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

Year Number of Results
1929 2
1938 1
1939 1
1940 1
1942 3
1943 1
1946 1
1948 2
1949 1
1950 2
1951 4
1952 4
1953 2
1954 3
1955 3
1956 1
1957 2
1959 3
1960 1
1961 1
1962 1
1963 3
1964 4
1965 4
1966 9
1968 5
1969 6
1970 3
1971 5
1972 11
1973 6
1974 6
1975 15
1976 8
1977 15
1978 7
1979 15
1980 16
1981 14
1982 18
1983 17
1984 25
1985 25
1986 33
1987 410
1988 911
1989 1104
1990 1166
1991 1287
1992 1304
1993 1330
1994 1470
1995 1500
1996 1518
1997 1498
1998 1605
1999 1579
2000 1567
2001 1741
2002 1767
2003 1779
2004 1866
2005 1899
2006 2063
2007 2062
2008 2196
2009 2100
2010 2309
2011 2365
2012 2267
2013 2570
2014 3593
2015 4039
2016 4176
2017 4177
2018 4092
2019 4159
2020 4065
2021 4064
2022 3649
2023 3495
2024 1373

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78,471 results

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Page 1
Bridged Proteolysis Targeting Chimera (PROTAC) Enables Degradation of Undruggable Targets.
Xiong Y, Zhong Y, Yim H, Yang X, Park KS, Xie L, Poulikakos PI, Han X, Xiong Y, Chen X, Liu J, Jin J. Xiong Y, et al. J Am Chem Soc. 2022 Dec 14;144(49):22622-22632. doi: 10.1021/jacs.2c09255. Epub 2022 Nov 30. J Am Chem Soc. 2022. PMID: 36448571 Free PMC article.
Proteolysis Targeting Chimeras (PROTACs) are attractive therapeutic modalities for degrading disease-causing proteins. While many PROTACs have been developed for numerous protein targets, current small-molecule PROTAC approaches cannot target undruggable proteins
Proteolysis Targeting Chimeras (PROTACs) are attractive therapeutic modalities for degrading disease-causing proteins. While many PRO …
Protein S-nitrosylation: purview and parameters.
Hess DT, Matsumoto A, Kim SO, Marshall HE, Stamler JS. Hess DT, et al. Nat Rev Mol Cell Biol. 2005 Feb;6(2):150-66. doi: 10.1038/nrm1569. Nat Rev Mol Cell Biol. 2005. PMID: 15688001 Review.
S-nitrosylation, the covalent attachment of a nitrogen monoxide group to the thiol side chain of cysteine, has emerged as an important mechanism for dynamic, post-translational regulation of most or all main classes of protein. S-nitrosylation thereby conveys a larg …
S-nitrosylation, the covalent attachment of a nitrogen monoxide group to the thiol side chain of cysteine, has emerged as an important mecha …
Ni-NTA Affinity Chromatography to Characterize Protein-Protein Interactions During Fe-S Cluster Biogenesis.
Carter TD, Outten FW. Carter TD, et al. Methods Mol Biol. 2021;2353:125-136. doi: 10.1007/978-1-0716-1605-5_7. Methods Mol Biol. 2021. PMID: 34292547 Free PMC article.
Affinity chromatography can be repurposed to provide useful information about the specific partner protein(s) to which a protein of interest may bind as well as the relative binding affinity of that partner protein for the protein of interest. H …
Affinity chromatography can be repurposed to provide useful information about the specific partner protein(s) to which a pr
Antithrombin III, protein C, and protein S. Naturally occurring anticoagulant proteins.
High KA. High KA. Arch Pathol Lab Med. 1988 Jan;112(1):28-36. Arch Pathol Lab Med. 1988. PMID: 2962557 Review.
Protein C, protein S, and antithrombin III are naturally occurring anticoagulant proteins. Activated protein C and protein S act by inhibiting the action of the cofactors factor Va and factor VIIIa. ...
Protein C, protein S, and antithrombin III are naturally occurring anticoagulant proteins. Activated protein
Dbl family proteins.
Whitehead IP, Campbell S, Rossman KL, Der CJ. Whitehead IP, et al. Biochim Biophys Acta. 1997 Feb 22;1332(1):F1-23. doi: 10.1016/s0304-419x(96)00040-6. Biochim Biophys Acta. 1997. PMID: 9061011 Review. No abstract available.
Recent insights into the biological functions of liver fatty acid binding protein 1.
Wang G, Bonkovsky HL, de Lemos A, Burczynski FJ. Wang G, et al. J Lipid Res. 2015 Dec;56(12):2238-47. doi: 10.1194/jlr.R056705. Epub 2015 Oct 6. J Lipid Res. 2015. PMID: 26443794 Free PMC article. Review.
Over four decades have passed since liver fatty acid binding protein (FABP)1 was first isolated. There are few protein families for which most of the complete tertiary structures, binding properties, and tissue occurrences are described in such detail and yet new fu …
Over four decades have passed since liver fatty acid binding protein (FABP)1 was first isolated. There are few protein familie …
Physicochemical code for quinary protein interactions in Escherichia coli.
Mu X, Choi S, Lang L, Mowray D, Dokholyan NV, Danielsson J, Oliveberg M. Mu X, et al. Proc Natl Acad Sci U S A. 2017 Jun 6;114(23):E4556-E4563. doi: 10.1073/pnas.1621227114. Epub 2017 May 23. Proc Natl Acad Sci U S A. 2017. PMID: 28536196 Free PMC article.
How proteins sense and navigate the cellular interior to find their functional partners remains poorly understood. ...Even so, the in-cell motions respond predictably to surface mutation, allowing us to tune and intermix the protein's behavior at will. The fi …
How proteins sense and navigate the cellular interior to find their functional partners remains poorly understood. ...Even so, the in …
Double-stranded RNA drives SARS-CoV-2 nucleocapsid protein to undergo phase separation at specific temperatures.
Roden CA, Dai Y, Giannetti CA, Seim I, Lee M, Sealfon R, McLaughlin GA, Boerneke MA, Iserman C, Wey SA, Ekena JL, Troyanskaya OG, Weeks KM, You L, Chilkoti A, Gladfelter AS. Roden CA, et al. Nucleic Acids Res. 2022 Aug 12;50(14):8168-8192. doi: 10.1093/nar/gkac596. Nucleic Acids Res. 2022. PMID: 35871289 Free PMC article.
Nucleocapsid protein (N-protein) is required for multiple steps in betacoronaviruses replication. ...We identify two separate and distinct double-stranded, RNA motifs (dsRNA stickers) that promote N-protein condensation. These dsRNA stickers are separately re …
Nucleocapsid protein (N-protein) is required for multiple steps in betacoronaviruses replication. ...We identify two separate …
Dynamical spectroscopy and microscopy of proteins in cells.
Gruebele M, Pielak GJ. Gruebele M, et al. Curr Opin Struct Biol. 2021 Oct;70:1-7. doi: 10.1016/j.sbi.2021.02.001. Epub 2021 Mar 1. Curr Opin Struct Biol. 2021. PMID: 33662744 Review.
With a strong understanding of how proteins fold in hand, it is now possible to ask how in-cell environments modulate their folding, binding and function. ...Here, we discuss this recent work and the emerging picture of protein surfaces as not just hydrophilic coats …
With a strong understanding of how proteins fold in hand, it is now possible to ask how in-cell environments modulate their folding, …
Protein dynamics in living cells.
Bryant JE, Lecomte JT, Lee AL, Young GB, Pielak GJ. Bryant JE, et al. Biochemistry. 2005 Jul 5;44(26):9275-9. doi: 10.1021/bi050786j. Biochemistry. 2005. PMID: 15981993 Retracted.
A protein's structure is most often used to explain its function, but function also depends on dynamics. To date, protein dynamics have been studied only in vitro under dilute solution conditions where solute concentrations are typically less than 10 g/L, yet …
A protein's structure is most often used to explain its function, but function also depends on dynamics. To date, protein
78,471 results
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