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1دورية أكاديمية
المؤلفون: Xu, Qingping, Chiu, Hsiu-Ju, Farr, Carol L, Jaroszewski, Lukasz, Knuth, Mark W, Miller, Mitchell D, Lesley, Scott A, Godzik, Adam, Elsliger, Marc-André, Deacon, Ashley M, Wilson, Ian A
المصدر: Journal of Molecular Biology. 426(1)
مصطلحات موضوعية: Microbiology, Biochemistry and Cell Biology, Biological Sciences, Prevention, Vaccine Related, Biodefense, Emerging Infectious Diseases, Infectious Diseases, 2.2 Factors relating to the physical environment, Aetiology, Infection, Amino Acid Sequence, Catalytic Domain, Clostridioides difficile, Crystallography, X-Ray, DNA Transposable Elements, Hydrolases, Models, Molecular, Molecular Sequence Data, Protein Conformation, Sequence Alignment, Staphylococcus aureus, bifunctional cell wall lysin, bacterial lysozyme, murarhidase, NIpC/P60 endopeptidase, Tn916 family conjugative transposons, JCSG, Joint Center for Structural Genomics, LT, MAD, MD, MGE, MR, N-acetylglucosamine, N-acetylmuramic acid, NAG, NAM, NIGMS, NIH, National Institute of General Medical Sciences, National Institutes of Health, NlpC/P60 endopeptidase, PSI, Protein Structure Initiative, SSRL, Stanford Synchrotron Radiation Lightsource, TEV, asu, asymmetric unit, lytic transglycosylase, mobile genetic element, molecular dynamics, molecular replacement, multi-wavelength anomalous dispersion, muramidase, tobacco etch virus, Medicinal and Biomolecular Chemistry, Biochemistry & Molecular Biology, Biochemistry and cell biology
وصف الملف: application/pdf
URL الوصول: https://escholarship.org/uc/item/99r483zn
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2مؤتمر
المساهمون: Bergmann, Uwe
المصدر: Conference: Brookhaven;s Women in Science Lecture Series, Brookhaven National Laboratory, Upton, New York, presented on May 20, 2009
وصف الملف: Medium: AV; Size: 1:12:06
URL الوصول: http://www.osti.gov/scitech/servlets/purl/988019
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المؤلفون: Hallonsten, Olof
المصدر: Lund Studies in Research Policy. 1
مصطلحات موضوعية: big science, little science, sophistication, collectivization, European Synchrotron Radiation Facility, Stanford Synchrotron Radiation Lightsource, MAX-lab, scientific entrepreneurs, changing dynamics of science, Synchrotron radiation, research policy, science policy, Samhällsvetenskap, Annan samhällsvetenskap, Tvärvetenskapliga studier inom samhällsvetenskap, Social Sciences, Other Social Sciences, Social Sciences Interdisciplinary
وصف الملف: electronic
URL الوصول: https://lup.lub.lu.se/record/1419054
https://portal.research.lu.se/files/6110708/1419183.pdf -
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وصف الملف: Medium: AV; Other: 00:01:49
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المصدر: Bioscience Reports
مصطلحات موضوعية: Models, Molecular, Protein Conformation, ATPase, MBD, metal-binding domain, SSRL, Stanford Synchrotron Radiation Lightsource, Crystallography, X-Ray, Biochemistry, RMSD, root mean square deviation, chemistry.chemical_compound, Protein structure, Adenosine Triphosphate, Copper Transport Proteins, Catalytic Domain, PEG, poly(ethylene glycol), P-domain, phosphorylation doamin, Cation Transport Proteins, Adenosine Triphosphatases, 0303 health sciences, biology, Chemistry, Hydrolysis, 030302 biochemistry & molecular biology, p[NH]ppA, adenosine 5′-[β,γ-imido]triphosphate, AMPPCP, adenosine 5′-(β,γ-methylene)triphosphate, ATPase transporter, Archaeoglobus fulgidus, Energy source, Binding domain, crystal structure, ATPBD, ATP-binding domain, Archaeal Proteins, Molecular Sequence Data, Biophysics, S2, Phosphates, 03 medical and health sciences, CopB, Hydrolase, HAD, haloacid dehalogenase, Amino Acid Sequence, Binding site, SERCA1, sarcoplasmic/endoplasmic reticulum Ca2+-ATPase 1, Molecular Biology, Lp-CopA, Legionella pneumophila CopA, 030304 developmental biology, Original Paper, Binding Sites, ATP-binding domain (ATPBD), Base Sequence, Cell Biology, metal transport, Protein Structure, Tertiary, Crystallography, Catalytic cycle, A-domain, actuator domain, copper, biology.protein, IPTG, isopropyl β-D-thiogalactoside, N-domain, nucleotide-binding domain, Adenosine triphosphate
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fb10135f8ccab5f2edee45830f61e213
http://europepmc.org/articles/PMC3475447 -
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المؤلفون: Lukasz Jaroszewski, Ashley M. Deacon, Qingping Xu, Scott A. Lesley, Ian A. Wilson, Adam Godzik, Mark W. Knuth, Mitchell D. Miller, Hsiu-Ju Chiu, Marc-André Elsliger, Carol L. Farr
المصدر: Journal of molecular biology, vol 426, iss 1
مصطلحات موضوعية: Models, Molecular, Hydrolases, Protein Conformation, Crystallography, X-Ray, tobacco etch virus, Joint Center for Structural Genomics, chemistry.chemical_compound, Protein structure, Structural Biology, Models, LT, Catalytic Domain, National Institutes of Health, 2.2 Factors relating to the physical environment, Glycoside hydrolase, PSI, SSRL, Aetiology, Peptide sequence, Crystallography, JCSG, biology, MAD, molecular replacement, Infectious Diseases, Biochemistry, multi-wavelength anomalous dispersion, Lysozyme, Infection, Staphylococcus aureus, Biochemistry & Molecular Biology, asymmetric unit, murarhidase, Molecular Sequence Data, Sequence alignment, muramidase, National Institute of General Medical Sciences, Microbiology, Article, Stanford Synchrotron Radiation Lightsource, Vaccine Related, Medicinal and Biomolecular Chemistry, Biodefense, Hydrolase, Tn916 family conjugative transposons, Amino Acid Sequence, Molecular Biology, NlpC/P60 endopeptidase, NIH, bacterial lysozyme, Clostridioides difficile, MD, Prevention, MGE, mobile genetic element, Active site, Molecular, MR, N-acetylglucosamine, NIpC/P60 endopeptidase, molecular dynamics, NAG, NIGMS, Emerging Infectious Diseases, chemistry, N-Acetylmuramic acid, NAM, biology.protein, DNA Transposable Elements, X-Ray, TEV, lytic transglycosylase, Biochemistry and Cell Biology, Sequence Alignment, N-acetylmuramic acid, bifunctional cell wall lysin, Protein Structure Initiative, asu
وصف الملف: application/pdf
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3ca799967e8ac6f497f217b1c707d035
https://escholarship.org/uc/item/99r483zn -
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المساهمون: Bushnell, Dave
وصف الملف: Medium: AV; Other: 00:04:00
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المؤلفون: Lukasz Jaroszewski, Dustin C. Ernst, Keith O. Hodgson, Lian Duan, Tamara Astakhova, Abhinav Kumar, Tiffany Wooten, Michelle Chiu, Julie Feuerhelm, Edward Nigoghossian, Daniel McMullan, Gye Won Han, Qingping Xu, Christine B Trame, Linda Okach, Debanu Das, Herbert L. Axelrod, Polat Abdubek, Heath E. Klock, Carol L. Farr, Mitchell D. Miller, Sanjay Krishna, Alex Bateman, Henry van den Bedem, Anna Grzechnik, David Marciano, Thomas Clayton, Marc C. Deller, Connie Chen, Christopher L. Rife, Natasha Sefcovic, John Wooley, Constantina Bakolitsa, Kevin K. Jin, Hsiu-Ju Chiu, Amanda Nopakun, Marc André Elsliger, Andrew T. Morse, Dennis Carlton, Ian A. Wilson, Christina Puckett, Adam Godzik, Ashley M. Deacon, Kyle Ellrott, Joanna C Grant, Robert D. Finn, Dana Weekes, Piotr Kozbial, Henry J Tien, Mark W. Knuth, Ron Reyes, Scott A. Lesley
المصدر: Journal of Molecular Biology
مصطلحات موضوعية: Models, Molecular, asu, asymmetric unit, Protein Data Bank (RCSB PDB), SSRL, Stanford Synchrotron Radiation Lightsource, Crystallography, X-Ray, Protein Structure, Secondary, chemistry.chemical_compound, PH, Pleckstrin homology, Structural Biology, Pleckstrin homology (PH) domain, Conserved Sequence, 0303 health sciences, 030302 biochemistry & molecular biology, bacterial PH domain (PHb), Pleckstrin homology domain, Eukaryotic Cells, Biochemistry, Domain (ring theory), TCEP, higher-order symmetry, DUF1696, domain of unknown function family 1696, lipids (amino acids, peptides, and proteins), VPS36, vacuolar protein sorting protein 36, Protein Binding, Protein family, Surface Properties, Stereochemistry, Molecular Sequence Data, PTB, phosphotyrosine binding, protein assembly, Biology, Ring (chemistry), Article, TEV, tobacco etch virus, Structural genomics, Evolution, Molecular, 03 medical and health sciences, TCEP, tris(2-carboxyethyl)phosphine–HCl, Bacterial Proteins, PDB, Protein Data Bank, MAD, multiwavelength anomalous diffraction, ALS, Advanced Light Source, Amino Acid Sequence, Protein Structure, Quaternary, PIPE, Polymerase Incomplete Primer Extension, protein evolution, Molecular Biology, PEG, polyethylene glycol, 030304 developmental biology, Binding Sites, Bacteria, Sequence Homology, Amino Acid, biology.organism_classification, Protein Structure, Tertiary, JCSG, Joint Center for Structural Genomics, Prokaryotic Cells, chemistry, PHb, bacterial PH domain, Sequence Alignment
URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::832d4b50fc307a2eeff690322443fe16
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9مورد إلكتروني
المصدر: Lund Studies in Research Policy; 1 (2009)
مصطلحات الفهرس: Social Sciences Interdisciplinary, big science, little science, sophistication, collectivization, European Synchrotron Radiation Facility, Stanford Synchrotron Radiation Lightsource, MAX-lab, scientific entrepreneurs, changing dynamics of science, Synchrotron radiation, research policy, science policy, thesis/docmono, info:eu-repo/semantics/doctoralThesis, text
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10دورية أكاديمية
المؤلفون: Davenport AM; Division of Chemistry and Chemical Engineering, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA., Huber FM; Division of Chemistry and Chemical Engineering, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA., Hoelz A; Division of Chemistry and Chemical Engineering, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA. Electronic address: hoelz@caltech.edu.
المصدر: Journal of molecular biology [J Mol Biol] 2014 Feb 06; Vol. 426 (3), pp. 526-41. Date of Electronic Publication: 2013 Oct 10.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
بيانات الدورية: Publisher: Elsevier Country of Publication: Netherlands NLM ID: 2985088R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1089-8638 (Electronic) Linking ISSN: 00222836 NLM ISO Abbreviation: J Mol Biol Subsets: MEDLINE
مواضيع طبية MeSH: Regulatory Elements, Transcriptional*, NAD/*metabolism , Sirtuin 1/*chemistry , Sirtuin 1/*metabolism, Acetylation ; Binding Sites ; Crystallography, X-Ray ; Humans ; Models, Molecular ; Protein Conformation