Rho/ROCK Signaling Pathway in Kidney Diseases: Mechanisms and Therapeutic Perspectives. [PDF]
Xiong W +4 more
europepmc +1 more source
Guanine Nucleotide Exchange Factors and Small GTPases: Their Regulation and Functions, Diseases, and Therapeutic Targets. [PDF]
Lin Z +15 more
europepmc +1 more source
The role of FMR1 mRNA structure on the efficiency of non-canonical translation of toxic polyglycine protein. [PDF]
Niewiadomska D +4 more
europepmc +1 more source
M-Ras distinct activation scenarios: A mechanistic outlook and targeting. [PDF]
Xu L, Liu Y, Jang H, Nussinov R.
europepmc +1 more source
Identification of locally activated spindle-associated proteins in oocytes uncovers a phosphatase-driven mechanism. [PDF]
Wan X +5 more
europepmc +1 more source
The Chromatin Protein CFDP1 Activates TPX2 and Promotes Chromosomal Microtubule Nucleation and Spindle Assembly. [PDF]
Gopinathan G, Luan X, Diekwisch TGH.
europepmc +1 more source
Polo-like kinase 1-mediated phosphorylation of the GTP-binding protein Ran is important for bipolar spindle formation [PDF]
Polo-like kinase functions are essential for the establishment of a normal bipolar mitotic spindle, although precisely how Plk1 regulates the spindle is uncertain. In this study, we report that the small GTP/GDP-binding protein Ran is associated with Plk1.
Andrea Ferris, Terry D Copeland
exaly +4 more sources
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Expression of the Xenopus GTP-binding protein gene Ran during embryogenesis
Development Genes and Evolution, 2000The Ran gene family encodes small GTP binding proteins that are associated with a variety of nuclear processes. We isolated a Xenopus Ran cDNA and analyzed the pattern of expression of this gene during embryogenesis. Ran is expressed maternally and later in the CNS, neural crest, mesenchyme, eyes, and otic vesicles.
Yasuko Onuma, M Asashima
exaly +3 more sources
The GTP-binding protein Ran/TC4 is required for protein import into the nucleus
Nature, 1993Two cytosolic fractions (A and B) from Xenopus oocytes are sufficient to support protein import into the nuclei of digitonin-permeabilized cells. Fraction A recognizes the nuclear localization sequence (NLS) and binds the import substrate to the nuclear envelope, whereas fraction B mediates the subsequent passage of the bound substrate into the nucleus.
Gunter Blobel +2 more
exaly +3 more sources

