Výsledky vyhledávání

Messenger ribonucleic acid encoding interferon-inducible guanylate binding protein 1 is induced in human endometrium within the putative window of implantation

Autor: S, Kumar, Q, Li, A, Dua, Y K, Ying, M K, Bagchi, I C, Bagchi

Publikováno v: The Journal of clinical endocrinology and metabolism. 86(6)

The putative window of embryo implantation in the human opens between days 19--24 of the menstrual cycle. During this period, the endometrium undergoes distinctive structural and functional changes orchestrated by steroid hormones, growth factors, an

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6805d361b2c6b0c028aa77d081576852
https://pubmed.ncbi.nlm.nih.gov/11397834

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Progesterone induces calcitonin gene expression in human endometrium within the putative window of implantation

Autor: S, Kumar, L J, Zhu, M, Polihronis, S T, Cameron, D T, Baird, F, Schatz, A, Dua, Y K, Ying, M K, Bagchi, I C, Bagchi

Publikováno v: The Journal of clinical endocrinology and metabolism. 83(12)

The human endometrium acquires the ability to implant the developing embryo within a specific time window that is thought to open between days 19-24 of the secretory phase of the menstrual cycle. During this period the endometrium undergoes pronounce

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7a257019cdd1cf4af4a5a80e22ba3beb
https://pubmed.ncbi.nlm.nih.gov/9851792

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Expression of calcitonin receptors in mouse preimplantation embryos and their function in the regulation of blastocyst differentiation by calcitonin

Autor: I. C. Bagchi, Jun Wang, Ujjwal K. Rout, D.R. Armant

Publikováno v: Development (Cambridge, England). 125(21)

Calcitonin secretion in the pregnant uterus is tightly regulated by the ovarian hormones, estrogen and progesterone, which limit its expression to a brief period preceding blastocyst implantation. The binding of calcitonin to a G protein-coupled rece

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59f9fa6478d58fc5a32b43ab6e213e77
https://pubmed.ncbi.nlm.nih.gov/9753683

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Calcitonin is a progesterone-regulated marker that forecasts the receptive state of endometrium during implantation

Autor: L J, Zhu, K, Cullinan-Bove, M, Polihronis, M K, Bagchi, I C, Bagchi

Publikováno v: Endocrinology. 139(9)

Previous studies established that in the rat, the uterus can accept a developing blastocyst for implantation only during a limited period of time on day 5 of gestation, termed the receptive phase. Our previous studies showed that the expression of ca

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8034895c596cf184835c8d574a755de6
https://pubmed.ncbi.nlm.nih.gov/9724048

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Calcitonin gene expression in the rat uterus during pregnancy

Autor: Y Q, Ding, M K, Bagchi, C W, Bardin, I C, Bagchi

Publikováno v: Recent progress in hormone research. 50

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::06b36eb894d5f256daeb4051c75c11e3
https://pubmed.ncbi.nlm.nih.gov/7740169

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Identification of amino acids essential for calmodulin binding and activation of smooth muscle myosin light chain kinase

Autor: I C, Bagchi, Q H, Huang, A R, Means

Publikováno v: The Journal of biological chemistry. 267(5)

Smooth muscle myosin light chain kinase (smMLCK) is a Ca(2+)-calmodulin (CaM)-dependent enzyme that phosphorylates the 20-kDa light chains of myosin. In a previous study (Bagchi, I.C., Kemp, B.E., and Means, A.R. (1989) J. Biol. Chem. 264, 15843-1584

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::1f68dce7047d4111ac02fd03e3cc2ab5
https://pubmed.ncbi.nlm.nih.gov/1737757

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Regulation of smooth muscle myosin light chain kinase by calmodulin

Autor: A R, Means, I C, Bagchi, M F, VanBerkum, B E, Kemp

Publikováno v: Advances in experimental medicine and biology. 304

The mutagenesis work described in this paper has been instrumental in furthering our understanding of how CaM binds to and activates MLCK. Figure 2 schematically represents this interaction. The inactive MLCK appears to have a catalytic domain that i

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::7545c7dba553d6c31f3f79246760a207
https://pubmed.ncbi.nlm.nih.gov/1803894

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Myosin light chain kinase structure function analysis using bacterial expression

Autor: I C, Bagchi, B E, Kemp, A R, Means

Publikováno v: The Journal of biological chemistry. 264(27)

A 40-kDa fragment of chicken smooth muscle myosin light chain kinase was produced and partially purified from a bacterial expression system. This fragment exhibits calmodulin binding and substrate phosphorylation properties similar to those of the is

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2da0f07201da008a75bfc27010886ae2
https://pubmed.ncbi.nlm.nih.gov/2674119

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