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Table representation of search results timeline featuring number of search results per year.

Year Number of Results
1970 1
1972 2
1974 3
1975 2
1976 6
1977 8
1978 9
1979 19
1980 34
1981 28
1982 35
1983 38
1984 37
1985 52
1986 54
1987 55
1988 62
1989 71
1990 89
1991 90
1992 84
1993 100
1994 144
1995 135
1996 121
1997 121
1998 127
1999 143
2000 112
2001 116
2002 133
2003 145
2004 149
2005 149
2006 135
2007 121
2008 119
2009 118
2010 141
2011 129
2012 147
2013 136
2014 125
2015 110
2016 118
2017 109
2018 109
2019 117
2020 126
2021 103
2022 82
2023 72
2024 76
2025 104
2026 66

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4,500 results

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Page 1
Calcium-dependent reversible coaggregation activity of C-reactive protein and M-ficolin.
Tanio M. Tanio M. Mol Immunol. 2022 Sep;149:157-164. doi: 10.1016/j.molimm.2022.07.001. Epub 2022 Jul 13. Mol Immunol. 2022. PMID: 35841688
In this report, a mixture of CRP and M-ficolin reversibly co-aggregated in a calcium-dependent manner. This coaggregation was enhanced at low pH (6.5) or low salt (35 mM NaCl) concentrations. ...The M-ficolin fibrinogen-like domain (FD1), the ligand-binding d …
In this report, a mixture of CRP and M-ficolin reversibly co-aggregated in a calcium-dependent manner. This coaggregation was …
Membrane-specific and calcium-dependent binding of the Arabidopsis C2 domain protein CaLB revealed by ATR-FTIR spectroscopy.
Maguire S, Scheibe C, Eisgruber T, Mosesso N, Isono E, Hauser K. Maguire S, et al. Spectrochim Acta A Mol Biomol Spectrosc. 2024 Feb 15;307:123629. doi: 10.1016/j.saa.2023.123629. Epub 2023 Nov 8. Spectrochim Acta A Mol Biomol Spectrosc. 2024. PMID: 37995652 Free article.
Membranes were composed of pure POPC lipids or of POPC/PI(3)P lipid mixtures. A significantly increased protein binding affinity was observed with membranes containing 1% PI(3)P indicating the high binding specificity of CaLB for PI(3)P. Furthermore, membrane …
Membranes were composed of pure POPC lipids or of POPC/PI(3)P lipid mixtures. A significantly increased protein binding affini …
Calcium-dependent and -independent interactions of the S100 protein family.
Santamaria-Kisiel L, Rintala-Dempsey AC, Shaw GS. Santamaria-Kisiel L, et al. Biochem J. 2006 Jun 1;396(2):201-14. doi: 10.1042/BJ20060195. Biochem J. 2006. PMID: 16683912 Free PMC article. Review.
More than 90 potential target proteins have been documented for the S100 proteins, including the cytoskeletal proteins tubulin, glial fibrillary acidic protein and F-actin, which have been identified mostly from in vitro experiments. In the last 5 years, efforts have conce …
More than 90 potential target proteins have been documented for the S100 proteins, including the cytoskeletal proteins tubulin, glial fibril …
Design of Calcium-Binding Proteins to Sense Calcium.
Tang S, Deng X, Jiang J, Kirberger M, Yang JJ. Tang S, et al. Molecules. 2020 May 4;25(9):2148. doi: 10.3390/molecules25092148. Molecules. 2020. PMID: 32375353 Free PMC article. Review.
Calcium controls numerous biological processes by interacting with different classes of calcium binding proteins (CaBP's), with different affinities, metal selectivities, kinetics, and calcium dependent conformational changes. ...Next, we report efforts to id …
Calcium controls numerous biological processes by interacting with different classes of calcium binding proteins (CaBP's), with diffe …
Calcium-dependent protein binding to phenothiazine columns.
Moore PB, Dedman JR. Moore PB, et al. J Biol Chem. 1982 Aug 25;257(16):9663-7. J Biol Chem. 1982. PMID: 7107584 Free article.
Nonmuscle, smooth muscle, and striated muscle tissue extracts contain several proteins, in addition to calmodulin, which bind fluphenazine affinity columns in a calcium-dependent manner. Sodium dodecyl sulfate-polyacrylamide gel electrophoretic analysis shows four p …
Nonmuscle, smooth muscle, and striated muscle tissue extracts contain several proteins, in addition to calmodulin, which bind fluphenazine a …
Annexin, a Protein for All Seasons: From Calcium Dependent Membrane Metabolism to RNA Recognition.
Vedeler A, Tartaglia GG, Pastore A. Vedeler A, et al. Bioessays. 2025 Jul;47(7):e70019. doi: 10.1002/bies.70019. Epub 2025 May 12. Bioessays. 2025. PMID: 40350993 Free PMC article. Review.
Annexins are a protein family well known to bind to phospholipids in a calcium-dependent way. They are involved in several different crucial cellular processes such as cell division, calcium signaling, membrane repair, vesicle trafficking, and apoptosis. ...W …
Annexins are a protein family well known to bind to phospholipids in a calcium-dependent way. They are involved in seve …
Calcium-independent binding of human C-reactive protein to lysophosphatidylcholine in supported planar phospholipid monolayers.
Goda T, Miyahara Y. Goda T, et al. Acta Biomater. 2017 Jan 15;48:206-214. doi: 10.1016/j.actbio.2016.10.043. Epub 2016 Nov 1. Acta Biomater. 2017. PMID: 27815167
Surprisingly, CRP binding to supported 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC)/LPC monolayers was calcium-independent although CRP binding to supported POPC monolayers was calcium-dependent. ...Docking analysis predicted a new bindin …
Surprisingly, CRP binding to supported 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC)/LPC monolayers was calcium-independent …
Visinin-like protein (VILIP) is a neuron-specific calcium-dependent double-stranded RNA-binding protein.
Mathisen PM, Johnson JM, Kawczak JA, Tuohy VK. Mathisen PM, et al. J Biol Chem. 1999 Oct 29;274(44):31571-6. doi: 10.1074/jbc.274.44.31571. J Biol Chem. 1999. PMID: 10531361 Free article.
In this study, we have demonstrated that the neuron-specific, calcium-binding protein, visinin-like protein (VILIP) contains one double-stranded RNA-binding domain, a protein motif conserved among many double-stranded RNA-binding proteins …
In this study, we have demonstrated that the neuron-specific, calcium-binding protein, visinin-like protein (VILIP) con …
Role of calcium-binding sites in calcium-dependent membrane association of annexin A4.
Arii Y, Butsusihta K, Fukuoka S. Arii Y, et al. Biosci Biotechnol Biochem. 2015;79(6):978-85. doi: 10.1080/09168451.2014.1003131. Epub 2015 Feb 4. Biosci Biotechnol Biochem. 2015. PMID: 25649809
Annexin A4 (Anx4) is a cytosolic calcium-binding protein with four repeat domains, each containing one calcium-binding site (CBS). The protein interacts with the phospholipid membrane through the CBS-coordinated calcium ion, although the role of each C …
Annexin A4 (Anx4) is a cytosolic calcium-binding protein with four repeat domains, each containing one calcium-binding …
4,500 results