Cited by 1,000RNA and protein synthesis mechanismsRNA modifications and cancerEnzyme Structure and Function

The DOI matches its Crossref record; 71 of the 72 references it cites were found in a registry or an index.

Structure of Functionally Activated Small Ribosomal Subunit at 3.3 Å Resolution

Open access

Schluenzen, Frank, Tocilj, Ante, Zarivach, Raz, Harms, Joerg, Gluehmann, Marco, Janell, Daniela, Bashan, Anat, Bartels, Heike, Agmon, Ilana, Franceschi, François, Yonath, Ada·2000·Cell

DOI 10.1016/s0092-8674(00)00084-2

Open this paper in CoChat — free account Open PDF

Abstract

The small ribosomal subunit performs the decoding of genetic information during translation. The structure of that from Thermus thermophilus shows that the decoding center, which positions mRNA and three tRNAs, is constructed entirely of RNA. The entrance to the mRNA channel will encircle the message when a latch-like contact closes and contributes to processivity and fidelity. Extended RNA helical elements that run longitudinally through the body transmit structural changes, correlating events at the particle's far end with the cycle of mRNA translocation at the decoding region. 96% of the nucleotides were traced and the main fold of all proteins was determined. The latter are either peripheral or appear to serve as linkers. Some may assist the directionality of translocation.

Integrity signals

Registry

Crossref · 10.1016/s0092-8674(00)00084-2

Cites

71 of 71 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
The CCP4 suite: programs for protein crystallography
Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,317
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,723
Crystal structure of the nucleosome core particle at 2.8 Å resolution
Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., & Richmond, T. J. (1997) · Nature · doi:10.1038/38444 · Cited by 9,466
[27] Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
Fortelle, E. D. L., & Bricogne, G. (1997) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(97)76073-7 · Cited by 1,892
Methods used in the structure determination of bovine mitochondrial F1 ATPase
Abrahams, J. P., & Leslie, A. G. W. (1996) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444995008754 · Cited by 1,090
Efficient anisotropic refinement of macromolecular structures using FFT
Murshudov, G. N., Vagin, A. A., Lebedev, A., Wilson, K. S., & Dodson, E. J. (1999) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s090744499801405x · Cited by 937
Structure, Function, and Genetics of Ribosomes
Hardesty, B., & Kramer, G. (1986) · Springer series in molecular biology · doi:10.1007/978-1-4612-4884-2 · Cited by 852
A ratchet-like inter-subunit reorganization of the ribosome during translocation
Frank, J., & Agrawal, R. K. (2000) · Nature · doi:10.1038/35018597 · Cited by 799
X-ray Crystal Structures of 70 S Ribosome Functional Complexes
Cate, J. H. D., Yusupov, M., Yusupova, G. Z., Earnest, T. N., & Noller, H. F. (1999) · Science · doi:10.1126/science.285.5436.2095 · Cited by 583

Show all 72 references

Sorted by citations

Items 901–1,000 of 1,000

Bioloogia-Geograafiateaduskond Molekulaar- ja Rakubioloogia Instituut Molekulaarbioloogia Õppetool
Karitkina, D. (2004)
Escherichia coli 23S rRNA heeliks 69 roll ribosoomis
Karitkina, D. (2004) · DSpace repository (University of Tartu)
The Future of Biological X-Ray Analysis
Rees, D. C. (2008) · IMPERIAL COLLEGE PRESS eBooks · doi:10.1142/9781848162013_0007
Ribosomes and the Synthesis of Proteins
Metzler, D. E., Metzler, C. M., & Sauke, D. J. (2001) · Elsevier eBooks · doi:10.1016/b978-012492543-4/50032-5
Diagnostics of inflammatory bowel disease using fecal microbiota: Diagnostic markers and commercial potential
Frøyland, C. (2010) · NORA - Norwegian Open Research Archives
RIBOSOMAL CRYSTALLOGRAPHY: DYNAMICS, FLEXIBILITY AND PEPTIDE BOND FORMATION
Yonath, A. (2004) · WORLD SCIENTIFIC eBooks · doi:10.1142/9789812562647_0012
Self-citation
Structure and mechanism of 16S rRNA in the ribosome studied by photocrosslinking
Nanda, K. (2004) · NCSU Libraries Repository (North Carolina State University Libraries)
Analysis of Genetic Translation using Signal Processing
Ponnala, L. (2008) · NCSU Libraries Repository (North Carolina State University Libraries)
A tale of two antibiotics : Fusidic acid and Viomycin
Holm, M. (2016) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
Rate and Accuracy of Bacterial Protein Synthesis
Johansson, M. (2012) · Uppsala University Publications (Uppsala University)
NMR study of eukaryotic translation termination
Wong, L. E. (2013) · DR-NTU (Nanyang Technological University) · doi:10.32657/10356/54845
Structure Function Relationships in the 5' ETS of the Schizosaccharomyces pombe pre-rRNA
Nellimarla, S. (2012) · The Atrium (University of Guelph)
The role of a highly conserved eubacterial ribosomal protein in translation quality control
Naganathan, A. (2015) · Journal of International Crisis and Risk Communication Research
A structural view on ligands at the ribosomal tunnel exit
Leidig, C. (2012) · doi:10.5282/edoc.15561
Kinetics of subunit rotation of the ribosome during tRNA-mRNA translocation
Sharma, H. (2017) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-6407
Constructing Mutant Ribosomes Containing Mutant Ribosomal RNAs
Kitahara, K., & Miyazaki, K. (2018) · Springer eBooks · doi:10.1007/978-981-10-8372-3_2
Investigation of the Kinetics of Tet(O)-mediated Tetracycline Resistance
Li, J. (2010) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r3fd69
Big data analytics in computational biology and bioinformatics
Byron, K. (2017)
Deletion or substitution of conserved amino acid residues at the tip of the domain IV of Tet(O) impairs tetracycline resistance
Mukherjee, O. (2011) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r3k43n
Towards X-ray crystallographic characterization of nucleosome interactions with linker histones, FOXA proteins and high mobility group N factors
Ravi, S. (2018) · doi:10.32657/10356/74380
Cryo-EM structure of the Mycobacterium smegmatis ribosome
Mishra, S. (2018) · doi:10.32657/10220/47514
Structure Information
Cygler, M., Matte, A., & Schrag, J. D. (2001) · Biotechnology · doi:10.1002/9783527620876.ch15
Predicting and data mining of RNA-ligand pattern interactions against RNA base residue arrangements
Yahaya, Z. H. B., & Firdaus‐Raih, M. (2019) · AIP conference proceedings · doi:10.1063/1.5111248
Crystallography of the past and in the future
Liljas, A. (2020) · Crystallography Reviews · doi:10.1080/0889311x.2020.1758076
Recoding of bacteriophage T4 gene 60 mRNA by programmed translational bypassing
Klimova, M. (2020) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-8128
Protein Crystallography: Recent Advances and the Future
Nakagawa, A. (2020) · Nihon Kessho Gakkaishi · doi:10.5940/jcrsj.62.185
The world of catalytic nucleic acids
Jaeger, L. (2001)
Applications of Ribosomal RNA Sequence and Structure Analysis for Extracting Evolutionary and Functional Insights
Ng, C. L., & Firdaus‐Raih, M. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-809633-8.20443-3 · Cited by 1
Protein and Peptide Gas-phase Structure Investigation Using Collision Cross Section Measurements and Hydrogen Deuterium Exchange
Khakinejad, M. (2017) · doi:10.33915/etd.5967
Next-Generation Sequencing Techniques to Study HIV-1 Transcription and RNA Structure
Tomezsko, P. J. (2020) · Digital Access to Scholarship at Harvard (DASH) (Harvard University)
6. Biotechnology. (1) X-Ray Protein Crystallography
Nakagawa, A. (2001) · RADIOISOTOPES · doi:10.3769/radioisotopes.50.special_78s
Путь к расшифровке атомных структур прокариотической и эукариотической рибосом
Yusupova, G. Z., & Yusupov, M. (2021) · Biochemistry (Moscow) · doi:10.31857/s0320972521080054
r RNA Structure
Malhotra, A. (2001) · Encyclopedia of Life Sciences · doi:10.1038/npg.els.0000537
Chemical Bonding in Crystals and Their Properties
Vologzhanina, A. V., & Nelyubina, Y. V. (2020) · MDPI eBooks · doi:10.3390/books978-3-03936-171-7
References
(2020) · Wiley eBooks · doi:10.1002/9781119309697.ref
Therapeutic Agents Acting on RNA Targets
Rife, J. P. (2003) · Burger's Medicinal Chemistry and Drug Discovery · doi:10.1002/0471266949.bmc025
Introduction
Davidovich, C. (2011) · Springer eBooks · doi:10.1007/978-3-642-16931-1_1
Enzym- und Proteinanalytik
Westermann, P., & Wittmann‐Liebold, B. (2003) · Springer eBooks · doi:10.1007/978-3-662-07588-3_14
Optimising His-tags for purification and phasing
Groβe, C. (2011) · doi:10.53846/goediss-2227
Structural Analysis of the 50S Ribosomal Stalk
Diaconu, M. (2007) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-214
Peer Review #1 of "The nematode homologue of Mediator complex subunit 28, F28F8.5, is a critical regulator of C. elegans development (v0.1)"
(2017) · PeerJ · doi:10.7287/peerj.3390v0.1/reviews/1
Macromolecular assemblages
Rey, F. A., & Sundquist, W. I. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.03.001
RIBOSOMAL RNA (r RNA )
Gutell, R. R. (2004) · Wiley eBooks · doi:10.1002/9780471650126.dob0628.pub2
Molekülmodelle und Modellmoleküle: Strukturanalyse großer biologischer Moleküle für die Medizin
Muller, Y. A., & Heinemann, U. (2003) · Springer eBooks · doi:10.1007/978-3-662-07588-3_11
Structure Information
Cygler, M., Matte, A., & Schrag, J. D. (2001) · Wiley eBooks · doi:10.1002/9783527620999.ch15e
Protein Translation
Jan, E. (2014) · Colloquium Series on Building Blocks of the Cell Cell Structure and Function · doi:10.4199/c00106ed1v01y201406bbc006
Ribosomes
Liljas, A. (2001) · Encyclopedia of Genetics · doi:10.1006/rwgn.2001.1126
Faculty Opinions recommendation of Protein crystallography for non-crystallographers, or how to get the best (but not more) from published macromolecular structures.
Gervasio, F. L., & Kuzmanic, A. (2019) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.10138956.793559457
The paths to the atomic structures of proteins and nucleic acids
Schulz, G. E. (2023) · ChemTexts · doi:10.1007/s40828-023-00180-x
Plant specificities in rRNA processing : from snoRNA to rRNA variations
Streit, D. (2023) · doi:10.21248/gups.74824
Atomic structures of ribosomes at work captured by in situ cryo-electron tomography
Guo, Q., Baumeister, W. P., & Gao, N. (2023) · 中国科学通报：英文版 · doi:10.1016/j.scib.2023.09.035
Identification of Selected Kinetoplastids 18S rRNA Residues required for Efficient Recruitment of Initiator tRNA Met and AUG Selection in silico
Mwangi, H. N., Muge, E. K., Wagacha, P. W., Ndakala, A., & Mulaa, F. J. (2023) · International Journal of Bioinformatics and Intelligent Computing · doi:10.61797/ijbic.v2i1.202
Deteksi Bakteri Endofit Dan Pengaruh Microbacterium arborescens Terhadap Pertumbuhan Sorgum Manis (Sorghum bicolor)
Putri, R. N. (2021) · Al-Hayat Journal of Biology and Applied Biology · doi:10.21580/ah.v4i2.18820
An Atlas of the base inter-RNA stacks involved in bacterial translation
Ali, Z., Kukhta, T., Trant, J. F., & Sharma, P. (2023) · Biophysical Chemistry · doi:10.1016/j.bpc.2023.107144
RNA Temelli Terapötik Yaklaşımlar
Korkmaz, İ., & Arslan, S. (2024) · Uludağ Üniversitesi Tıp Fakültesi Dergisi · doi:10.32708/uutfd.1427446
Characterization of the herbivore and carnivore faecal microbiota with special emphasis on diet and host-specificity
Zoelzer, F. (2024) · Publication Server of Goethe University Frankfurt am Main (Goethe University Frankfurt) · doi:10.21248/gups.85997
Applications of Ribosomal RNA Sequence and Structure Analysis for Extracting Evolutionary and Functional Insights
Ng, C. L., & Firdaus‐Raih, M. (2019) · Elsevier eBooks · doi:10.1016/b978-0-323-95502-7.00354-7
Specialty grand challenges in theoretical modeling, structure prediction and design
Exertier, C., & Ilari, A. (2025) · Frontiers in Chemical Biology · doi:10.3389/fchbi.2025.1635423
GluK2 kainate receptor subunit-selective, potentiating RNA aptamer
Ingenito, S. R., Saunders, N., Lininger, K. J., & Niu, L. (2025) · Scientific Reports · doi:10.1038/s41598-025-15323-y
The Microbiome in Epidemiological Research
Shaw, L. P. (2025) · Springer eBooks · doi:10.1007/978-3-031-76448-6_4
RNA secondary structure prediction: a practical guide
Mao, L., & Mathews, D. H. (2025) · Elsevier eBooks · doi:10.1016/b978-0-323-99507-8.00005-6
The NeverEnding E-Story
Metelev, V., & Bogdanov, A. A. (2025) · Biochemistry (Moscow) · doi:10.1134/s0006297925602503
Ribosomal proteins L5 and L15 : Functional characterisation of important features, in vivo
Simoff, I. (2009) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
The ribosome, stringent factor and the bacterial stringent response.
Jenvert, R.-M. (2007) · KTH Publication Database DiVA (KTH Royal Institute of Technology)
The Role of SmpB in Licensing tmRNA Entry into Stalled Ribosomes
Miller, M. R. (2013) · ScholarsArchive (Brigham Young University)
Dynamics, Degradation, and Chemical Modification of Non-Coding RNA
Hoerter, J. A. H. (2008) · Deep Blue (University of Michigan)
Binding characteristics and localization of Arabidopsis thaliana ribosomal protein S15a isoforms
Wakely, H. (2008) · University Library - University of Saskatchewan (University of Saskatchewan)
Additional file 4 of A comparative plastome approach enhances the assessment of genetic variation in the Melilotus genus
Xu, P., Meng, M., Wu, F., & Zhang, J. (2024) · Figshare · doi:10.6084/m9.figshare.26729227
Additional file 1 of A comparative plastome approach enhances the assessment of genetic variation in the Melilotus genus
Xu, P., Meng, M., Wu, F., & Zhang, J. (2024) · Figshare · doi:10.6084/m9.figshare.25963169
Additional file 2 of A comparative plastome approach enhances the assessment of genetic variation in the Melilotus genus
Xu, P., Meng, M., Wu, F., & Zhang, J. (2024) · Figshare · doi:10.6084/m9.figshare.25963284
Additional file 3 of A comparative plastome approach enhances the assessment of genetic variation in the Melilotus genus
Xu, P., Meng, M., Wu, F., & Zhang, J. (2024) · Figshare · doi:10.6084/m9.figshare.26729224
Transcriptome Analysis of Germinating Cyst-Like Dormant Cells of Escherichia coli K-12
El-Registan, G. I., Deryabin, D. G., Лойко, Н. Г., Mardanov, A. V., Beletsky, A. V., Galuza, O. A., & Nikolaev, Y. A. (2026) · Microbiology · doi:10.1134/s002626172560363x
Structural study of the eukaryotic ribosome
de Loubresse, N. G. (2012) · theses.fr (ABES) · doi:10.70675/a228e931zfe02z4725zad2fz53f91e8c1b78
Aminoglycoside modifying enzymes involved in antibiotic resistance : functional and structural studies
Kaplan, E. (2015) · doi:10.70675/ee48557dz9007z47c9zbf9az52f552e5421e
Structural studies of the Staphylococcus aureus ribosome
Khusainov, I. S. (2015) · theses.fr (ABES) · doi:10.70675/c0dbca86zfcfcz4ea7z9038z773a5c0eedc4
Structure-function studies of human ribosome complexes
Khatter, H. (2014) · theses.fr (ABES) · doi:10.70675/576d1963z5f06z4969z8e92za6c59db0443a
Le contrôle qualité de la synthèse protéique comme cible pour le développement de nouveaux antibiotiques
Macé, K. (2016) · theses.fr (ABES) · doi:10.70675/3a39f6d2zca67z40e5z926ezf4ff78260a14
Etude des erreurs programmées du ribosome par microscopie de fluorescence en molécule unique
Barbier, N. (2017) · doi:10.70675/fc337e4ez4c3ez4e09za08bze7d1e0c93f3d
Etude de la structure et de la fonction d'un complexe constitué de 5 protéines non ribosomiques Npa1p, Npa2p, Dbp6p, Nop8p et Rsa3p essentielles à la formation de la grande sous unité des ribosomes eucaryotes
Joret, C. (2016) · theses.fr (ABES) · doi:10.70675/50f3ec36z11f5z4497za5b4za48a486bf61e
Docking Flexible Proteins using Polynomial Expansions.
Hoffmann, A. (2018) · doi:10.70675/55e49914z669bz4744zbc01zaa022e76e6d9
Études structurales de la trans-traduction, cible privilégiée pour le développement de nouveaux antibiotiques
Guyomar, C. (2018) · theses.fr (ABES) · doi:10.70675/fbc75c6ez3a43z4ec9zab44z8e4d0b359aaa
Analyse structurale de la biogenèse de la petite sous-unité ribosomique eucaryote par cryo-microscopie électronique et analyse d'images
Azad, S. R. S. (2019) · theses.fr (ABES) · doi:10.70675/84295de9zf03fz4fffzacddzcadc50df26a7
Metagenomics, a relevant tool for assessing the impact of different agricultural practices on soil microbial communities
Alahmad, A. (2017) · theses.fr (ABES) · doi:10.70675/2f42402dzacb0z4a81z9c9cz239c677938b9
Exploration of Catalytic Ribonucleic Acids and Implementation of an Essential Function in Escherichia coli
Trottier, K. (2019) · theses.fr (ABES) · doi:10.70675/0a1315e7zb79ez478az9edaz4a50fd4774d2
Structural differences and specificities of mRNA translation initiation complexes between trypanosomes and their hosts
Bochler, A. (2020) · theses.fr (ABES) · doi:10.70675/c6c84d2ez1844z4ce2z8e9cz814164ecbf34
Structural and functional studies on transcriptional proofreading by GreA
Eduljee, A. (2021) · theses.fr (ABES) · doi:10.70675/27cce8d0zdc6dz4d77z9f4dzd631b6a7c7f5
Dbp6, an RNA helicase required for the early steps of synthesis of the large subunit of the eukaryotic ribosome
Khreiss, A. (2022) · theses.fr (ABES) · doi:10.70675/439e8092z87b7z4839zb66aza05d463a84af
Identification et caractérisation de gènes candidats pour la découverte de nouveaux mécanismes physiopathologiques à l'origine de l'anémie de Blackfan-Diamond
Anton, A. (2020) · theses.fr (ABES) · doi:10.70675/3d6a17a8z63e6z411fz9ebcz30fc679d6128
Étude du mécanisme d’action de nouveaux antibiotiques et de peptides antimicrobiens envers des cibles bactériennes
Adélaïde, M. (2023) · theses.fr (ABES) · doi:10.70675/0ae8bf9bz8546z4bf1za739zae0c9b1c527c
Role of aIF5B in archaeal translation initiation
Kazan, R. (2022) · theses.fr (ABES) · doi:10.70675/271059cdz82bcz4d1ez9c06z1f66f8033eb6
Exploiting Serial Crystallography in Structure-based Drug Design
Rizk, M. (2023) · doi:10.70675/51495fc0z882ez4243z81a1z0cb89047e143
Insights into the structural organization of the avian 80S ribosome from Gallus gallus
Nurullina, L. (2023) · doi:10.70675/2f747b0eza725z4eabz9c30zbd5b440af83c
Ribosome inhibition : cryo-EM and advancements in X-ray crystallography
Kolosova, O. A. (2023) · theses.fr (ABES) · doi:10.70675/fac7636bz91a9z4dbazb803z20817e06b018
Caractérisation structurale et fonctionnelle d'une asparagine isomérase dans la biogénèse de la petite sous-unité ribosomique bactérienne
Bonnettaz, B. (2024) · doi:10.70675/c1dc656bz0aebz48c2zb5f9z57deec7f1fc1
Etude de cinétique de la traduction eucaryote à l'échelle de la molécule unique
Fiszman, N. (2013) · doi:10.70675/254425a2z6659z4d26z9cd0z3f053b274a30
Shared Pathways to Peptides in Biochemistry and Prebiotic Chemistry through Ester Amide Exchange Chemistry
Ezerzer, Y., Hiregange, D., Bashan, A., Yonath, A., & Frenkel‐Pinter, M. (2026) · BioCosmos · doi:10.2478/biocosmos-2026-0002 · Cited by 1
Self-citation
Archaeology as a Toolkit for mRNA: History and Meaning in Use
Ariza‐Mateos, A., Bonilla, M. D.-Z., & Gómez, J. (2026) · Springer eBooks · doi:10.1007/978-3-032-24295-2_16
Mycobacteria Emerge as Leaders in Leaderless Translation
Canestrari, J. G., & Gray, T. A. (2026) · Annual Review of Microbiology · doi:10.1146/annurev-micro-042424-051945
Coupled metabolic reactions relevant to early biological evolution
Boog, H., & Unrau, P. J. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2619023123
Foundations of DNA and RNA Biology
Haseltine, W. A., & Patarca, R. (2026) · Springer eBooks · doi:10.1007/978-3-032-31089-7_1

Authors: Schluenzen, F., Tocilj, A., Zarivach, R., Harms, J., Gluehmann, M., Janell, D., Bashan, A., Bartels, H., Agmon, I., Franceschi, F., & Yonath, A.
Affiliations: Weizmann Institute of Science (IL)
ORCID: Schluenzen, Frank
Zarivach, Raz
Bashan, Anat
Agmon, Ilana
Yonath, Ada
Venue: Cell
Publisher: Elsevier BV
Published: 2000-09
Volume: 102
Issue: 5
Pages: 615-623
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/s0092-8674(00)00084-2
OpenAlex: W2092617311
Cited by: 979
References: 72
Citations by year: 2026: 11 · 2025: 13 · 2024: 18 · 2023: 28 · 2022: 18 · 2021: 26 · 2020: 27 · 2019: 18 · 2018: 22 · 2017: 25 · 2016: 18 · 2015: 31 · 2014: 26 · 2013: 27 · 2012: 43
FWCI: 28.84
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 4702 d)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute of General Medical Sciences (GM-34360, R01GM034360)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords: small ribosomal subunit, ribosome structure, Thermus thermophilus, decoding center, tRNA binding, mRNA translocation, translation fidelity, ribosomal proteins
MeSH terms: Binding Sites, Models, Molecular, Nucleic Acid Conformation, Protein Conformation, Ribosomes, RNA, Bacterial, RNA, Messenger, RNA, Ribosomal, 16S, RNA, Transfer, Structure-Activity Relationship, Thermus thermophilus, Crystallography, X-Ray, Base Pairing

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Structure of Functionally Activated Small Ribosomal Subunit at 3.3 Å Resolution

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks