Histidine Kinase
"Histidine Kinase" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A member of the transferase superfamily of proteins. In the activated state, protein-histidine kinase autophosphorylates at a histidine residue, subsequently transferring high-energy phosphoryl groups to an aspartate residue of the response-regulator domain, which results in a conformational shift in the effector domain. Histidine kinases mediate signal transduction in a wide range of processes involving cellular adaptation to environmental stress.
Descriptor ID |
D000071677
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MeSH Number(s) |
D08.811.913.696.620.682.675
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Concept/Terms |
Histidine Kinase- Histidine Kinase
- Kinase, Histidine
- Histidine Protein Kinase
- Kinase, Histidine Protein
- Protein Kinase, Histidine
- Protein-Histidine Kinase
- Kinase, Protein-Histidine
- Protein Histidine Kinase
Protein Histidine Pros-Kinase- Protein Histidine Pros-Kinase
- Histidine Pros-Kinase, Protein
- Pros-Kinase, Protein Histidine
- Protein Histidine Pros Kinase
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Below are MeSH descriptors whose meaning is more general than "Histidine Kinase".
Below are MeSH descriptors whose meaning is more specific than "Histidine Kinase".
This graph shows the total number of publications written about "Histidine Kinase" by people in this website by year, and whether "Histidine Kinase" was a major or minor topic of these publications.
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Year | Major Topic | Minor Topic | Total |
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1995 | 0 | 1 | 1 | 1996 | 0 | 1 | 1 | 1997 | 0 | 1 | 1 | 1998 | 0 | 1 | 1 | 1999 | 0 | 1 | 1 | 2000 | 0 | 1 | 1 | 2003 | 0 | 1 | 1 | 2005 | 0 | 3 | 3 | 2006 | 0 | 1 | 1 | 2008 | 0 | 1 | 1 | 2009 | 0 | 2 | 2 | 2010 | 0 | 2 | 2 | 2011 | 0 | 1 | 1 | 2012 | 0 | 1 | 1 | 2013 | 0 | 2 | 2 | 2014 | 0 | 3 | 3 | 2015 | 0 | 2 | 2 | 2016 | 2 | 0 | 2 | 2019 | 1 | 0 | 1 | 2020 | 1 | 0 | 1 |
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Below are the most recent publications written about "Histidine Kinase" by people in Profiles.
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Zuniga EG, Figueroa NM, Gonzalez A, Pantoja AP, Risser DD. The Hybrid Histidine Kinase HrmK Is an Early-Acting Factor in the Hormogonium Gene Regulatory Network. J Bacteriol. 2020 02 11; 202(5).
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Affandi T, McEvoy MM. Mechanism of metal ion-induced activation of a two-component sensor kinase. Biochem J. 2019 01 15; 476(1):115-135.
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Andrews FH, Tong Q, Sullivan KD, Cornett EM, Zhang Y, Ali M, Ahn J, Pandey A, Guo AH, Strahl BD, Costello JC, Espinosa JM, Rothbart SB, Kutateladze TG. Multivalent Chromatin Engagement and Inter-domain Crosstalk Regulate MORC3 ATPase. Cell Rep. 2016 09 20; 16(12):3195-3207.
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Affandi T, Issaian AV, McEvoy MM. The Structure of the Periplasmic Sensor Domain of the Histidine Kinase CusS Shows Unusual Metal Ion Coordination at the Dimeric Interface. Biochemistry. 2016 09 20; 55(37):5296-306.
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Parkinson JS, Hazelbauer GL, Falke JJ. Signaling and sensory adaptation in Escherichia coli chemoreceptors: 2015 update. Trends Microbiol. 2015 May; 23(5):257-66.
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Gendrin C, Lembo A, Whidbey C, Burnside K, Berry J, Ngo L, Banerjee A, Xue L, Arrington J, Doran KS, Tao WA, Rajagopal L. The sensor histidine kinase RgfC affects group B streptococcal virulence factor expression independent of its response regulator RgfA. Infect Immun. 2015 Mar; 83(3):1078-88.
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Falke JJ. Piston versus scissors: chemotaxis receptors versus sensor His-kinase receptors in two-component signaling pathways. Structure. 2014 Sep 02; 22(9):1219-1220.
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Piasta KN, Falke JJ. Increasing and decreasing the ultrastability of bacterial chemotaxis core signaling complexes by modifying protein-protein contacts. Biochemistry. 2014 Sep 09; 53(35):5592-600.
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Briegel A, Wong ML, Hodges HL, Oikonomou CM, Piasta KN, Harris MJ, Fowler DJ, Thompson LK, Falke JJ, Kiessling LL, Jensen GJ. New insights into bacterial chemoreceptor array structure and assembly from electron cryotomography. Biochemistry. 2014 Mar 18; 53(10):1575-85.
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Piasta KN, Ulliman CJ, Slivka PF, Crane BR, Falke JJ. Defining a key receptor-CheA kinase contact and elucidating its function in the membrane-bound bacterial chemosensory array: a disulfide mapping and TAM-IDS Study. Biochemistry. 2013 Jun 04; 52(22):3866-80.
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