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1846 1
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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 39559
1974 43264
1975 44408
1976 44423
1977 45841
1978 47330
1979 51471
1980 54651
1981 56720
1982 61146
1983 65736
1984 70824
1985 76011
1986 79984
1987 83637
1988 89975
1989 97493
1990 105074
1991 109519
1992 114928
1993 119995
1994 126772
1995 132253
1996 135018
1997 139424
1998 146636
1999 151997
2000 161968
2001 168365
2002 174607
2003 184986
2004 198931
2005 214181
2006 228955
2007 238854
2008 248553
2009 256451
2010 272409
2011 287995
2012 300978
2013 310637
2014 315429
2015 317857
2016 312787
2017 311566
2018 315151
2019 323633
2020 347388
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2024 326313
2025 129101
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8,824,810 results

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Proteins: molecules defined by their trade-offs.
Bigman LS, Levy Y. Bigman LS, et al. Curr Opin Struct Biol. 2020 Feb;60:50-56. doi: 10.1016/j.sbi.2019.11.005. Epub 2019 Dec 7. Curr Opin Struct Biol. 2020. PMID: 31816559 Review.
Proteins are subject to various conflicting forces that trade-off against each other. For example, during folding, the protein achieves lower enthalpy at the cost of lower entropy. ...Furthermore, attaining increased stability may reduce a protein's ab …
Proteins are subject to various conflicting forces that trade-off against each other. For example, during folding, the protein …
The Ubiquitin-like Proteins of Saccharomyces cerevisiae.
Sengupta S, Pick E. Sengupta S, et al. Biomolecules. 2023 Apr 24;13(5):734. doi: 10.3390/biom13050734. Biomolecules. 2023. PMID: 37238603 Free PMC article. Review.
In this review, we present a comprehensive list of the ubiquitin-like modifiers (Ubls) of Saccharomyces cerevisiae, a common model organism used to study fundamental cellular processes that are conserved in complex multicellular organisms, such as humans. Ubls are a family of …
In this review, we present a comprehensive list of the ubiquitin-like modifiers (Ubls) of Saccharomyces cerevisiae, a common model organism …
The physiology of protein S-acylation.
Chamberlain LH, Shipston MJ. Chamberlain LH, et al. Physiol Rev. 2015 Apr;95(2):341-76. doi: 10.1152/physrev.00032.2014. Physiol Rev. 2015. PMID: 25834228 Free PMC article. Review.
Protein S-acylation, the only fully reversible posttranslational lipid modification of proteins, is emerging as a ubiquitous mechanism to control the properties and function of a diverse array of proteins and consequently physiological processes. ...Th …
Protein S-acylation, the only fully reversible posttranslational lipid modification of proteins, is emerging as a ubiqu …
Functional Proteins from Short Peptides: Dayhoff's Hypothesis Turns 50.
Romero Romero ML, Rabin A, Tawfik DS. Romero Romero ML, et al. Angew Chem Int Ed Engl. 2016 Dec 23;55(52):15966-15971. doi: 10.1002/anie.201609977. Epub 2016 Nov 16. Angew Chem Int Ed Engl. 2016. PMID: 27865046 Review.
First and foremost: Margaret Dayhoff's 1966 hypothesis on the origin of proteins is now an accepted model for the emergence of large, globular, functional proteins from short, simple peptides. However, the fundamental question of how the first protein(s …
First and foremost: Margaret Dayhoff's 1966 hypothesis on the origin of proteins is now an accepted model for the emergence of large, …
Mechanisms and functions of protein S-acylation.
S Mesquita F, Abrami L, Linder ME, Bamji SX, Dickinson BC, van der Goot FG. S Mesquita F, et al. Nat Rev Mol Cell Biol. 2024 Jun;25(6):488-509. doi: 10.1038/s41580-024-00700-8. Epub 2024 Feb 14. Nat Rev Mol Cell Biol. 2024. PMID: 38355760 Review.
Over the past two decades, protein S-acylation (often referred to as S-palmitoylation) has emerged as an important regulator of vital signalling pathways. S-Acylation is a reversible post-translational modification that involves the attachment of a fatty acid to a …
Over the past two decades, protein S-acylation (often referred to as S-palmitoylation) has emerged as an important regulator o …
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 …
Transport of proteins across the endoplasmic reticulum membrane.
Rapoport TA. Rapoport TA. Science. 1992 Nov 6;258(5084):931-6. doi: 10.1126/science.1332192. Science. 1992. PMID: 1332192 Review.
The biosynthesis of many eukaryotic proteins requires their transport across the endoplasmic reticulum (ER) membrane. The process can be divided into two phases: (i) a targeting cycle, during which, by virtue of their signal sequences, nascent polypeptides are directed to …
The biosynthesis of many eukaryotic proteins requires their transport across the endoplasmic reticulum (ER) membrane. The process can …
Fluctuations within folded proteins: implications for thermodynamic and allosteric regulation.
DuBay KH, Bowman GR, Geissler PL. DuBay KH, et al. Acc Chem Res. 2015 Apr 21;48(4):1098-105. doi: 10.1021/ar500351b. Epub 2015 Feb 17. Acc Chem Res. 2015. PMID: 25688669 Review.
Folded protein structures are both stable and dynamic. Historically, our clearest window into these structures came from X-ray crystallography, which generally provided a static image of each protein's singular "folded state", highlighting its stability. ...H …
Folded protein structures are both stable and dynamic. Historically, our clearest window into these structures came from X-ray crysta …
Mass spectrometry and the search for moonlighting proteins.
Jeffery CJ. Jeffery CJ. Mass Spectrom Rev. 2005 Nov-Dec;24(6):772-82. doi: 10.1002/mas.20041. Mass Spectrom Rev. 2005. PMID: 15605385 Review.
Mass spectrometry has become one of the most important techniques in proteomics because of its use to identify the proteins found in different cell types, organelles, and multiprotein complexes. This information about protein location and binding partners can provid …
Mass spectrometry has become one of the most important techniques in proteomics because of its use to identify the proteins found in …
Biogenesis of mitochondrial inner membrane proteins.
Tokatlidis K, Schatz G. Tokatlidis K, et al. J Biol Chem. 1999 Dec 10;274(50):35285-8. doi: 10.1074/jbc.274.50.35285. J Biol Chem. 1999. PMID: 10585389 Free article. Review. No abstract available.
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