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Filters applied: . Clear all The following term was not found in PubMed: Tanachaichoksirikun
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Did you mean penit tanachaichoksirikun (335 results)?
The PINIT domain of PIAS3: structure-function analysis of its interaction with STAT3.
Mautsa N, Prinsloo E, Bishop ÖT, Blatch GL. Mautsa N, et al. J Mol Recognit. 2011 Sep-Oct;24(5):795-803. doi: 10.1002/jmr.1111. J Mol Recognit. 2011. PMID: 21812053
The conserved proline, isoleucine, asparagine, isoleucine, threonine (PINIT) domain of PIAS3 is thought to promote STAT3-PIAS3 interaction. ...L97A, R99N and R99Q mutations of the PINIT domain were found to abrogate binding to STAT3, suggesting that these residues w …
The conserved proline, isoleucine, asparagine, isoleucine, threonine (PINIT) domain of PIAS3 is thought to promote STAT3-PIAS3 intera …
Duck PIAS2 negatively regulates RIG-I mediated IFN-β production by interacting with IRF7.
Zu S, Xue Q, He Z, Shi C, Wu W, Zhang J, Li W, Huang J, Jiao P, Liao M. Zu S, et al. Dev Comp Immunol. 2020 Jul;108:103664. doi: 10.1016/j.dci.2020.103664. Epub 2020 Mar 6. Dev Comp Immunol. 2020. PMID: 32151676
Here, we cloned duck PIAS (duPIAS), finding PIAS2 could repress IFN-beta production. DuPIAS2 contains SAP-PINIT-RLD-S/T characteristic domains, and its overexpression could inhibit virus-induced IFN-beta promoter activation. ...
Here, we cloned duck PIAS (duPIAS), finding PIAS2 could repress IFN-beta production. DuPIAS2 contains SAP-PINIT-RLD-S/T characteristi …
The 'PINIT' motif, of a newly identified conserved domain of the PIAS protein family, is essential for nuclear retention of PIAS3L.
Duval D, Duval G, Kedinger C, Poch O, Boeuf H. Duval D, et al. FEBS Lett. 2003 Nov 6;554(1-2):111-8. doi: 10.1016/s0014-5793(03)01116-5. FEBS Lett. 2003. PMID: 14596924 Free article.
We have identified a novel conserved domain of 180 residues in PIAS proteins and shown that its 'PINIT' motif as well as other conserved motifs (in the SAP box and in the RING domain) are independently involved in nuclear retention of PIAS3L, the long form of PIAS3, that w …
We have identified a novel conserved domain of 180 residues in PIAS proteins and shown that its 'PINIT' motif as well as other conser …
Specific domain structures control abscisic acid-, salicylic acid-, and stress-mediated SIZ1 phenotypes.
Cheong MS, Park HC, Hong MJ, Lee J, Choi W, Jin JB, Bohnert HJ, Lee SY, Bressan RA, Yun DJ. Cheong MS, et al. Plant Physiol. 2009 Dec;151(4):1930-42. doi: 10.1104/pp.109.143719. Epub 2009 Oct 16. Plant Physiol. 2009. PMID: 19837819 Free PMC article.
Four conserved motifs in SIZ1 include SAP (for scaffold attachment factor A/B/acinus/PIAS domain), PINIT (for proline-isoleucine-asparagine-isoleucine-threonine), SP-RING (for SIZ/PIAS-RING), and SXS (for serine-X-serine, where X is any amino acid) motifs. ...The SXS domai …
Four conserved motifs in SIZ1 include SAP (for scaffold attachment factor A/B/acinus/PIAS domain), PINIT (for proline-isoleucine-aspa …
Interrupter resistance elucidated by alveolar pressure measurement in open-chest normal dogs.
Bates JH, Ludwig MS, Sly PD, Brown K, Martin JG, Fredberg JJ. Bates JH, et al. J Appl Physiol (1985). 1988 Jul;65(1):408-14. doi: 10.1152/jappl.1988.65.1.408. J Appl Physiol (1985). 1988. PMID: 3042744
The pressure signal observed invariably exhibits two distinct phases. The first phase is a very rapid jump, designated delta Pinit, which occurs immediately on interruption of flow. The second phase is designated delta Pdif and is a further pressure change in the same dire …
The pressure signal observed invariably exhibits two distinct phases. The first phase is a very rapid jump, designated delta Pinit, w …
Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA.
Yunus AA, Lima CD. Yunus AA, et al. Mol Cell. 2009 Sep 11;35(5):669-82. doi: 10.1016/j.molcel.2009.07.013. Mol Cell. 2009. PMID: 19748360 Free PMC article.
The X-ray structure of an active Siz1 ligase revealed an elongated tripartite architecture comprised of an N-terminal PINIT domain, a central zinc-containing RING-like SP-RING domain, and a C-terminal domain we term the SP-CTD. Structure-based mutational analysis and bioch …
The X-ray structure of an active Siz1 ligase revealed an elongated tripartite architecture comprised of an N-terminal PINIT domain, a …
Chordate PIAS proteins act as conserved repressors of the TRAF6 self-polyubiquitination.
Fu X, Wang R, Li M, Yan X, Huang H, Li J, Chen S, Yue Z, Chen S, Li Y, Dong M, Xu A, Huang S. Fu X, et al. Dev Comp Immunol. 2020 Mar;104:103554. doi: 10.1016/j.dci.2019.103554. Epub 2019 Nov 20. Dev Comp Immunol. 2020. PMID: 31758961
Here we discover that in mammalian cells, amphioxus PIAS inhibited NF-kappaB activation by co-localizing and binding with TRAF6. The interaction relied on the N-terminal SAP and PINIT domains of PIAS. TRAF6 is an E3 ubiquitin ligase, which initiates downstream NF-kappaB si …
Here we discover that in mammalian cells, amphioxus PIAS inhibited NF-kappaB activation by co-localizing and binding with TRAF6. The interac …
Gastric duplication.
Pruksapong C, Donovan RJ, Pinit A, Heldrich FJ. Pruksapong C, et al. J Pediatr Surg. 1979 Feb;14(1):83-5. doi: 10.1016/s0022-3468(79)80583-7. J Pediatr Surg. 1979. PMID: 423071
PIASy is a SUMOylation-independent negative regulator of the insulin transactivator MafA.
Onishi S, Kataoka K. Onishi S, et al. J Mol Endocrinol. 2019 Nov;63(4):297-308. doi: 10.1530/JME-19-0172. J Mol Endocrinol. 2019. PMID: 31614335
In addition, SUMO-interacting motif 1 (SIM1) at the carboxyl-terminal region of PIASy was required to repress the synergistic transactivation of MafA, Pdx1, and Beta2, transcription factors playing central roles in beta-cell differentiation and function. The PINIT and SP-R …
In addition, SUMO-interacting motif 1 (SIM1) at the carboxyl-terminal region of PIASy was required to repress the synergistic transactivatio …
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