Mitosis in Drosophila

1989 ◽  
Vol 92 (2) ◽  
pp. 137-146 ◽  
Author(s):  
D.M. Glover
Keyword(s):  
Genetic Analysis ◽  
Embryonic Development ◽  
Protein Interactions ◽  
Dynamic Process ◽  
Early Embryogenesis ◽  
Female Sterility ◽  
Protein Protein Interactions ◽  
Stages Of Development ◽  
Cell Cycles

Drosophila is an attractive organism in which to study both the rapid rounds of mitosis typical of embryonic development in many species, and the longer cell cycles of diploid tissues later in development. Mutations in genes essential for mitosis in Drosophila may result in lethality in late embryonic, larval or pupal stages of development. In addition, mutations in many genes required for the nuclear divisions of early embryogenesis have been found in screens for female sterility. The mitotic mutations have phenotypes indicative of lesions at a variety of mitotic stages. A combined molecular and genetic analysis of these genes has the potential to unravel the complex set of protein-protein interactions that occur in this dynamic process.

Folding and unfolding for binding: large-scale protein dynamics in protein–protein interactions

2006 ◽  
Vol 34 (5) ◽  
pp. 971-974 ◽  
Author(s):  
G.C.K. Roberts
Keyword(s):  
Protein Dynamics ◽  
Protein Interactions ◽  
Dynamic Process ◽  
Large Scale ◽  
Protein Protein Interactions ◽  
Key Residues

The role of dynamics in the function of proteins, from enzymes to signalling proteins, is widely recognized. In many cases, the dynamic process is a relatively localized one, involving motion of a limited number of key residues, while in others large-scale domain movements may be involved. These motions all take place within the context of a folded protein; however, there is increasing evidence for the existence of some proteins where a transition between folded and unfolded structures is required for function.

Utilizing Split Fluorescent Proteins to Visualize Binary Cell Fate Decisions

2021 ◽  
Author(s):  
Setu Mehta
Keyword(s):  
Embryonic Development ◽  
Cell Fate ◽  
Protein Interactions ◽  
Fluorescent Proteins ◽  
Protein Protein Interactions ◽  
Temporal Expression ◽  
Cell Fate Decisions ◽  
Cellular Decision Making ◽  
Decision Making Processes ◽  
Intimate Knowledge

Binary cell fate decisions serve at a cornerstone of cellular decision-making processes during embryonic development. Understanding and studying these decisions require an intimate knowledge of the spatial and temporal expression dynamics of critical genes. Split fluorescent proteins (sFP) can serve as a novel tool to study these binary cell fate decisions, with unique applications such as the potential to amplify weak genetic signals. Ultimately, sFPs can be utilized to revolutionize the study of protein-protein interactions during embryonic development and beyond.

scholarly journals msiDBN: A Method of Identifying Critical Proteins in Dynamic PPI Networks

2014 ◽  
Vol 2014 ◽  
pp. 1-10 ◽  
Author(s):  
Yuan Zhang ◽  
Nan Du ◽  
Kang Li ◽  
Jinchao Feng ◽  
Kebin Jia ◽  
...  
Keyword(s):  
Yeast Cell ◽  
Protein Interactions ◽  
Structural Changes ◽  
Biological Processes ◽  
Protein Protein Interactions ◽  
Cell Cycles ◽  
Construction Methods ◽  
Ppi Networks ◽  
Time Courses ◽  
Traditional Construction

Dynamics of protein-protein interactions (PPIs) reveals the recondite principles of biological processes inside a cell. Shown in a wealth of study, just a small group of proteins, rather than the majority, play more essential roles at crucial points of biological processes. This present work focuses on identifying these critical proteins exhibiting dramatic structural changes in dynamic PPI networks. First, a comprehensive way of modeling the dynamic PPIs is presented which simultaneously analyzes the activity of proteins and assembles the dynamic coregulation correlation between proteins at each time point. Second, a novel method is proposed, named msiDBN, which models a common representation of multiple PPI networks using a deep belief network framework and analyzes the reconstruction errors and the variabilities across the time courses in the biological process. Experiments were implemented on data of yeast cell cycles. We evaluated our network construction method by comparing the functional representations of the derived networks with two other traditional construction methods. The ranking results of critical proteins in msiDBN were compared with the results from the baseline methods. The results of comparison showed that msiDBN had better reconstruction rate and identified more proteins of critical value to yeast cell cycle process.

scholarly journals PINCH1 Plays an Essential Role in Early Murine Embryonic Development but Is Dispensable in Ventricular Cardiomyocytes

2005 ◽  
Vol 25 (8) ◽  
pp. 3056-3062 ◽  
Author(s):  
Xingqun Liang ◽  
Qiang Zhou ◽  
Xiaodong Li ◽  
Yunfu Sun ◽  
Min Lu ◽  
...  
Keyword(s):  
Embryonic Development ◽  
Protein Interactions ◽  
Essential Role ◽  
Adaptor Protein ◽  
Protein Protein Interactions ◽  
Signaling Complex ◽  
Basal Phenotype ◽  
Lim Domains ◽  
Ventricular Cardiomyocytes ◽  
Integrin Linked Kinase

ABSTRACT PINCH1, an adaptor protein composed of five LIM domains, mediates protein-protein interactions and functions as a component of the integrin-integrin-linked kinase (ILK) complex. The integrin-ILK signaling complex plays a pivotal role in cell motility, proliferation, and survival during embryonic development of many animal species. To elucidate the physiological function of PINCH1 in mouse embryonic development, we have deleted the mouse PINCH1 gene by homologous recombination. Mice heterozygous for PINCH1 are viable and indistinguishable from wild-type littermates. However, no viable homozygous offspring were observed from PINCH1 +/ − intercrosses. Histological analysis of homozygous mutant embryos revealed that they had a disorganized egg cylinder by E5.5, which degenerated by E6.5. Furthermore, E5.5 PINCH1 − / − embryos exhibited decreased cell proliferation and excessive cell death. We have also generated and analyzed mice in which PINCH1 has been specifically deleted in ventricular cardiomyocytes. These mice exhibit no basal phenotype, with respect to mouse survival, cardiac histology, or cardiac function as measured by echocardiography. Altogether, these data indicate that PINCH1 plays an essential role in early murine embryonic development but is dispensable in ventricular cardiomyocytes.

scholarly journals A proteomic analysis of mammalian preimplantation embryonic development

Reproduction ◽  
2005 ◽  
Vol 130 (6) ◽  
pp. 899-905 ◽  
Author(s):  
Mandy G Katz-Jaffe ◽  
Donald W Linck ◽  
William B Schoolcraft ◽  
David K Gardner
Keyword(s):  
Embryonic Development ◽  
Protein Interactions ◽  
Reproductive Tract ◽  
Cellular Function ◽  
Protein Profiles ◽  
Protein Protein Interactions ◽  
Post Translational Modifications ◽  
Flight Mass Spectrometry ◽  
Mammalian Embryos

Genetic studies on the mammalian preimplantation embryo are providing a wealth of information regarding gene expression. However, changes in the transcriptome do not always reflect cellular function or the complexity and diversity of the mammalian proteome with post-translational modifications or protein–protein interactions. To elucidate embryonic cellular function, a detailed understanding at the protein level is necessary. The aim of this study was to generate protein profiles of mammalian embryos throughout development, and to investigate the effects of oxygen concentration on the embryonic proteome. A protocol was developed to analyse small groups of embryos (n = 5) by time-of-flight mass spectrometry. F1 mice zygotes were cultured in G1/G2 sequential media with recombinant albumin (2.5 mg/ml) in 6% CO2 and O2 concentrations of either 5% or 20%. In vivo-developed embryos were flushed from the reproductive tract (day 4). Protein profiles were generated for all embryonic samples and statistical analysis revealed 32 potential proteins/biomarkers with significant changes (P < 0.05). Embryos generated under 5% O2 more closely resembled in vivo-developed embryos. Under 20% O2 conditions, embryos showed down-regulation of 10 proteins/biomarkers (masses between 4 to 20 kDa) (P < 0.05) confirming the pathological effects of oxygen during embryonic development. These data demonstrate for the first time the complexity of the mammalian preimplantation proteome. The unique protein profiles of in vivo-developed embryos and a panel of selected biomarkers represent optimal cellular function, against which comparisons can be made to facilitate improvements in mammalian assisted reproduction techniques procedures.

Protein-protein interactions of the p53 family with the Bcl-2 family in hepatocellular carcinoma

2011 ◽  
Vol 49 (08) ◽  
Author(s):  
LC König ◽  
M Meinhard ◽  
C Sandig ◽  
MH Bender ◽  
A Lovas ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Protein Interactions ◽  
Protein Protein Interactions ◽  
P53 Family

Partial Purification of a Specific Plasminogen Activator from Porcine Parotid Glands

1974 ◽  
Vol 31 (03) ◽  
pp. 403-414 ◽  
Author(s):  
Terence Cartwright
Keyword(s):  
Nucleic Acid ◽  
Salivary Glands ◽  
Plasminogen Activator ◽  
Protein Interactions ◽  
Partial Purification ◽  
Protein Protein Interactions ◽  
Parotid Glands ◽  
Two Stage ◽  
Preliminary Characterization ◽  
Specific Inhibitors

SummaryA method is described for the extraction with buffers of near physiological pH of a plasminogen activator from porcine salivary glands. Substantial purification of the activator was achieved although this was to some extent complicated by concomitant extraction of nucleic acid from the glands. Preliminary characterization experiments using specific inhibitors suggested that the activator functioned by a similar mechanism to that proposed for urokinase, but with some important kinetic differences in two-stage assay systems. The lack of reactivity of the pig gland enzyme in these systems might be related to the tendency to protein-protein interactions observed with this material.

Target-Templated de novo Design of Macrocyclic D-/L-Peptides: Inhibitors of the PD-1/PD-L1 Interaction

2020 ◽  
Author(s):  
Salvador Guardiola ◽  
Monica Varese ◽  
Xavier Roig ◽  
Jesús Garcia ◽  
Ernest Giralt
Keyword(s):  
Protein Interactions ◽  
Cyclic Peptides ◽  
General Framework ◽  
Large Scale ◽  
De Novo ◽  
Inhibitory Effect ◽  
Original Text ◽  
Protein Protein Interactions ◽  
Retraction Notice ◽  
Pharmaceutical Properties

<p>NOTE: This preprint has been retracted by consensus from all authors. See the retraction notice in place above; the original text can be found under "Version 1", accessible from the version selector above.</p><p><br></p><p>------------------------------------------------------------------------</p><p><br></p><p>Peptides, together with antibodies, are among the most potent biochemical tools to modulate challenging protein-protein interactions. However, current structure-based methods are largely limited to natural peptides and are not suitable for designing target-specific binders with improved pharmaceutical properties, such as macrocyclic peptides. Here we report a general framework that leverages the computational power of Rosetta for large-scale backbone sampling and energy scoring, followed by side-chain composition, to design heterochiral cyclic peptides that bind to a protein surface of interest. To showcase the applicability of our approach, we identified two peptides (PD-<i>i</i>3 and PD-<i>i</i>6) that target PD-1, a key immune checkpoint, and work as protein ligand decoys. A comprehensive biophysical evaluation confirmed their binding mechanism to PD-1 and their inhibitory effect on the PD-1/PD-L1 interaction. Finally, elucidation of their solution structures by NMR served as validation of our <i>de novo </i>design approach. We anticipate that our results will provide a general framework for designing target-specific drug-like peptides.<i></i></p>

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