicating a relatively uniform conformation. Meanwhile the F20D mutant has the same phosphorylation activity as the wild type protein. Here we report the backbone assignment of PhoBNF20D mutant. The chemical shift (HN, N, CO, Cα and Cβ) analysis shows that the predicted regions of secondary structure are in good agreement with those observed in the crystal structure of apo PhoBN. Therefore, the backbone chemical shifts assignment of PhoBNF20D mutant would be useful for studying the structure and dynamics of PhoB receiver domain and it has significance for explaining the mechanism of phosphorylation in TCSs.
      PubDate: 2018-01-03
      DOI: 10.1007/s12104-017-9795-y
       
  • Assignment of 1 H, 13 C and 15 N resonances and secondary structure of the
           Rgd1-RhoGAP domain
    • Authors: Denis Martinez; Valérie Prouzet-Mauléon; Michel Hugues; François Doignon; Benoît Odaert
      Abstract: The protein Rgd1 is involved in the regulation of cytoskeleton formation and in signalling pathways that control cell polarity and growth in Saccharomyces cerevisiae. Rgd1p is composed of a F-BAR domain required for membrane binding and a RhoGAP domain responsible for activating Rho3p and Rho4p, two GTPases respectively involved in bud growth and cytokinesis. Rgd1p is recruited to the membrane through interactions with phosphoinositide lipids, which bind the two isolated domains and stimulate the RhoGAP activity on Rho4p. As previously shown by crystallography, the membrane-binding F-BAR domain contains a conserved inositol phosphate binding site, which explains the preferential binding of phosphoinositides. In contrast, RhoGAP domains are not expected to bind lipids. In order to unravel this puzzling feature, we solved the three-dimensional structure of the isolated protein and found a cryptic phosphoinositide binding site involving non conserved residues (Martinez et al. 2017). The assignment of the resonances and secondary structure of Rgd1-RhoGAP (aa 450–666) is presented here.
      PubDate: 2017-12-26
      DOI: 10.1007/s12104-017-9794-z
       
  • Chemical shift assignments of the partially deuterated Fyn SH2–SH3
           domain
    • Authors: Fabien Kieken; Karine Loth; Nico van Nuland; Peter Tompa; Tom Lenaerts
      Abstract: Src Homology 2 and 3 (SH2 and SH3) are two key protein interaction modules involved in regulating the activity of many proteins such as tyrosine kinases and phosphatases by respective recognition of phosphotyrosine and proline-rich regions. In the Src family kinases, the inactive state of the protein is the direct result of the interaction of the SH2 and the SH3 domain with intra-molecular regions, leading to a closed structure incompetent with substrate modification. Here, we report the 1H, 15N and 13C backbone- and side-chain chemical shift assignments of the partially deuterated Fyn SH3–SH2 domain and structural differences between tandem and single domains. The BMRB accession number is 27165.
      PubDate: 2017-12-09
      DOI: 10.1007/s12104-017-9792-1
       
  • 1 H, 13 C, and 15 N chemical shift assignments of a G-quadruplex forming
           sequence within the KRAS proto-oncogene promoter region
    • Authors: Julien Marquevielle; M. V. Vasantha Kumar; Jean-Louis Mergny; Gilmar F. Salgado
      Abstract: Single stranded guanine rich DNA (or RNA) sequences adopt noncanonical secondary structures called G-quadruplexes (G4). Functionally, quadruplexes control gene transcription and regulate activities such as replication, gene recombination or alternative splicing. Hence they are potential targets for cancer, neuronal, and viral related diseases. KRAS is one of the most mutated oncogenes in the genome of cancer cells and contains a nuclease hypersensitive element (NHE) sequence capable of forming G-quadruplexes via its six runs of guanines. In our work, we are interested in the NMR structure of the major G4 scaffold formed in the KRAS NHE region with a mutated sequence of 22 residues. Here, we report 1H, 13C and 15N chemical shift assignments the G4 formed within KRAS22RT sequence.
      PubDate: 2017-11-30
      DOI: 10.1007/s12104-017-9793-0
       
 
 
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