Journal of Maxillofacial and Oral Surgery

Springer Nature
Springer Nature
ISSN: 09728279, 0974942X
SCImago
Q3
WOS
Q4
Impact factor
0.8
SJR
0.317
CiteScore
1.9
Categories
Oral Surgery
Otorhinolaryngology
Surgery
Areas
Dentistry
Medicine
Years of issue
2009-2025
journal names
Journal of Maxillofacial and Oral Surgery
J MAXILLOFAC ORAL SU
Publications
2 474
Citations
13 683
h-index
35
Top-3 countries
India (1679 publications)
Brazil (71 publications)
USA (64 publications)

Most cited in 5 years

Found 
from chars
Publications found: 1215
Backbone resonance assignment of the catalytic and ATP-binding domain of CpxA from Escherichia coli
Deng J., Zeng G., Xia W., Tang W., Chai Z., Liu Y., Li C., Huang L., Jiang L.
Q3
Springer Nature
Biomolecular NMR Assignments 2025 citations by CoLab: 0
Backbone and side‑chain 1H, 13C and 15N resonance assignments and secondary structure determination of the rhizobial FixJ
Horikawa A., Okubo R., Hishikura N., Watanabe R., Kurashima-Ito K., Sayeesh P.M., Inomata K., Mishima M., Koteishi H., Sawai H., Shiro Y., Ikeya T., Ito Y.
Q3
Springer Nature
Biomolecular NMR Assignments 2025 citations by CoLab: 0  |  Abstract
Abstract The symbiotic nitrogen-fixing bacterium Bradyrhizobium japonicum (B.japonicum) enables high soybean yields with little or no nitrogen fertiliser. A two component regulatory system comprising FixL, a histidine kinase with O2-sensing activity, and FixJ, a response regulator, controls the expression of genes involved in nitrogen fixation, such as fixK and nifA. Only under anaerobic conditions, the monophosphate group is transferred from FixL to the N-terminal receiver domain of FixJ (FixJN), which eventually promote the association of the C-terminal effector domain (FixJC) to the promoter regions of the nitrogen-fixation-related genes. Structural biological analyses carried out so far for rhizobial FixJ molecules have proposed a solution structure for FixJ that differs from the crystal structures, in which the two domains are extended. To understand the FixJ activation caused by phosphorylation of the N-terminal domain, which presumably regulates through the interactions between FixJN and FixJC, here we have performed backbone and sidechain resonance assignments of the unphosphorylated state of B. japonicum FixJ.
1H, 13C, 15N and 31P chemical shift assignment of the first stem-loop Guanidine-II riboswitch from Escherichia coli
Koob T., Döpp S., Schwalbe H.
Q3
Springer Nature
Biomolecular NMR Assignments 2025 citations by CoLab: 0  |  Abstract
Abstract A comprehensive understanding of RNA-based gene regulation is a fundamental aspect for the development of innovative therapeutic options in medicine and for a more targeted response to environmental problems. Within the different mechanisms of RNA-based gene regulation, riboswitches are particularly interesting as they change their structure in response to the interaction with a low molecular weight ligand, often a well-known metabolite. Four distinct classes of riboswitches recognize the very small guanidinium cation. We are focused on the Guanidine-II riboswitch with the mini-ykkC motif. We report here the assignment of the 1H, 13C, 15N and 31P chemical shifts of the 23 nucleotide-long sequence of the first stem-loop of the Guanidine-II riboswitch aptamer from Escherichia coli. Despite its small size, the assignment of the NMR signals of this RNA proved to be challenging as it has symmetrical base pairs and palindromic character.
Chemical shift assignments of DRB2 domains, a dsRNA binding protein in A. thaliana RNAi pathway
Rai U., Patra D., Deshmukh M.V.
Q3
Springer Nature
Biomolecular NMR Assignments 2025 citations by CoLab: 0
1H, 15N, 13C backbone resonance assignment of human Alkbh7
Faal B., Purslow J.A., Venditti V.
Q3
Springer Nature
Biomolecular NMR Assignments 2025 citations by CoLab: 0
Backbone assignment of the N-terminal domain of the A subunit of the Bacillus cereus GerI germinant receptor
Pustovalova Y., Li Y., Hoch J.C., Hao B.
Q3
Springer Nature
Biomolecular NMR Assignments 2025 citations by CoLab: 0
Backbone resonance assignments of PhoCl, a photocleavable protein
Wang R., Zhu L., Wang J., Zhu L.
Q3
Springer Nature
Biomolecular NMR Assignments 2025 citations by CoLab: 0
Assignment of the N-terminal domain of mouse cGAS
Aucharova H., Linser R.
Q3
Springer Nature
Biomolecular NMR Assignments 2025 citations by CoLab: 0  |  Abstract
AbstractCyclic GMP-AMP synthase (cGAS) is a DNA-sensing enzyme that is a member of the nucleotidyltransferase (NTase) family and functions as a DNA sensor. The protein is comprised of a catalytic NTase core domain and an unstructured hypervariable N-terminal domain (NTD) that was reported to increase protein activity by providing an additional DNA-binding surface. We report nearly complete 1H, 15N, and 13C backbone chemical-shift assignments of mouse cGAS NTD (residues 5-146), obtained with a set of 3D and 4D solution NMR experiments. Analysis of the chemical-shift values confirms that the NTD is intrinsically disordered. These resonance assignments can provide the basis for further studies such as activation by DNA and protein-protein interactions.
Backbone NMR resonance assignment of Sis1, a type B J-domain protein from Saccharomyces cerevisiae
Pinheiro G.M., Amorim G.C., Matos C.O., Ramos C.H., Almeida F.C.
Q3
Springer Nature
Biomolecular NMR Assignments 2024 citations by CoLab: 0
Correction: 1H, 13C, and 15N resonance assignments of the amyloidogenic peptide SEM2(49–107) by NMR spectroscopy
Troshkina A.A., Klochkov V.V., Bikmullin A.G., Klochkova E.A., Blokhin D.S.
Q3
Springer Nature
Biomolecular NMR Assignments 2024 citations by CoLab: 0
NMR resonance assignment of a ligand-binding domain of ephrin receptor A2
Mineev K.S., Gande S.L., Linhard V., Moghaddam S.K., Schwalbe H.
Q3
Springer Nature
Biomolecular NMR Assignments 2024 citations by CoLab: 0  |  Abstract
AbstractEphrin receptors regulate intercellular communication and are thus involved in tumor development. Ephrin receptor A2 (EphA2), in particular, is overexpressed in a variety of cancers and is a proven target for anti-cancer drugs. The N-terminal ligand-binding domain of ephrin receptors is responsible for the recognition of their ligands, ephrins, and is directly involved in receptor activation. Here, we report on the complete 1H, 15N and 13C NMR chemical shift assignment of EphA2 ligand binding domain that provides the basis for NMR-assisted drug design.
Backbone resonance assignments of the C-terminal thioesterase domain of tyrocidine synthetase C
Takeda M., Saito R., Konno S., Nagae T., Aoyama H., Yoshinaga S., Terasawa H., Taguchi A., Taniguchi A., Hayashi Y., Mishima M.
Q3
Springer Nature
Biomolecular NMR Assignments 2024 citations by CoLab: 0
1H, 13C, and 15N resonance assignments of the amyloidogenic peptide SEM2(49–107) by NMR spectroscopy
Troshkina A.A., Klochkov V.V., Bikmullin A.G., Klochkova E.A., Blokhin D.S.
Q3
Springer Nature
Biomolecular NMR Assignments 2024 citations by CoLab: 0
1H, 15N and 13C backbone resonance assignment of the N-terminal region of Zika virus NS4B protein in detergent micelles
Li Y., Loh Y.R., Li Q., Luo D., Kang C.
Q3
Springer Nature
Biomolecular NMR Assignments 2024 citations by CoLab: 0
Backbone 1H, 15N, and 13C resonance assignments of the FF1 domain from P190A RhoGAP in 5 and 8 M urea
Camilo-Ramos A., Korzhnev D.M., Pinheiro-Aguiar R., Almeida F.C.
Q3
Springer Nature
Biomolecular NMR Assignments 2024 citations by CoLab: 0

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India, 1679, 67.87%
Brazil, 71, 2.87%
USA, 64, 2.59%
Iran, 63, 2.55%
United Kingdom, 59, 2.38%
Italy, 53, 2.14%
Japan, 51, 2.06%
Turkey, 45, 1.82%
Germany, 38, 1.54%
Spain, 28, 1.13%
Egypt, 26, 1.05%
Nigeria, 25, 1.01%
China, 18, 0.73%
Saudi Arabia, 18, 0.73%
Mexico, 16, 0.65%
Australia, 13, 0.53%
Lebanon, 12, 0.49%
Greece, 11, 0.44%
Malaysia, 11, 0.44%
Nepal, 11, 0.44%
South Africa, 11, 0.44%
France, 10, 0.4%
Iraq, 8, 0.32%
Colombia, 8, 0.32%
Switzerland, 8, 0.32%
Ireland, 7, 0.28%
Syria, 6, 0.24%
Sudan, 6, 0.24%
Belgium, 5, 0.2%
Netherlands, 5, 0.2%
UAE, 5, 0.2%
Thailand, 5, 0.2%
Sweden, 5, 0.2%
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Ukraine, 2, 0.08%
Portugal, 2, 0.08%
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Kuwait, 2, 0.08%
Libya, 2, 0.08%
Poland, 2, 0.08%
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Estonia, 1, 0.04%
Argentina, 1, 0.04%
Bhutan, 1, 0.04%
Hungary, 1, 0.04%
Venezuela, 1, 0.04%
Ghana, 1, 0.04%
Jordan, 1, 0.04%
Canada, 1, 0.04%
Mozambique, 1, 0.04%
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India, 644, 58.65%
Brazil, 44, 4.01%
Iran, 38, 3.46%
USA, 29, 2.64%
United Kingdom, 28, 2.55%
Italy, 27, 2.46%
Japan, 19, 1.73%
Germany, 17, 1.55%
Turkey, 17, 1.55%
Egypt, 16, 1.46%
Spain, 11, 1%
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Colombia, 6, 0.55%
Saudi Arabia, 6, 0.55%
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Portugal, 1, 0.09%
Argentina, 1, 0.09%
Bhutan, 1, 0.09%
Hungary, 1, 0.09%
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Iraq, 1, 0.09%
Ireland, 1, 0.09%
Kuwait, 1, 0.09%
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Poland, 1, 0.09%
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