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

Year Number of Results
1917 1
1918 1
1938 2
1943 1
1944 1
1945 30
1946 107
1947 148
1948 153
1949 150
1950 210
1951 306
1952 392
1953 424
1954 442
1955 441
1956 439
1957 504
1958 524
1959 690
1960 866
1961 878
1962 1053
1963 1636
1964 2183
1965 1850
1966 2058
1967 2513
1968 3075
1969 3435
1970 3544
1971 4115
1972 4550
1973 4728
1974 5145
1975 4822
1976 4749
1977 4543
1978 4376
1979 4996
1980 5158
1981 5098
1982 5404
1983 5798
1984 6175
1985 6671
1986 6975
1987 6653
1988 7014
1989 7442
1990 7758
1991 8290
1992 8429
1993 8353
1994 8893
1995 9203
1996 9378
1997 9846
1998 10383
1999 11044
2000 12436
2001 13130
2002 13847
2003 15246
2004 15840
2005 16773
2006 17852
2007 18595
2008 19214
2009 19464
2010 20342
2011 21027
2012 22093
2013 22237
2014 21588
2015 21384
2016 20372
2017 19577
2018 18488
2019 18078
2020 20001
2021 18934
2022 18807
2023 15633
2024 6782

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620,421 results

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Page 1
Editorial: Lysosomal peptidases in tumor immunity.
Perišić Nanut M, Božić Nedeljković B, Jewett A. Perišić Nanut M, et al. Front Immunol. 2023 Mar 14;14:1176736. doi: 10.3389/fimmu.2023.1176736. eCollection 2023. Front Immunol. 2023. PMID: 36999043 Free PMC article. No abstract available.
Structure and function of prodrug-activating peptidases.
Velilla JA, Kenney GE, Gaudet R. Velilla JA, et al. Biochimie. 2023 Feb;205:124-135. doi: 10.1016/j.biochi.2022.07.019. Epub 2022 Nov 8. Biochimie. 2023. PMID: 36803695 Free PMC article. Review.
In one resistance mechanism, bacteria assemble a non-toxic precursor on an N-acyl-d-asparagine prodrug motif in the cytoplasm, then export it to the periplasm where a dedicated d-amino peptidase hydrolyzes the prodrug motif. These prodrug-activating peptidases conta …
In one resistance mechanism, bacteria assemble a non-toxic precursor on an N-acyl-d-asparagine prodrug motif in the cytoplasm, then export i …
Cell-surface peptidases.
Mentlein R. Mentlein R. Int Rev Cytol. 2004;235:165-213. doi: 10.1016/S0074-7696(04)35004-7. Int Rev Cytol. 2004. PMID: 15219783 Free PMC article. Review.
Furthermore, nonenzymatic (binding) functions and participation in intracellular signal transduction of cell surfaces peptidases are described. An overview on the different cell-surface peptidases is given, and their divergent functions are explained in detail. An e …
Furthermore, nonenzymatic (binding) functions and participation in intracellular signal transduction of cell surfaces peptidases are …
The peptidases involved in plant mitochondrial protein import.
Ghifari AS, Huang S, Murcha MW. Ghifari AS, et al. J Exp Bot. 2019 Nov 18;70(21):6005-6018. doi: 10.1093/jxb/erz365. J Exp Bot. 2019. PMID: 31738432 Review.
Research over the last few decades has elucidated a range of mitochondrial peptidases that are involved in the initial removal of the targeting signal and its sequential degradation, allowing for the recovery of single amino acids. ...Here, we review the multitude of plant …
Research over the last few decades has elucidated a range of mitochondrial peptidases that are involved in the initial removal of the …
Bacterial peptidases.
Potempa J, Pike RN. Potempa J, et al. Contrib Microbiol. 2005;12:132-180. doi: 10.1159/000081693. Contrib Microbiol. 2005. PMID: 15496780 Review. No abstract available.
Human proline specific peptidases: A comprehensive analysis.
Dunaevsky YE, Tereshchenkova VF, Oppert B, Belozersky MA, Filippova IY, Elpidina EN. Dunaevsky YE, et al. Biochim Biophys Acta Gen Subj. 2020 Sep;1864(9):129636. doi: 10.1016/j.bbagen.2020.129636. Epub 2020 May 17. Biochim Biophys Acta Gen Subj. 2020. PMID: 32433934 Review.
BACKGROUND: Proline specific peptidases (PSPs) are a unique group of enzymes that specifically cleave bonds formed by a proline residue. The study of PSPs is important due to their role in the maturation and degradation of peptide hormones and neuropeptides. In addi …
BACKGROUND: Proline specific peptidases (PSPs) are a unique group of enzymes that specifically cleave bonds formed by a proline resid …
Origins of peptidases.
Rawlings ND, Bateman A. Rawlings ND, et al. Biochimie. 2019 Nov;166:4-18. doi: 10.1016/j.biochi.2019.07.026. Epub 2019 Aug 1. Biochimie. 2019. PMID: 31377195 Free PMC article.
No family was found to be ubiquitous and even peptidases thought to be essential for life, such as signal peptidase and methionyl aminopeptides are missing from some clades. ...These include peptidases with different catalytic types, exo- and endopeptidases, …
No family was found to be ubiquitous and even peptidases thought to be essential for life, such as signal peptidase and methio …
Peptidases: Role and Function in Health and Disease.
Kos J. Kos J. Int J Mol Sci. 2023 Apr 25;24(9):7823. doi: 10.3390/ijms24097823. Int J Mol Sci. 2023. PMID: 37175526 Free PMC article.
Peptidases represent a large family of hydrolases present in all living organisms, which catalyze the degradation of peptide bonds in different biological processes....
Peptidases represent a large family of hydrolases present in all living organisms, which catalyze the degradation of peptid …
'Species' of peptidases.
Barrett AJ, Rawlings ND. Barrett AJ, et al. Biol Chem. 2007 Nov;388(11):1151-7. doi: 10.1515/BC.2007.151. Biol Chem. 2007. PMID: 17976007 Review.
A good system for the naming and classification of peptidases can contribute much to the study of these enzymes. Having already described the building of families and clans in the MEROPS system, we here focus on the lowest level in the hierarchy, in which the huge number o …
A good system for the naming and classification of peptidases can contribute much to the study of these enzymes. Having already descr …
Mitochondrial Processing Peptidases-Structure, Function and the Role in Human Diseases.
Kunová N, Havalová H, Ondrovičová G, Stojkovičová B, Bauer JA, Bauerová-Hlinková V, Pevala V, Kutejová E. Kunová N, et al. Int J Mol Sci. 2022 Jan 24;23(3):1297. doi: 10.3390/ijms23031297. Int J Mol Sci. 2022. PMID: 35163221 Free PMC article. Review.
In the mitochondria, the presequences are removed by several processing peptidases, including the mitochondrial processing peptidase (MPP), the inner membrane processing peptidase (IMP), the inter-membrane processing peptidase (MIP), and the mitochondr …
In the mitochondria, the presequences are removed by several processing peptidases, including the mitochondrial processing peptida …
620,421 results
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