Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
1.5field-weighted citation impact, top 21% of its field
1 · What the graph read from it
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
2 · The registry
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
3 · Its place in the literature
Who cites it
1 citing paper in PubMed, 7 citations in OpenAlex.
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
5 · Who and what money
Authors and funding
17 authors at 8 institutions in 3 countries.
Alexander G BobylevInstitute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, 142290 Moscow Region, Russia.ORCID 0000-0002-9477-1214
Elmira I YakupovaA.N. Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991 Moscow Region, Russia.
Liya G BobylevaInstitute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, 142290 Moscow Region, Russia.
Nikolay V MolochkovInstitute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, 142290 Moscow Region, Russia.
Alexander A TimchenkoInstitute of Protein Research, Russian Academy of Sciences, Pushchino, 142290 Moscow Region, Russia.
Maria A TimchenkoInstitute for Biological Instrumentation, Federal Research Center, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, Pushchino, 142290 Moscow Region, Russia.ORCID 0000-0003-2547-8804
Hiroshi KiharaDepartment of Early Childhood Education, Himeji-Hinomoto College, 890 Koro, Kodera-cho, Himeji 679-2151, Japan.
Alexey D NikulinInstitute of Protein Research, Russian Academy of Sciences, Pushchino, 142290 Moscow Region, Russia.
Azat G GabdulkhakovInstitute of Protein Research, Russian Academy of Sciences, Pushchino, 142290 Moscow Region, Russia.ORCID 0000-0003-1016-5936
Tatiana N MelnikInstitute of Protein Research, Russian Academy of Sciences, Pushchino, 142290 Moscow Region, Russia.ORCID 0000-0002-9081-4678
Nikita V PenkovInstitute of Cell Biophysics, FRC PSCBR, Russian Academy of Sciences, Pushchino, 142290 Moscow Region, Russia.ORCID 0000-0003-2212-5640
Michail Y LobanovInstitute of Protein Research, Russian Academy of Sciences, Pushchino, 142290 Moscow Region, Russia.
Alexey S KazakovInstitute for Biological Instrumentation, Federal Research Center, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, Pushchino, 142290 Moscow Region, Russia.
Miklós KellermayerDepartment of Biophysics and Radiation Biology, Semmelweis University, 1085 Budapest, Hungary.ORCID 0000-0002-5553-6553
Zsolt MártonfalviDepartment of Biophysics and Radiation Biology, Semmelweis University, 1085 Budapest, Hungary.ORCID 0000-0001-7820-8109
Oxana V GalzitskayaInstitute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, 142290 Moscow Region, Russia.ORCID 0000-0002-3962-1520
Ivan M VikhlyantsevInstitute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, 142290 Moscow Region, Russia.ORCID 0000-0001-6063-6789
Institute of Protein Research · RUInstitute of Theoretical and Experimental Biophysics · RUInstitute for Biological Instrumentation · RUSemmelweis University · HUHimeji Hinomoto College · JPInstitute of Cell Biophysics · RUKazan Federal University · RULomonosov Moscow State University · RU
Funding
National Research, Development and Innovation Office K135360 to M.K.Russian Science Foundation 22-24-00805
6 · The paper itself
Abstract
A giant multidomain protein of striated and smooth vertebrate muscles, titin, consists of tandems of immunoglobulin (Ig)- and fibronectin type III (FnIII)-like domains representing β-sandwiches, as well as of disordered segments. Chicken smooth muscles express several titin isoforms of ~500-1500 kDa. Using various structural-analysis methods, we investigated in vitro nonspecific amyloid aggregation of the high-molecular-weight isoform of chicken smooth-muscle titin (SMT
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.
Nonspecific Amyloid Aggregation of Chicken Smooth-Muscle Titin: In Vitro Investigations. · full record | OpenQuestion