881 results match your criteria Biomolecular Nmr Assignments[Journal]


Correction to: Complete NMR chemical shift assignments of odorant binding protein 22 from the yellow fever mosquito, Aedes aegypti, bound to arachidonic acid.

Biomol NMR Assign 2019 Apr 2. Epub 2019 Apr 2.

Department of Pharmacology, University of Colorado School of Medicine, 12801 East 17th Ave, Aurora, CO, 80045, USA.

The article listed above was initially published with incorrect copyright information. Upon publication of this Correction, the copyright of the article is changed to "The Author(s)". The original article has been corrected. Read More

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http://dx.doi.org/10.1007/s12104-019-09891-0DOI Listing
April 2019
2 Reads

Backbone and side-chain resonance assignments of centromeric protein Scm3 from Saccharomyces cerevisiae.

Biomol NMR Assign 2019 Apr 1. Epub 2019 Apr 1.

Department of Biosciences and Bioengineering, Indian Institute of Technology Bombay, Mumbai, 400076, India.

The centromeric chromatin plays an essential role in regulating the attachment of microtubules and controlling the segregation of sister chromatids during mitosis. In budding yeast, the evolutionary conserved histone variant, Cse4 is a vital component of the multiprotein kinetochore complex and is recruited to the centromere through its chaperone, Suppressor of chromosome mis-segregation (Scm3). Scm3 is an inner kinetochore protein crucial for the formation of a functional inner kinetochore. Read More

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http://dx.doi.org/10.1007/s12104-019-09889-8DOI Listing

H, C and N resonance assignments for the tandem CUE domains from chromatin remodeler SMARCAD1.

Biomol NMR Assign 2019 Mar 27. Epub 2019 Mar 27.

Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.

SMARCAD1 is a non-canonical chromatin remodelling ATPase, unique in its domain organization in that is encodes tandem ubiquitin binding CUE domains along with a classical SNF2 helicase ATP-dependent motor. SMARCAD1 is conserved from yeast to humans and has reported roles in the maintenance of heterochromatin following replication and in double-strand break repair. Here we present the H, C and N assignments for the tandem CUE domains and for the disordered regions that flank them. Read More

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http://dx.doi.org/10.1007/s12104-019-09888-9DOI Listing

Backbone and side chain H, N and C assignments of a putative peptidyl prolyl cis-trans isomerase FKBP12 from Mycobacterium tuberculosis.

Biomol NMR Assign 2019 04 16;13(1):239-243. Epub 2019 Mar 16.

Institute of Chemistry, Federal University of Rio de Janeiro, Av. Carlos Chagas Filho, 373 CCS/Anexo CNRMN, Rio de Janeiro, RJ, 21941-920, Brazil.

FK506 Binding Proteins (FKBPs) are a family of highly conserved and important proteins that possess a peptidyl cis-trans isomerase (PPIases) domain. Human FKBP12 is a prototype of this family and it is involved in many diseases due to its interaction with the immunosuppressive drugs FK506 and rapamycin. They inhibit calcineurin and mTOR complex, respectively, leading to parasite death by inhibiting cell proliferation through cytokinesis blockade being an important target to find new drugs. Read More

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http://dx.doi.org/10.1007/s12104-019-09884-zDOI Listing

HC, and N resonance assignments of human calmodulin bound to a peptide derived from the STRA6 vitamin A transporter (CaMBP2).

Biomol NMR Assign 2019 Mar 14. Epub 2019 Mar 14.

Department of Biochemistry and Molecular Biology, Center for Biomolecular Therapeutics (CBT), University of Maryland School of Medicine, 108 N. Greene St., Baltimore, MD, 21201, USA.

Vitamin A is a necessary nutrient for all mammals, and it is required for the transcription of many genes and vital for vision. While fasting, the vitamin A alcohol form (Retinol) from storage in the liver is mobilized and transported through the bloodstream while bound to retinol binding protein (RBP). Details of how exactly vitamin A is released from RBP and taken into the cells are still unclear. Read More

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http://link.springer.com/10.1007/s12104-019-09890-1
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http://dx.doi.org/10.1007/s12104-019-09890-1DOI Listing
March 2019
3 Reads

NMR assignments of human linker histone H1x N-terminal domain and globular domain in the presence and absence of perchlorate.

Biomol NMR Assign 2019 04 13;13(1):249-254. Epub 2019 Mar 13.

University of Johannesburg, PO Box 524, Auckland Park, Johannesburg, South Africa.

Human linker histone H1 plays a seminal role in eukaryotic DNA packaging. H1 has a tripartite structure consisting of a central, conserved globular domain, which adopts a winged-helix fold, flanked by two variable N- and C-terminal domains. Here we present the backbone resonance assignments of the N-terminal domain and globular domain of human linker histone H1x in the presence and absence of the secondary structure stabilizer sodium perchlorate. Read More

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http://dx.doi.org/10.1007/s12104-019-09886-xDOI Listing

Solution NMR assignment of the ARC4 domain of human tankyrase 2.

Biomol NMR Assign 2019 04 7;13(1):255-260. Epub 2019 Mar 7.

School of Cardiovascular Medicine and Sciences and Randall Centre, King's College London, Guy's Campus, London, SE1 1UL, UK.

Tankyrases are poly(ADP-ribose)polymerases (PARPs) which recognize their substrates via their ankyrin repeat cluster (ARC) domains. The human tankyrases (TNKS/TNKS2) contain five ARCs in their extensive N-terminal region; of these, four bind peptides present within tankyrase interactors and substrates. These short, linear segments, known as tankyrase-binding motifs (TBMs), contain some highly conserved features: an arginine at position 1, which occupies a predominantly acidic binding site, and a glycine at position 6 that is sandwiched between two aromatic side chains on the surface of the ARC domain. Read More

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http://dx.doi.org/10.1007/s12104-019-09887-wDOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6439159PMC
April 2019
1 Read

H, C and N NMR assignments of Bacillus subtilis bacteriophage SPO1 protein Gp46.

Biomol NMR Assign 2019 04 4;13(1):245-247. Epub 2019 Mar 4.

BioBank, The First Affiliated Hospital of Xi'an Jiaotong University, Shaanxi, 710061, China.

Bacterial antibiotic resistance is a serious threat to public health and bacteriophage therapy is an alternative for antibiotics in the era of multidrug resistance. While phage draws attention in fighting bacterial infection and is used in protein display to study macromolecular interactions, the molecular machinery of the host invasion mechanism remains largely unclear for many bacteriophages. Despite recent studies on T4 and T7 phages of Gram-negative model organism Escherichia coli revealing many interesting features of their invasive strategies, the studies on Gram-positive bacterial phages still lag far behind their counterparts. Read More

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http://dx.doi.org/10.1007/s12104-019-09885-yDOI Listing

Resonance assignments of sigma factor S binding protein Crl from Escherichia coli.

Biomol NMR Assign 2019 04 26;13(1):223-226. Epub 2019 Feb 26.

BioBank, The First Affiliated Hospital of Xi'an Jiaotong University, Shaanxi, 710061, China.

During bacterial transcription, sigma (σ) factors reversibly bind to RNA polymerase (RNAP) and recognize specific promoter sequences to initiate the process. While different sigma factors are utilized under different external conditions, Sigma S (RpoS, σ), a stress-responding sigma factor, is activated when bacteria face external threats. σ, which has a much lower affinity to RNAP compared with sigma D (RpoD, σ), is controlled by a very complex network of regulatory factors. Read More

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http://dx.doi.org/10.1007/s12104-019-09881-2DOI Listing

NMR H,C, N resonance assignment of the G12C mutant of human K-Ras bound to GppNHp.

Biomol NMR Assign 2019 04 23;13(1):227-231. Epub 2019 Feb 23.

Warp Drive Bio, Inc., A Subsidiary of Revolution Medicines, 700 Saginaw Drive, Redwood City, CA, 94063, USA.

K-Ras exists in two distinct structural conformations specific to binding of GDP and GTP nucleotides. The cycling between an inactive, GDP-bound state and an active, GTP-bound state is regulated by guanine nucleotide exchange factors and GTPase activating proteins, respectively. The activated form of K-Ras regulates cell proliferation, differentiation and survival by controlling several downstream signaling pathways. Read More

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http://dx.doi.org/10.1007/s12104-019-09882-1DOI Listing
April 2019
1 Read

Chemical shift assignments of a calmodulin intermediate with two Ca bound in complex with the IQ-motif of voltage-gated Ca channels (Ca1.2).

Biomol NMR Assign 2019 04 20;13(1):233-237. Epub 2019 Feb 20.

Department of Chemistry, University of California, 95616, Davis, CA, USA.

Calcium-dependent inactivation (CDI) of neuronal voltage-gated Ca channels (Ca1.2) is important for synaptic plasticity, which is associated with learning and memory. The Ca-dependent binding of calmodulin (CaM) to Ca1. Read More

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http://dx.doi.org/10.1007/s12104-019-09883-0DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6440834PMC

H, C, and N resonance assignments of the cytokine interleukin-36β isoform-2.

Biomol NMR Assign 2019 04 13;13(1):155-161. Epub 2019 Feb 13.

Leibniz Institute on Aging - Fritz Lipmann Institute, Beutenbergstr. 11, 07745, Jena, Germany.

Interleukins are cytokines performing central tasks in the human immune system. Interleukin-36β (IL-36β) is a member of the interleukin-1 superfamily as are its homologues IL-36α and IL-36γ. All of them interact with a common receptor composed of IL-36R and IL-1R/acP. Read More

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http://link.springer.com/10.1007/s12104-018-09869-4
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http://dx.doi.org/10.1007/s12104-018-09869-4DOI Listing
April 2019
5 Reads

Backbone H, C, and N resonance assignments of BoMan26A, a β-mannanase of the glycoside hydrolase family 26 from the human gut bacterium Bacteroides ovatus.

Biomol NMR Assign 2019 04 7;13(1):213-218. Epub 2019 Feb 7.

Department of Chemistry, Biophysical Chemistry, Center for Molecular Protein Science, Lund University, Lund, Sweden.

Bacteroides ovatus is a member of the human gut microbiota. The importance of this microbial consortium involves the degradation of complex dietary glycans mainly conferred by glycoside hydrolases. In this study we focus on one such catabolic glycoside hydrolase from B. Read More

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http://dx.doi.org/10.1007/s12104-019-09879-wDOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6439179PMC

Backbone resonance assignments of innate immune evasion protein EapH2 from the S. aureus.

Biomol NMR Assign 2019 04 7;13(1):219-222. Epub 2019 Feb 7.

Department of Biochemistry and Molecular Biophysics, Kansas State University, 141 Chalmers Hall, Manhattan, KS, 66506, USA.

Staphylococcus aureus is a ubiquitous and persistent pathogen of humans and livestock. The bacterium disrupts the host's innate immune system's ability to recognize and clear bacteria with optimal efficiency by expressing a wide variety of virulence proteins. Two single domain protein homologs (EapH1, EapH2) of the extracellular adherence protein (Eap) have been reported. Read More

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http://link.springer.com/10.1007/s12104-019-09880-3
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http://dx.doi.org/10.1007/s12104-019-09880-3DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6440808PMC
April 2019
9 Reads

N, C and H resonance assignments of FKBP12 proteins from the pathogenic fungi Mucor circinelloides and Aspergillus fumigatus.

Biomol NMR Assign 2019 04 1;13(1):207-212. Epub 2019 Feb 1.

Duke University NMR Center, Duke University, Durham, NC, USA.

Invasive fungal infections are a leading cause of death in immunocompromised patients and remain difficult to treat since fungal pathogens, like mammals, are eukaryotes and share many orthologous proteins. As a result, current antifungal drugs have limited clinical value, are sometimes toxic, can adversely affect human reaction pathways and are increasingly ineffective due to emerging resistance. One potential antifungal drug, FK506, establishes a ternary complex between the phosphatase, calcineurin, and the 12-kDa peptidyl-prolyl isomerase FK506-binding protein, FKBP12. Read More

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http://dx.doi.org/10.1007/s12104-019-09878-xDOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6439170PMC

Chemical shift assignments of retinal guanylyl cyclase activating protein 5 (GCAP5).

Biomol NMR Assign 2019 04 31;13(1):201-205. Epub 2019 Jan 31.

Department of Chemistry, University of California, Davis, CA, 95616, USA.

Retinal membrane guanylyl cyclase (RetGC) in photoreceptor rod and cone cells is regulated by a family of guanylyl cyclase activating proteins (GCAP1-7). GCAP5 is expressed in zebrafish photoreceptors and promotes Ca-dependent regulation of RetGC enzymatic activity that regulates visual phototransduction. We report NMR chemical shift assignments of the Ca-free activator form of GCAP5 (BMRB No. Read More

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http://dx.doi.org/10.1007/s12104-019-09877-yDOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6440817PMC

H, N and C backbone assignment of apo TDP-43 RNA recognition motifs.

Biomol NMR Assign 2019 04 29;13(1):163-167. Epub 2019 Jan 29.

Department of Pharmacology, College of Medicine, University of Arizona, 1501 North Campbell Drive, P.O. Box 245050, Tucson, AZ, 85724, USA.

TAR DNA-binding protein 43 (TDP-43) is a ubiquitously expressed nuclear protein that influences diverse cellular processes by regulating alternative splicing of RNA and microRNA biogenesis. It is also a pathological protein found in sporadic ALS and in the most common subtype of frontotemporal lobar degeneration with ubiquitinated inclusions (FLTD-U). TDP-43 has two tandem RNA-binding domains, RRM1 and RRM2. Read More

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http://dx.doi.org/10.1007/s12104-018-09870-xDOI Listing

H, C and N resonance assignments of the second peptidyl-prolyl isomerase domain of chaperone SurA from Escherichia coli.

Biomol NMR Assign 2019 04 25;13(1):183-186. Epub 2019 Jan 25.

College of Life Sciences, Peking University, Beijing, 100871, China.

The periplasmic chaperone SurA in Gram-negative bacteria plays a central role in the biogenesis of integral outer membrane proteins and is critical to the maintenance of bacterial membrane integrity. SurA contains a core chaperone module comprising the N- and C-terminal domains, along with two peptidyl-prolyl isomerase (PPIase) domains. The chaperone activity of SurA has been demonstrated to rely on the core module, whereas recent works suggested that the PPIase domains may regulate the chaperone activity through large conformational rearrangements. Read More

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http://dx.doi.org/10.1007/s12104-019-09874-1DOI Listing
April 2019
1 Read

Complete NMR chemical shift assignments of odorant binding protein 22 from the yellow fever mosquito, Aedes aegypti, bound to arachidonic acid.

Biomol NMR Assign 2019 04 25;13(1):187-193. Epub 2019 Jan 25.

Department of Pharmacology, University of Colorado School of Medicine, 12801 East 17th Ave, Aurora, CO, 80045, USA.

Aedes aegypti mosquitoes are the vector for transmission of Dengue, Zika and chikungunya viruses. These mosquitos feed exclusively on human hosts for a blood meal. Previous studies have established that Dengue virus infection of the mosquito results in increased expression of the odorant binding proteins 22 and 10 within the mosquito salivary gland and silencing of these genes dramatically reduces blood-feeding behaviors. Read More

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http://dx.doi.org/10.1007/s12104-019-09875-0DOI Listing
April 2019
14 Reads

NMR chemical shift assignment of the C-terminal region of the Menangle virus phosphoprotein.

Biomol NMR Assign 2019 04 24;13(1):195-199. Epub 2019 Jan 24.

School of Biological Sciences, The University of Auckland, Auckland, New Zealand.

Menangle virus is a bat-borne paramyxovirus with zoonotic potential. The single-stranded RNA genome of the virus is encapsidated in a helical nucleocapsid which is the template for both transcription and genome replication. Each of these operations is performed by the viral RNA polymerase. Read More

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http://dx.doi.org/10.1007/s12104-019-09876-zDOI Listing

Chemical shift assignments of the catalytic and ATP-binding domain of HK853 from Thermotoga maritime.

Biomol NMR Assign 2019 04 23;13(1):173-176. Epub 2019 Jan 23.

Key Laboratory of Magnetic Resonance in Biological Systems, National Center for Magnetic Resonance in Wuhan, State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Institute of Physics and Mathematics, The Chinese Academy of Sciences, Wuhan, 430071, China.

HK853 is a transmembrane protein from Thermotoga maritime, which belongs to HK853/RR468 two-component signal transduction system (TCS) and acts as a sensor histidine kinase. HK853 is mainly composed of a transmembrane domain, dimerization and histidine-containing phosphotransfer domain (HK853), catalytic and ATP-binding domain (HK853) and several linkers. HK853 can be completely autophosphorylated, which is the first step for signal transduction of TCS. Read More

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http://dx.doi.org/10.1007/s12104-019-09872-3DOI Listing
April 2019
1 Read

Resonance assignments for the tandem PWWP-ARID domains of human RBBP1.

Biomol NMR Assign 2019 04 21;13(1):177-181. Epub 2019 Jan 21.

Shandong Provincial Key Laboratory of Synthetic Biology, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, 266101, China.

Retinoblastoma-binding protein 1 (RBBP1), also known as AT-rich interaction domain 4A (ARID4A), is a tumour suppressor involved in the regulation of the epigenetic programming in leukemia and Prader-Willi/Angelman syndromes. The ARID domain of RBBP1 binds to DNA non-specifically and has gene suppression activity. However, no structural data has been obtained for the human RBBP1 ARID domain so far. Read More

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http://dx.doi.org/10.1007/s12104-019-09873-2DOI Listing

Resonance assignment of human LARP4A La module.

Biomol NMR Assign 2019 04 10;13(1):169-172. Epub 2019 Jan 10.

Randall Centre for Cell and Molecular Biophysics, King's College London, London, SE1 1UL, UK.

Human LARP4A belongs to a superfamily of RNA binding proteins called La-related proteins (LARPs). Whilst being a positive regulator of protein synthesis and a promoter of mRNA stability, LARP4A also controls cell morphology and motility in human breast and prostate cancer cells. All LARPs share a characteristic RNA binding unit named the La-module, which despite a high level of primary structure conservation exhibits a great versatility in RNA target selection. Read More

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http://link.springer.com/10.1007/s12104-019-09871-4
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http://dx.doi.org/10.1007/s12104-019-09871-4DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6439165PMC
April 2019
10 Reads

H, C, N resonance assignment of the C-terminal domain of the bifunctional enzyme TraI of plasmid R1.

Biomol NMR Assign 2019 04 7;13(1):121-125. Epub 2019 Jan 7.

Institute of Chemistry, University of Graz, 8010, Graz, Austria.

Transfer of genetic material is the main mechanism underlying the spread of antibiotic resistance and virulence factors within the bacterial community. Conjugation is one such process by which the genetic material is shared from one bacterium to another. The DNA substrate is processed and prepared for transfer by a multi-protein complex called the relaxosome . Read More

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http://dx.doi.org/10.1007/s12104-018-9863-yDOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6439144PMC

NMR resonance assignments and secondary structure of a mutant form of the human KCNE1 channel accessory protein that exhibits KCNE3-like function.

Biomol NMR Assign 2019 04 2;13(1):143-147. Epub 2019 Jan 2.

Department of Biochemistry and Center for Structural Biology, Vanderbilt University School of Medicine Basic Sciences, Nashville, TN, 37240-7917, USA.

KCNQ1 (Q1) is a voltage-gated potassium channel that is modulated by members of the KCNE family, the best-characterized being KCNE1 (E1) and KCNE3 (E3). The Q1/E1 complex generates a channel with delayed activation and increased conductance. This complex is expressed in cardiomyocytes where it provides the I current that is critical for the repolarization phase of the cardiac action potential. Read More

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http://dx.doi.org/10.1007/s12104-018-09867-6DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6440842PMC

NMR resonance assignments of the NZF domain of mouse HOIL-1L free and bound to linear di-ubiquitin.

Biomol NMR Assign 2019 04 19;13(1):149-153. Epub 2018 Dec 19.

Department of Molecular Engineering, Graduate School of Engineering, Kyoto University, Kyoto-Daigaku Katsura, Nishikyo-Ku, Kyoto, 615-8510, Japan.

Nuclear factor-κB (NF-κB) activation plays a central role in immunity and inflammation. In the canonical NF-κB activation pathway, linear polyubiquitin chains conjugated by the linear ubiquitin chain assembly complex (LUBAC) are specifically recognized by the Npl4 zinc finger (NZF) domain of heme-oxidized IRP2 ligase-1L (HOIL-1L). Recently, a crystal structure of the NZF domain in complex with linear di-ubiquitin has been reported; however, to understand the recognition mechanism in more detail, it is also necessary to investigate the structure and dynamics of the NZF domain in solution. Read More

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http://dx.doi.org/10.1007/s12104-018-09868-5DOI Listing

H, C, and N backbone resonance assignments for KPC-2, a class A serine-β-lactamase.

Biomol NMR Assign 2019 04 14;13(1):139-142. Epub 2018 Dec 14.

Department of Chemistry and Biochemistry, Miami University, 651 E. High St, Oxford, OH, 45056, USA.

The ever-increasing occurrence of antibiotic resistance presents a major threat to public health. Specifically, resistance conferred by β-lactamases places the efficacy of currently available antibiotics at risk. Klebsiella pneumoniae carbapenemase-2 (KPC-2) is a β-lactamase that enables carbapenem resistance and represents a clear and present danger to global public health. Read More

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http://dx.doi.org/10.1007/s12104-018-9866-8DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6440833PMC
April 2019
16 Reads

NMR resonance assignments of the pathogenesis-related peach allergen Pru p 1.0101.

Biomol NMR Assign 2019 04 12;13(1):127-130. Epub 2018 Dec 12.

Institute of Organic Chemistry and Center for Molecular Biosciences Innsbruck (CMBI), University of Innsbruck, Innrain 80/82, 6020, Innsbruck, Austria.

In Europe, Northern America, and China a large number of individuals are suffering from peach (Prunus persica) allergy caused by the protein Pru p 1. Immunologic reactions against this 17.5 kDa protein result from initial sensitization to the birch (Betula verrucosa) pollen allergen Bet v 1 and subsequent immunologic cross-reactivity of Bet v 1 specific antibodies. Read More

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http://dx.doi.org/10.1007/s12104-018-9864-xDOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6439177PMC

NMR backbone and methyl resonance assignments of an inhibitory G-alpha subunit in complex with GDP.

Biomol NMR Assign 2019 04 11;13(1):131-137. Epub 2018 Dec 11.

Bavarian NMR Center at the Department of Chemistry and Institute for Advanced Study, Technical University of Munich, Ernst-Otto-Fischer-Str. 2, 85748, Garching, Germany.

G-proteins are essential switch points at the cell membrane that control downstream signaling by their ability to adopt an inactive, GDP-bound or an active, GTP-bound state. Among other exchange factors, G-protein coupled receptors (GPCRs) induce exchange of GDP to GTP and thus promote the active state of the G-protein. The nucleotide-binding α subunit of the G-protein undergoes major conformational changes upon nucleotide binding. Read More

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http://dx.doi.org/10.1007/s12104-018-9865-9DOI Listing

Sequential backbone resonance assignment of AT-rich interaction domain of human BAF200.

Biomol NMR Assign 2019 04 10;13(1):115-119. Epub 2018 Dec 10.

Molecular Biophysics Unit, Indian Institute of Science, Bengaluru, India.

BAF200 is a subunit of PBAF chromatin remodeling complex that contains an N-terminal AT-rich interaction domain (ARID). ARID domain in general has been shown to bind to the AT-rich DNA sequences. The human BAF200 ARID (~ 110 residues) has the potential to bind the DNA sequences with high affinity, however, the structure and the exact contribution of hBAF200 ARID in PBAF functions as well its DNA binding specificities have not been established. Read More

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http://link.springer.com/10.1007/s12104-018-9862-z
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http://dx.doi.org/10.1007/s12104-018-9862-zDOI Listing
April 2019
12 Reads

H, N, C resonance assignment of the human CD44 cytoplasmic tail (669-742).

Biomol NMR Assign 2019 04 24;13(1):109-113. Epub 2018 Nov 24.

Max F. Perutz Laboratories, Department of Computational and Structural Biology, University of Vienna, Campus Vienna Biocenter 5, 1030, Vienna, Austria.

CD44 is a universally and abundantly expressed single-pass type I protein that spans the cytoplasmic membrane and is considered the principal receptor for hyaluronan in the extracellular matrix. CD44 exerts a multitude of biological functions, especially in cell adhesion and migration, and its deregulation has several pathological implications, including a putative role in cancer cell dissemination. Here we report the NMR chemical shift assignment of the recombinant intrinsically disordered CD44 cytoplasmic region (669-742). Read More

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http://dx.doi.org/10.1007/s12104-018-9861-0DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6439174PMC

Resonance assignments of a cellulosomal double-dockerin from Clostridium thermocellum.

Biomol NMR Assign 2019 04 30;13(1):97-101. Epub 2018 Oct 30.

Shandong Provincial Key Laboratory of Energy Genetics, Qingdao Institute of Bioenergy and Bioprocess Technology, Chinese Academy of Sciences, Qingdao, 266101, China.

Cellulosomes are highly efficient multienzyme complexes for lignocellulose degradation secreted by some lignocellulolytic bacteria. Cellulosomes are assembled through protein modules named cohesin and dockerin, and multiple cohesin modules in the scaffold protein generally determine the complexity of the cellulosomes. Some cellulosomal proteins contain multiple dockerin modules, which may generate more complex cellulosomal architectures. Read More

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http://link.springer.com/10.1007/s12104-018-9859-7
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http://dx.doi.org/10.1007/s12104-018-9859-7DOI Listing
April 2019
14 Reads

Backbone chemical shift assignments of human 14-3-3σ.

Biomol NMR Assign 2019 04 30;13(1):103-107. Epub 2018 Oct 30.

UMR 8576 CNRS-Lille University, 59000, Lille, France.

14-3-3 proteins are a group of seven dimeric adapter proteins that exert their biological function by interacting with hundreds of phosphorylated proteins, thus influencing their sub-cellular localization, activity or stability in the cell. Due to this remarkable interaction network, 14-3-3 proteins have been associated with several pathologies and the protein-protein interactions (PPIs) established with a number of partners are now considered promising drug targets. The activity of 14-3-3 proteins is often isoform specific and to our knowledge only one out of seven isoforms, 14-3-3[Formula: see text], has been assigned. Read More

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http://link.springer.com/10.1007/s12104-018-9860-1
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http://dx.doi.org/10.1007/s12104-018-9860-1DOI Listing
April 2019
1 Read

H, C and N resonance assignments and structure prediction of translation initiation factor 1 from Clostridium difficile.

Biomol NMR Assign 2019 04 28;13(1):91-95. Epub 2018 Oct 28.

Department of Chemistry, The University of Texas Rio Grande Valley, Edinburg, TX, USA.

Clostridium difficile is a gram-positive, toxin-producing, anaerobic bacterium whose virulence factors and mechanisms of pathogenesis require further investigation. C. difficile infections (CDI) result in the severe and potentially fatal gastrointestinal diseases pseudomembranous colitis and toxic megacolon following extensive broad spectrum antibiotic treatment. Read More

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http://link.springer.com/10.1007/s12104-018-9858-8
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http://dx.doi.org/10.1007/s12104-018-9858-8DOI Listing
April 2019
14 Reads

Backbone and side-chain chemical shift assignments of full-length, apo, human Pin1, a phosphoprotein regulator with interdomain allostery.

Biomol NMR Assign 2019 04 23;13(1):85-89. Epub 2018 Oct 23.

Department of Biochemistry and Molecular Genetics, University of Colorado Anschutz Medical Campus, 12801 East 17th Avenue, Aurora, CO, 80045, USA.

Pin1 is a human peptidyl-prolyl cis-trans isomerase important for the regulation of phosphoproteins that are implicated in many diseases including cancer and Alzheimer's. Further biophysical study of Pin1 will elucidate the importance of the two-domain system to regulate its own activity. Here, we report near-complete backbone and side-chain H, C and N NMR chemical shift assignments of full-length, apo Pin1 for the purpose of studying interdomain allostery and dynamics. Read More

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http://dx.doi.org/10.1007/s12104-018-9857-9DOI Listing

NMR resonance assignments of the TPR domain of human aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1).

Biomol NMR Assign 2019 04 19;13(1):79-83. Epub 2018 Oct 19.

Department of Molecular Physiology and Biophysics, University of Iowa Carver College of Medicine, 5-532 BSB, 51 Newton Road, Iowa City, IA, 52242, USA.

Aryl hydrocarbon receptor-interacting protein-like 1 (AIPL1) is a photoreceptor-specific chaperone of phosphodiesterase-6, a key effector enzyme in the phototransduction cascade. It contains an N-terminal FK506-binding protein (FKBP) domain and a C-terminal tetratricopeptide repeat (TPR) domain. Mutations in AIPL1, including many missense mutations in both FKBP and TPR domains, have been associated with Leber congenital amaurosis, a severe inherited retinopathy that causes blindness. Read More

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http://dx.doi.org/10.1007/s12104-018-9856-xDOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6440825PMC

Chemical shift assignments of a camelid nanobody against aflatoxin B.

Biomol NMR Assign 2019 04 16;13(1):75-78. Epub 2018 Oct 16.

State Key Laboratory of Magnetic Resonance and Atomic Molecular Physics, Wuhan Center for Magnetic Resonance, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan, 430071, China.

Nanobodies (Nbs) are the variable domain of the heavy-chain antibodies produced from Camelidae, which possess comparable binding affinities and specificity to conventional antibodies. Nbs have become valuable and versatile tools for numerous biotechnology applications due to their small size (12-15 kDa), high solubility, exceptional stability, and facile genetic manipulation. The interactions between Nbs and protein antigens have been well-studied, but less work has been done to characterize their ability to bind small molecule haptens. Read More

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http://dx.doi.org/10.1007/s12104-018-9855-yDOI Listing
April 2019
2 Reads

Backbone resonance assignment for the N-terminal region of bacterial tRNA-(NG37) methyltransferase.

Biomol NMR Assign 2019 04 8;13(1):49-53. Epub 2018 Oct 8.

Experimental Therapeutics Centre, 31 Biopolis Way, #03-01 Nanos, Singapore, 138669, Singapore.

Bacterial tRNA (guanine-N)-methyltransferase (TrmD) is an important antibacterial target due to its essential role in translation. TrmD has two domains connected with a flexible linker. The N-terminal domain (NTD) of TrmD contains the S-adenosyl-L-methionine (SAM) cofactor binding site and the C-terminal domain is critical for tRNA binding. Read More

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http://dx.doi.org/10.1007/s12104-018-9849-9DOI Listing
April 2019
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H, N, and C resonance assignments of the intrinsically disordered SH4 and Unique domains of Hck.

Biomol NMR Assign 2019 04 4;13(1):71-74. Epub 2018 Oct 4.

Department of Biochemistry and Molecular Biology, Gordon Center for Integrative Science, University of Chicago, 929 E 57th Street, Chicago, IL, 60637, USA.

Hematopoietic cell kinase (Hck) is an important signaling enzyme and a potential drug target for HIV infections and Bcr/Abl-chronic myeloid leukemia. The protein shares the same SH4-Unique-SH3-SH2-kinase multi-domain architecture as the other eight members of the Src family of non-receptor tyrosine kinases. These enzymes are often found anchored to the intracellular side of the membrane via lipidation of the SH4 domain and are integral components of signaling cascades localized at the cell surface. Read More

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http://link.springer.com/10.1007/s12104-018-9854-z
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http://dx.doi.org/10.1007/s12104-018-9854-zDOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6440858PMC
April 2019
11 Reads

H, C and N NMR assignments of self-incompatibility protein homologue 15 from Arabidopsis thaliana.

Biomol NMR Assign 2019 04 3;13(1):67-70. Epub 2018 Oct 3.

Department of Chemistry, University of Oxford, Oxford, OX1 3QR, UK.

The SPH proteins are a large family of small, disulphide-bonded, secreted proteins, originally found to be involved in the self-incompatibility response in the field poppy (Papaver rhoeas). They are now known to be widely distributed in plants, many containing multiple members of this protein family. Apart from the PrsS proteins in Papaver the function of these proteins is unknown but they are thought to be involved in plant development and cell signalling. Read More

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http://dx.doi.org/10.1007/s12104-018-9853-0DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6439154PMC

H, C, and N resonance assignments of N-acetylmuramyl-L-alanine amidase (AmiC) N-terminal domain (NTD) from Neisseria gonorrhoeae.

Biomol NMR Assign 2019 04 1;13(1):63-66. Epub 2018 Oct 1.

Department of Biochemistry and Molecular Biology, Medical University of South Carolina, Charleston, SC, 29425, USA.

Gonorrhea infections are becoming more difficult to treat due to the prevalence of strains exhibiting resistance to antibiotics and new therapeutic approaches are needed. N-acetylmuramyl-L-alanine amidase (AmiC) from Neisseria gonorrhoeae is a hydrolase that functions during cell division by cleaving the bond between the N-acetylmuramyl and L-alanine moieties of peptidoglycan. Inhibiting this enzyme offers the prospect of restoring the efficacy of existing antibiotics as treatments against N. Read More

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http://link.springer.com/10.1007/s12104-018-9852-1
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http://dx.doi.org/10.1007/s12104-018-9852-1DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6440844PMC
April 2019
6 Reads

H, C and N backbone and side-chain assignment of a carbohydrate binding module from a xylanase from Roseburia intestinalis.

Biomol NMR Assign 2019 04 22;13(1):55-58. Epub 2018 Sep 22.

NOBIPOL, Department of Biotechnology and Food Science, NTNU Norwegian University of Science and Technology, Trondheim, Norway.

The N-terminal domain (residues 28-165) from the glycoside hydrolase family 10 from Roseburia intestinalis (RiCBMx), has been isotopically labeled and recombinantly expressed in Escherichia coli. Here we report H, C and N NMR chemical shift assignments for this carbohydrate binding module (CBM). Read More

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http://link.springer.com/10.1007/s12104-018-9850-3
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http://dx.doi.org/10.1007/s12104-018-9850-3DOI Listing
April 2019
1 Read

Backbone and side-chain resonance assignments of the methyl-CpG-binding domain of MBD6 from Arabidopsis thaliana.

Biomol NMR Assign 2019 04 21;13(1):59-62. Epub 2018 Sep 21.

Department of Molecular Engineering, Graduate School of Engineering, Kyoto University, Kyoto-Daigaku Katsura, Nishikyo-Ku, Kyoto, 615-8510, Japan.

Epigenetic regulation is essential to various biological phenomena such as cell differentiation and cancer. DNA methylation is one of the most important epigenetic signals, as it is directly involved in gene silencing of transposable elements, genomic imprinting, and chromosome X inactivation. To mediate these processes, methyl-CpG-binding domain (MBD) proteins recognize specific signals encoded in the form of DNA methylation patterns. Read More

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http://dx.doi.org/10.1007/s12104-018-9851-2DOI Listing
April 2019
3 Reads

Chemical shift assignment of the viral protein genome-linked (VPg) from potato virus Y.

Biomol NMR Assign 2019 04 21;13(1):9-13. Epub 2018 Sep 21.

Department of Pathology and Cell Biology, Institute of Research in Immunology and Cancer (IRIC), Université de Montréal, Pavilion Marcelle-Coutu, Chemin Polytechnique, Montreal, QC, Canada.

The dysregulation of translation contributes to many pathogenic conditions in humans. Discovering new translational mechanisms is important to understanding the diversity of this process and its potential mechanisms. Such mechanisms can be initially observed in viruses. Read More

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http://dx.doi.org/10.1007/s12104-018-9842-3DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6428624PMC
April 2019
2 Reads

H, N and C resonance assignments of the C-terminal domain of the P protein of the Nishigahara strain of rabies virus.

Biomol NMR Assign 2019 04 20;13(1):5-8. Epub 2018 Sep 20.

Department of Biochemistry and Molecular Biology, University of Melbourne, Parkville, VIC, 3010, Australia.

The C-terminal domain of the P protein of rabies virus is a multifunctional domain that interacts with both viral and host cell proteins. Here we report the H, C and N chemical shift assignments of this domain from P protein of the Nishigahara strain of rabies virus, a pathogenic laboratory strain well established for studies of virulence functions of rabies virus proteins, including P protein. The data and secondary structure analysis are in good agreement with the reported predominantly helical structure of the same domain from the CVS strain of rabies solved by crystallography. Read More

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http://dx.doi.org/10.1007/s12104-018-9841-4DOI Listing
April 2019
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Backbone H, C, and N resonance assignments of deubiquitinase A in non-phosphorylated and phosphorylated forms.

Biomol NMR Assign 2019 04 19;13(1):37-42. Epub 2018 Sep 19.

Department of Chemistry, University of Louisville, 2320 South Brook Street, Louisville, KY, 40208, USA.

Ubiquitination is one of the most prevalent forms of post-translational modifications that are important for regulating many cellular processes in eukaryotes. Deubiquitinases are proteases that hydrolyze the isopeptide or peptide bonds formed between ubiquitin and the target proteins or within a polyubiquitin chain. Deubiquitinase A (DUBA) is a deubiquitinase known to be a negative regulator of innate immune responses in humans by suppressing production of type I interferons (INF-I). Read More

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http://link.springer.com/10.1007/s12104-018-9847-y
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http://dx.doi.org/10.1007/s12104-018-9847-yDOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6424661PMC
April 2019
18 Reads

Sequence specific H, C and N resonance assignments of the C-terminal domain of human γS-crystallin.

Biomol NMR Assign 2019 04 19;13(1):43-47. Epub 2018 Sep 19.

Center for Interdisciplinary Sciences, Tata Institute of Fundamental Research, Gopanpally, Hyderabad, 500107, India.

The high solubility and stability of crystallins present in the human eye lens maintains its transparency and refractive index with negligible protein turnover. Monomeric γ-crystallins and oligomeric β-crystallins are made up of highly homologous double Greek key domains. These domains are symmetric and possess higher stability as a result of the complex topology of individual Greek key motifs. Read More

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http://dx.doi.org/10.1007/s12104-018-9848-xDOI Listing
April 2019
3 Reads

H, C and N NMR assignments of two plant protease inhibitors (IRD7 and IRD12) from the plant Capsicum annuum.

Biomol NMR Assign 2019 04 18;13(1):31-35. Epub 2018 Sep 18.

Center for Interdisciplinary Sciences, Tata Institute of Fundamental Research, Gopanpally, Hyderabad, 500075, India.

Helicoverpa species are polyphagous pests, with the larval stages causing major damage to economically valuable crops such as cotton, tomato, corn, sorghum, peas, sunflower, wheat and other pulses. Over the years, Helicoverpa armigera has developed resistance to most classes of chemical insecticides, and consequently it is now largely controlled on cotton plants via the use of Bt transgenic crops that express insecticidal Cry toxins which in-turn expedited resistance development in a number of pest species including H. armigera. Read More

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http://dx.doi.org/10.1007/s12104-018-9846-zDOI Listing
April 2019
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H, C, and N resonance assignments of the C-terminal lobe of the human HECT E3 ubiquitin ligase ITCH.

Biomol NMR Assign 2019 04 18;13(1):15-20. Epub 2018 Sep 18.

Gustaf H. Carlson School of Chemistry and Biochemistry, Clark University, 950 Main St., Worcester, MA, 01610, USA.

ITCH (aka Atrophin-1-interacting protein 4) is a prominent member of the NEDD4 HECT (Homologous to E6AP C-Terminus) E3 ubiquitin ligase family that regulates numerous cellular functions including inflammatory responses through T-cell activation, cell differentiation, and apoptosis. Known intracellular targets of ITCH-dependent ubiquitylation include receptor proteins, signaling molecules, and transcription factors. The HECT C-terminal lobe of ITCH contains the conserved catalytic cysteine required for the covalent attachment of ubiquitin onto a substrate and polyubiquitin chain assembly. Read More

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http://dx.doi.org/10.1007/s12104-018-9843-2DOI Listing
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6439258PMC
April 2019
1 Read

Backbone chemical shift assignment of macrophage infectivity potentiator virulence factor of Trypanosoma cruzi.

Biomol NMR Assign 2019 04 18;13(1):21-25. Epub 2018 Sep 18.

Centro de Espectroscopia de Resonancia Magnética Nuclear (CERMN), Departamento de Ciencias - Química, Pontificia Universidad Católica del Perú, Lima, Peru.

Chagas disease is a trypanosomiasis disease inflicted by Trypanosoma cruzi parasite. In Latin America, at least 10 million people are infected and annually, 10,000 casualties are deplored. Macrophage infectivity potentiator protein is one of the major virulence factors secreted by T. Read More

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http://dx.doi.org/10.1007/s12104-018-9844-1DOI Listing
April 2019
2 Reads