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

Year Number of Results
1846 1
1897 1
1898 1
1899 1
1903 1
1906 2
1907 6
1908 6
1909 7
1910 8
1911 19
1912 15
1913 24
1914 18
1915 17
1916 14
1917 24
1918 16
1919 24
1920 28
1921 25
1922 42
1923 36
1924 40
1925 45
1926 43
1927 50
1928 47
1929 37
1930 56
1931 56
1932 70
1933 58
1934 50
1935 64
1936 54
1937 60
1938 63
1939 62
1940 59
1941 63
1942 61
1943 56
1944 59
1945 466
1946 1397
1947 1697
1948 1960
1949 1740
1950 3120
1951 4077
1952 4513
1953 4850
1954 5428
1955 5785
1956 5482
1957 5780
1958 5990
1959 6012
1960 6271
1961 7173
1962 8195
1963 12731
1964 17369
1965 14731
1966 15425
1967 19497
1968 23789
1969 27405
1970 28594
1971 33382
1972 37014
1973 39560
1974 43264
1975 44408
1976 44423
1977 45841
1978 47330
1979 51470
1980 54651
1981 56722
1982 61148
1983 65739
1984 70827
1985 76011
1986 79985
1987 83637
1988 89977
1989 97494
1990 105079
1991 109545
1992 114952
1993 120014
1994 126815
1995 132286
1996 135044
1997 139456
1998 146680
1999 152021
2000 161994
2001 168391
2002 174631
2003 185023
2004 198974
2005 214196
2006 228940
2007 238876
2008 248578
2009 256485
2010 272440
2011 288037
2012 301024
2013 310674
2014 315474
2015 317934
2016 312857
2017 311646
2018 315261
2019 323723
2020 347330
2021 352110
2022 335769
2023 301801
2024 59857

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8,462,596 results

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Page 1
Mitochondria-targeting sequence, a multi-role sorting sequence recognized at all steps of protein import into mitochondria.
Omura T. Omura T. J Biochem. 1998 Jun;123(6):1010-6. doi: 10.1093/oxfordjournals.jbchem.a022036. J Biochem. 1998. PMID: 9603986 Free article. Review.
MTS is required, however, not only for targeting newly synthesized preproteins to mitochondria, but also for all the following steps along the mitochondrial protein import pathway. MTS of nascent preproteins is first recognized by a cytoplasmic molecular chaperone, MSF, an …
MTS is required, however, not only for targeting newly synthesized preproteins to mitochondria, but also for all the following steps along t …
Protein S is a cofactor for tissue factor pathway inhibitor.
Rosing J, Maurissen LF, Tchaikovski SN, Tans G, Hackeng TM. Rosing J, et al. Thromb Res. 2008;122 Suppl 1:S60-3. doi: 10.1016/S0049-3848(08)70021-5. Thromb Res. 2008. PMID: 18691502 Review.
Protein S is a vitamin K-dependent protein that acts as a cofactor of the anticoagulant protein APC. However, protein S also exhibits anticoagulant activity in the absence of APC. ...
Protein S is a vitamin K-dependent protein that acts as a cofactor of the anticoagulant protein APC. However,
Activated protein C anticoagulant system dysfunction and thrombophilia in Asia.
Hamasaki N, Kuma H, Tsuda H. Hamasaki N, et al. Ann Lab Med. 2013 Jan;33(1):8-13. doi: 10.3343/alm.2013.33.1.8. Epub 2012 Dec 17. Ann Lab Med. 2013. PMID: 23301217 Free PMC article. Review.
Approximately 50% of Japanese and Chinese individuals who develop venous thrombosis have reduced activities of protein S. The abnormal sites causing the protein S molecule abnormalities are distributed throughout the protein S gene, PROS1 …
Approximately 50% of Japanese and Chinese individuals who develop venous thrombosis have reduced activities of protein S. The …
Protein S and thrombotic disease.
Walker FJ. Walker FJ. Proc Soc Exp Biol Med. 1992 Jul;200(3):285-95. doi: 10.3181/00379727-200-43435. Proc Soc Exp Biol Med. 1992. PMID: 1535444 Review. No abstract available.
Protein degradation: recognition of ubiquitinylated substrates.
Hartmann-Petersen R, Gordon C. Hartmann-Petersen R, et al. Curr Biol. 2004 Sep 21;14(18):R754-6. doi: 10.1016/j.cub.2004.09.012. Curr Biol. 2004. PMID: 15380085 Free article. Review.
A cell-free system has been developed in budding yeast that provides direct evidence that the Dsk2/Dph1, Rad23/Rhp23 and Rpn10/Pus1 multi-ubiquitin-binding proteins, long implicated in substrate recognition and presentation to the 26S proteasome, actually fulfil such a rol …
A cell-free system has been developed in budding yeast that provides direct evidence that the Dsk2/Dph1, Rad23/Rhp23 and Rpn10/Pus1 multi-ub …
8-Nitro-cGMP: A Novel Protein-Reactive cNMP and Its Emerging Roles in Autophagy.
Arimoto H, Takahashi D. Arimoto H, et al. Handb Exp Pharmacol. 2017;238:253-268. doi: 10.1007/164_2016_5000. Handb Exp Pharmacol. 2017. PMID: 28213625 Review.
The characteristic chemical feature of 8-nitro-cGMP is its ability to modify proteinous cysteine residues via a stable sulfide bond. In this posttranslational modification, the nitro group is detached from the guanine base. This modification, termed "protein S
The characteristic chemical feature of 8-nitro-cGMP is its ability to modify proteinous cysteine residues via a stable sulfide bond. …
Protein S and C4b-binding protein: components involved in the regulation of the protein C anticoagulant system.
Dahlbäck B. Dahlbäck B. Thromb Haemost. 1991 Jul 12;66(1):49-61. Thromb Haemost. 1991. PMID: 1833851 Review.
Protein S is a cofactor in these reactions. It is a vitamin K-dependent protein with multiple domains. ...As C4BP lacking the beta-chain is unable to bind protein S, the beta-chain is required for protein S binding, but not for the
Protein S is a cofactor in these reactions. It is a vitamin K-dependent protein with multiple domains. ...As C4BP lacki
Protein and lipid sorting between the endoplasmic reticulum and the Golgi complex.
Nickel W, Brügger B, Wieland FT. Nickel W, et al. Semin Cell Dev Biol. 1998 Oct;9(5):493-501. doi: 10.1006/scdb.1998.0256. Semin Cell Dev Biol. 1998. PMID: 9835636 Review.
While COPII-coated vesicles appear to be involved exclusively in the export of secretory proteins and lipids from the endoplasmic reticulum (ER), COPI-coated vesicles seem to function in both anterograde and retrograde transport between the ER-Golgi intermediate compartmen …
While COPII-coated vesicles appear to be involved exclusively in the export of secretory proteins and lipids from the endoplasmic ret …
The protein-only theory and the yeast Saccharomyces cerevisiae: the prions and the propagons.
Fernandez-Bellot E, Cullin C. Fernandez-Bellot E, et al. Cell Mol Life Sci. 2001 Nov;58(12-13):1857-78. doi: 10.1007/PL00000823. Cell Mol Life Sci. 2001. PMID: 11766884 Review.
The more extensively studied yeast prion [PSI] leads to a propagation model that links auto-aggregation in amyloid formation and inactivation of the cellular function of the yeast 'prion protein' Sup35p. The other prion model, [URE3], appears to be similar in some genetic …
The more extensively studied yeast prion [PSI] leads to a propagation model that links auto-aggregation in amyloid formation and inactivatio …
[Protein C, protein S, protein Z].
Hamada Y, Hayashi T, Suzuki K. Hamada Y, et al. Nihon Rinsho. 2004 Dec;62 Suppl 12:681-6. Nihon Rinsho. 2004. PMID: 15658423 Review. Japanese. No abstract available.
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