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<Article>
<Journal>
				<PublisherName>Shiraz University Press</PublisherName>
				<JournalTitle>Molecular Biology Research Communications</JournalTitle>
				<Issn>2322-181X</Issn>
				<Volume>10</Volume>
				<Issue>4</Issue>
				<PubDate PubStatus="epublish">
					<Year>2021</Year>
					<Month>12</Month>
					<Day>01</Day>
				</PubDate>
			</Journal>
<ArticleTitle>Tissue expression of MMP-9, TIMP-1, RECK, and miR338-3p in prostate gland: can it predict cancer?</ArticleTitle>
<VernacularTitle></VernacularTitle>
			<FirstPage>149</FirstPage>
			<LastPage>156</LastPage>
			<ELocationID EIdType="pii">6424</ELocationID>
			
<ELocationID EIdType="doi">10.22099/mbrc.2021.40912.1646</ELocationID>
			
			<Language>EN</Language>
<AuthorList>
<Author>
					<FirstName>Rodolfo Pacheco</FirstName>
					<LastName>De Moraes</LastName>
<Affiliation>Laboratory of Medical Investigation (LIM55), Urology Department, Faculdade de Medicina da Universidade de São Paulo (FMUSP), São Paulo, Brazil</Affiliation>

</Author>
<Author>
					<FirstName>Ruan</FirstName>
					<LastName>Pimenta</LastName>

						<AffiliationInfo>
						<Affiliation>Laboratory of Medical Investigation (LIM55), Urology Department, Faculdade de Medicina da Universidade de São Paulo (FMUSP), São Paulo, Brazil</Affiliation>
						</AffiliationInfo>

						<AffiliationInfo>
						<Affiliation>D&amp;#039;Or Institute for Research and Education (IDOR), São Paulo, Brazil</Affiliation>
						</AffiliationInfo>

</Author>
<Author>
					<FirstName>Fernando Noburu Cabral</FirstName>
					<LastName>Mori</LastName>
<Affiliation>Laboratory of Medical Investigation (LIM55), Urology Department, Faculdade de Medicina da Universidade de São Paulo (FMUSP), São Paulo, Brazil</Affiliation>

</Author>
<Author>
					<FirstName>Gabriel Arantes</FirstName>
					<LastName>Dos Santos</LastName>

						<AffiliationInfo>
						<Affiliation>Laboratory of Medical Investigation (LIM55), Urology Department, Faculdade de Medicina da Universidade de São Paulo (FMUSP), São Paulo, Brazil</Affiliation>
						</AffiliationInfo>

						<AffiliationInfo>
						<Affiliation>D&amp;#039;Or Institute for Research and Education (IDOR), São Paulo, Brazil</Affiliation>
						</AffiliationInfo>

</Author>
<Author>
					<FirstName>Nayara Izabel</FirstName>
					<LastName>Viana</LastName>
<Affiliation>Laboratory of Medical Investigation (LIM55), Urology Department, Faculdade de Medicina da Universidade de São Paulo (FMUSP), São Paulo, Brazil</Affiliation>

</Author>
<Author>
					<FirstName>Vanessa Ribeiro</FirstName>
					<LastName>Guimarães</LastName>
<Affiliation>Laboratory of Medical Investigation (LIM55), Urology Department, Faculdade de Medicina da Universidade de São Paulo (FMUSP), São Paulo, Brazil</Affiliation>

</Author>
<Author>
					<FirstName>Juliana Alves</FirstName>
					<LastName>De Camargo</LastName>
<Affiliation>Laboratory of Medical Investigation (LIM55), Urology Department, Faculdade de Medicina da Universidade de São Paulo (FMUSP), São Paulo, Brazil</Affiliation>

</Author>
<Author>
					<FirstName>Katia Ramos Moreira-</FirstName>
					<LastName>Leite</LastName>
<Affiliation>Laboratory of Medical Investigation (LIM55), Urology Department, Faculdade de Medicina da Universidade de São Paulo (FMUSP), São Paulo, Brazil</Affiliation>

</Author>
<Author>
					<FirstName>Miguel</FirstName>
					<LastName>Srougi</LastName>

						<AffiliationInfo>
						<Affiliation>Laboratory of Medical Investigation (LIM55), Urology Department, Faculdade de Medicina da Universidade de São Paulo (FMUSP), São Paulo, Brazil</Affiliation>
						</AffiliationInfo>

						<AffiliationInfo>
						<Affiliation>D&amp;#039;Or Institute for Research and Education (IDOR), São Paulo, Brazil</Affiliation>
						</AffiliationInfo>

</Author>
<Author>
					<FirstName>William Carlos</FirstName>
					<LastName>Nahas</LastName>
<Affiliation>Instituto Do Cancer Do Estado De São Paulo (ICESP), Universidade de São Paulo, São Paulo, Brazil</Affiliation>

</Author>
<Author>
					<FirstName>Sabrina T.</FirstName>
					<LastName>Reis</LastName>
<Affiliation>Laboratory of Medical Investigation (LIM55), Urology Department, Faculdade de Medicina da Universidade de São Paulo (FMUSP), São Paulo, Brazil</Affiliation>

</Author>
</AuthorList>
				<PublicationType>Journal Article</PublicationType>
			<History>
				<PubDate PubStatus="received">
					<Year>2021</Year>
					<Month>06</Month>
					<Day>08</Day>
				</PubDate>
			</History>
		<Abstract>Prostate cancer is the most frequent malignancy affecting men worldwide. Due to the low sensitivity and specificity of the prostate-specific antigen test and the digital rectal exam as screening modalities, several alternatives are being studied. This study aimed to evaluate the application of MMP-9 and its regulators (TIMP-1, RECK, and miR-338-3p) as diagnostic and prognostic indicators of prostate cancer. A total of 134 randomly selected patients under investigation for prostate cancer submitted to a transrectal ultrasound-guided prostate biopsy were enrolled in the study; of these, 61 were positive for the disease (cases), and 73 were negative (control group). The tissue samples were further analyzed by gene and miR-338-3p expression analysis using qRT-PCR (one randomly selected fragment of each patient).  Approximately 58% of the patients with prostate cancer presented MMP9 upregulation, while 73%, 65%, and 69% downregulated IMP-1, RECK, and miR-338-3p, respectively. MiR-338-3p was expressed at lower levels in patients with PSA concentrations exceeding 20 ng/mL (p=0.045) and abnormal DRE (p=0.006), while the RECK was more expressed in patients with abnormal DRE (p=0.01). We found that most patients with prostate cancer overexpressed MMP-9; on the other hand, most of them underexpressed TIMP-1, RECK, and miR-338-3p. MiR-338-3p presented as a possible predictor of poor prognosis. Further studies are warranted to evaluate these biomarkers as prognosis factors better.</Abstract>
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			<Param Name="value">Image-guided biopsy</Param>
			</Object>
			<Object Type="keyword">
			<Param Name="value">Biomarkers</Param>
			</Object>
			<Object Type="keyword">
			<Param Name="value">Matrix metalloproteinases</Param>
			</Object>
			<Object Type="keyword">
			<Param Name="value">TIMP proteins</Param>
			</Object>
			<Object Type="keyword">
			<Param Name="value">MicroRNA</Param>
			</Object>
		</ObjectList>
<ArchiveCopySource DocType="pdf">https://mbrc.shirazu.ac.ir/article_6424_fde4c2935682898bf39df3a009a0a928.pdf</ArchiveCopySource>
</Article>

<Article>
<Journal>
				<PublisherName>Shiraz University Press</PublisherName>
				<JournalTitle>Molecular Biology Research Communications</JournalTitle>
				<Issn>2322-181X</Issn>
				<Volume>10</Volume>
				<Issue>4</Issue>
				<PubDate PubStatus="epublish">
					<Year>2021</Year>
					<Month>12</Month>
					<Day>01</Day>
				</PubDate>
			</Journal>
<ArticleTitle>A phenotypic and molecular investigation of biofilm formation in clinical samples of Pseudomonas aeruginosa</ArticleTitle>
<VernacularTitle></VernacularTitle>
			<FirstPage>157</FirstPage>
			<LastPage>163</LastPage>
			<ELocationID EIdType="pii">6425</ELocationID>
			
<ELocationID EIdType="doi">10.22099/mbrc.2021.41708.1673</ELocationID>
			
			<Language>EN</Language>
<AuthorList>
<Author>
					<FirstName>Leila</FirstName>
					<LastName>Dolatshah</LastName>
<Affiliation>Department of Pathobiology, School of Veterinary Medicine, Shiraz University, Shiraz, Iran</Affiliation>

</Author>
<Author>
					<FirstName>Mohammad</FirstName>
					<LastName>Tabatabaei</LastName>
<Affiliation>Department of Pathobiology, School of Veterinary Medicine, Shiraz University, Shiraz, Iran</Affiliation>

</Author>
</AuthorList>
				<PublicationType>Journal Article</PublicationType>
			<History>
				<PubDate PubStatus="received">
					<Year>2021</Year>
					<Month>09</Month>
					<Day>11</Day>
				</PubDate>
			</History>
		<Abstract>&lt;em&gt;Pseudomonas aeruginosa&lt;/em&gt; is identified as a versatile opportunistic microorganism with metabolic diversity contributing to a wide range of health burdens, especially in immunocompromised patients. This bacterium is the cause of 10 to 20% of nosocomial infections. In this study, we evaluated the phenotypic characterizations of biofilm formation in &lt;em&gt;P. aeruginosa&lt;/em&gt; clinical isolates using micro-titer plate assay. Indeed, we estimated the prevalence of QS (&lt;em&gt;rhlI&lt;/em&gt;, &lt;em&gt;rhlR&lt;/em&gt;, &lt;em&gt;rhlAB&lt;/em&gt;, &lt;em&gt;lasB&lt;/em&gt;, &lt;em&gt;lasI&lt;/em&gt;, &lt;em&gt;lasR, aprA&lt;/em&gt;) and virulence genes (&lt;em&gt;pslA&lt;/em&gt; and &lt;em&gt;cupA&lt;/em&gt;) by PCR. The results showed that among 69% of the isolates forming biofilm, 9% were strong biofilm producers, whereas 13% and 47% of isolates produced moderate and low amounts of biofilm, respectively. All isolates possessed &lt;em&gt;cupA &lt;/em&gt;and seven QS genes (&lt;em&gt;rhlI&lt;/em&gt;, &lt;em&gt;rhlR&lt;/em&gt;, &lt;em&gt;rhlAB&lt;/em&gt;, &lt;em&gt;lasB&lt;/em&gt;,  &lt;em&gt;lasI&lt;/em&gt;, &lt;em&gt;lasR&lt;/em&gt;, &lt;em&gt;aprA&lt;/em&gt;), while 92% of the isolates possessed the &lt;em&gt;pslA&lt;/em&gt; gene. Identification of these genes and their association with biofilm formation can be advantageous in adopting therapeutic methods.</Abstract>
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			<Param Name="value">Pseudomonas aeruginosa</Param>
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			<Object Type="keyword">
			<Param Name="value">Biofilm</Param>
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			<Object Type="keyword">
			<Param Name="value">Quorum sensing</Param>
			</Object>
			<Object Type="keyword">
			<Param Name="value">Fimbrial</Param>
			</Object>
			<Object Type="keyword">
			<Param Name="value">cupA</Param>
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			<Object Type="keyword">
			<Param Name="value">pslA</Param>
			</Object>
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<ArchiveCopySource DocType="pdf">https://mbrc.shirazu.ac.ir/article_6425_1d4d97cb990e1b5be8411f03a9944289.pdf</ArchiveCopySource>
</Article>

<Article>
<Journal>
				<PublisherName>Shiraz University Press</PublisherName>
				<JournalTitle>Molecular Biology Research Communications</JournalTitle>
				<Issn>2322-181X</Issn>
				<Volume>10</Volume>
				<Issue>4</Issue>
				<PubDate PubStatus="epublish">
					<Year>2021</Year>
					<Month>12</Month>
					<Day>01</Day>
				</PubDate>
			</Journal>
<ArticleTitle>Investigation of p16 protein expression and its association with histopathologic parameters in breast cancer</ArticleTitle>
<VernacularTitle></VernacularTitle>
			<FirstPage>165</FirstPage>
			<LastPage>170</LastPage>
			<ELocationID EIdType="pii">6444</ELocationID>
			
<ELocationID EIdType="doi">10.22099/mbrc.2021.41691.1671</ELocationID>
			
			<Language>EN</Language>
<AuthorList>
<Author>
					<FirstName>Siamak</FirstName>
					<LastName>Naji-Haddadi</LastName>
<Affiliation>Mahzad Women’s Hospital Urmia Medical Sciences University (UMSU), Urmia, Iran</Affiliation>

</Author>
<Author>
					<FirstName>Daniel</FirstName>
					<LastName>Elieh-Ali-Komi</LastName>
<Affiliation>Cellular and Molecular Research Center, Cellular and Molecular Medicine Institute, Urmia University of Medical Sciences, Urmia, Iran</Affiliation>

</Author>
<Author>
					<FirstName>Saeid</FirstName>
					<LastName>Aghayan</LastName>
<Affiliation>Department of Pathology, Urmia University of Medical Sciences, Urmia, Iran</Affiliation>

</Author>
<Author>
					<FirstName>Rahim</FirstName>
					<LastName>Asghari</LastName>
<Affiliation>Immune Cell Therapy, Stem Cell Transplantation Research Center (HİSRC), Urmia Medical University (UMSU), Urmia, Iran</Affiliation>

</Author>
<Author>
					<FirstName>Javad</FirstName>
					<LastName>Rasouli</LastName>
<Affiliation>Department of Biostatistics and Epidemiology, School of Medicine Urmia University of Medical Sciences, Urmia, Iran</Affiliation>

</Author>
</AuthorList>
				<PublicationType>Journal Article</PublicationType>
			<History>
				<PubDate PubStatus="received">
					<Year>2021</Year>
					<Month>09</Month>
					<Day>09</Day>
				</PubDate>
			</History>
		<Abstract>We investigated the association between p16 expression and histopathologic parameters including size, neural and vascular invasion, and lymph node involvement in breast cancer. 58 specimens from patients with different grades of breast cancer were included. Hematoxylin and eosin and immunohistochemistry staining for p16 was performed. 5 patients (8.6%) had grade I, 23 (39.7%) had grade II, and 30 (51.7%) had grade III breast cancer. Assessment of the tumor size showed that 5 (8.6%) tumors had a size of ≤2cm, 29 (50%) were between 2-5 cm and 24 (41.4%) had a size of ≥5cm. Moreover, 45 (77.6%) of the included patients had axillary lymph node involvement. Investigation of association between p16 positivity with pathological parameters in three groups with positivity to p16 (1-25%, 26-75%, &gt;75%) showed that there was no association between p16 positivity and other parameters including histologic score (p=0.44), tumor size (p=0.77), neural invasion (p=0.79), perivascular invasion (p=0.98) and the number of involved LNs (p=0.49). From the group including eight patients with &gt;75% p16 positivity, seven (87.5%) were found with neural invasion and two (25%) with perivascular invasion. P16 positivity was not associated with size, neural and vascular invasion, and LN involvement in breast cancer.</Abstract>
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			<Param Name="value">Breast cancer</Param>
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			<Object Type="keyword">
			<Param Name="value">p16</Param>
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			<Object Type="keyword">
			<Param Name="value">Neural invasion</Param>
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			<Object Type="keyword">
			<Param Name="value">Vascular invasion</Param>
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			<Object Type="keyword">
			<Param Name="value">Nodal involvement</Param>
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<ArchiveCopySource DocType="pdf">https://mbrc.shirazu.ac.ir/article_6444_fe3d6ad6fe373ff384ed863fb8156b9c.pdf</ArchiveCopySource>
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<Article>
<Journal>
				<PublisherName>Shiraz University Press</PublisherName>
				<JournalTitle>Molecular Biology Research Communications</JournalTitle>
				<Issn>2322-181X</Issn>
				<Volume>10</Volume>
				<Issue>4</Issue>
				<PubDate PubStatus="epublish">
					<Year>2021</Year>
					<Month>12</Month>
					<Day>01</Day>
				</PubDate>
			</Journal>
<ArticleTitle>Analysis and comparison of physiochemical properties, mutations and glycosylation patterns between RNA polymerase and membrane protein of SARS-CoV and SARS-CoV-2</ArticleTitle>
<VernacularTitle></VernacularTitle>
			<FirstPage>171</FirstPage>
			<LastPage>178</LastPage>
			<ELocationID EIdType="pii">6445</ELocationID>
			
<ELocationID EIdType="doi">10.22099/mbrc.2021.42187.1692</ELocationID>
			
			<Language>EN</Language>
<AuthorList>
<Author>
					<FirstName>Mandana</FirstName>
					<LastName>Behbahani</LastName>
<Affiliation>Department of Biotechnology, Faculty of Biological Science and Technology, University of Isfahan, Isfahan, Iran</Affiliation>

</Author>
<Author>
					<FirstName>Parisa</FirstName>
					<LastName>Rabiei</LastName>
<Affiliation>Department of Biotechnology, Faculty of Biological Science and Technology, University of Isfahan, Isfahan, Iran</Affiliation>

</Author>
<Author>
					<FirstName>Hassan</FirstName>
					<LastName>Mohabatkar</LastName>
<Affiliation>Department of Biotechnology, Faculty of Biological Science and Technology, University of Isfahan, Isfahan, Iran</Affiliation>

</Author>
</AuthorList>
				<PublicationType>Journal Article</PublicationType>
			<History>
				<PubDate PubStatus="received">
					<Year>2021</Year>
					<Month>11</Month>
					<Day>08</Day>
				</PubDate>
			</History>
		<Abstract>SARS-CoV-2 is a member of β-genus of the coronavirus subfamily, alongside the virus that causes SARS (Severe Acute Respiratory Syndrome). As implied by their names, SARS-CoV-2 and SARS-CoV genome sequences&lt;strong&gt; &lt;/strong&gt;have close kinship (about 79% genomic sequence similarity). In the current research, sequence-based physiochemical properties of RNA polymerase and membrane glycoprotein of SARS-CoV-2 and SARS-CoV were compared. In addition, impacts of substitution mutations on stability and glycosylation patterns of these proteins were studied. In comparison of physiochemical features of membrane and RNA polymerase proteins, only instability index of membrane protein was difference between SARS-CoV and SARS-CoV-2. Mutation analysis showed increase in stability of RNA polymerase and decrease in stability of membrane protein in SARS-CoV-2. Glycosylation pattern analysis showed glycosylation enhancement in both membrane and RNA polymerase proteins of SARS-CoV-2 in comparison to SARS-CoV. In conclusion, more glycosylation and stability of SARS-CoV-2 RNA polymerase could be one of the reasons of high pathogenicity property and host immune system evasion of SARS-CoV-2. </Abstract>
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			<Param Name="value">COVID-19</Param>
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			<Object Type="keyword">
			<Param Name="value">Betacoronavirus</Param>
			</Object>
			<Object Type="keyword">
			<Param Name="value">MEME motifs</Param>
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			<Object Type="keyword">
			<Param Name="value">Glycosylation</Param>
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			<Object Type="keyword">
			<Param Name="value">Substitution mutation</Param>
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<ArchiveCopySource DocType="pdf">https://mbrc.shirazu.ac.ir/article_6445_82b100f5f4c11a7674409fbf993dc35a.pdf</ArchiveCopySource>
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<Article>
<Journal>
				<PublisherName>Shiraz University Press</PublisherName>
				<JournalTitle>Molecular Biology Research Communications</JournalTitle>
				<Issn>2322-181X</Issn>
				<Volume>10</Volume>
				<Issue>4</Issue>
				<PubDate PubStatus="epublish">
					<Year>2021</Year>
					<Month>12</Month>
					<Day>01</Day>
				</PubDate>
			</Journal>
<ArticleTitle>Fission yeast Ase1PRC1 is required for the G2-microtubule damage response</ArticleTitle>
<VernacularTitle></VernacularTitle>
			<FirstPage>179</FirstPage>
			<LastPage>188</LastPage>
			<ELocationID EIdType="pii">6452</ELocationID>
			
<ELocationID EIdType="doi">10.22099/mbrc.2021.41001.1651</ELocationID>
			
			<Language>EN</Language>
<AuthorList>
<Author>
					<FirstName>Rose M.</FirstName>
					<LastName>Doss</LastName>
<Affiliation>Department of Biology, University of Colorado at Colorado Springs, Colorado Springs, 
CO 80918</Affiliation>

</Author>
<Author>
					<FirstName>Sindi</FirstName>
					<LastName>Xhunga</LastName>
<Affiliation>Department of Biology, University of Colorado at Colorado Springs, Colorado Springs, 
CO 80918</Affiliation>

</Author>
<Author>
					<FirstName>Dorothy</FirstName>
					<LastName>Klimczak</LastName>
<Affiliation>Department of Biology, University of Colorado at Colorado Springs, Colorado Springs, 
CO 80918</Affiliation>

</Author>
<Author>
					<FirstName>Molly</FirstName>
					<LastName>Cameron</LastName>
<Affiliation>Department of Biology, University of Colorado at Colorado Springs, Colorado Springs, 
CO 80918</Affiliation>

</Author>
<Author>
					<FirstName>Jordan</FirstName>
					<LastName>Verlare</LastName>
<Affiliation>Department of Biology, University of Colorado at Colorado Springs, Colorado Springs, 
CO 80918</Affiliation>

</Author>
<Author>
					<FirstName>Tom D.</FirstName>
					<LastName>Wolkow</LastName>
<Affiliation>Department of Biology, University of Colorado at Colorado Springs, Colorado Springs, 
CO 80918</Affiliation>

</Author>
</AuthorList>
				<PublicationType>Journal Article</PublicationType>
			<History>
				<PubDate PubStatus="received">
					<Year>2021</Year>
					<Month>06</Month>
					<Day>18</Day>
				</PubDate>
			</History>
		<Abstract>&lt;em&gt;Schizosaccharomyces pombe&lt;/em&gt; delays entry into mitosis following G&lt;sub&gt;2&lt;/sub&gt; microtubule damage. This pathway is dependent on Rad26&lt;sup&gt;ATRIP&lt;/sup&gt;, the regulatory subunit of the Rad26&lt;sup&gt;ATRIP&lt;/sup&gt;/Rad3&lt;sup&gt;ATR&lt;/sup&gt; DNA damage response (DDR) complex. However, this G&lt;sub&gt;2&lt;/sub&gt; microtubule damage response pathway acts independently of the G&lt;sub&gt;2&lt;/sub&gt; DNA damage checkpoint pathway. To identify other proteins in this G&lt;sub&gt;2&lt;/sub&gt; microtubule damage pathway, we previously screened a cDNA overexpression library for genes that rescued the sensitivity of &lt;em&gt;rad26Δ&lt;/em&gt; cells to the microtubule poison thiabendazole. A partial cDNA fragment encoding only the C-terminal regulatory region of the microtubule bundling protein &lt;em&gt;Ase1&lt;sup&gt;PRC1 &lt;/sup&gt;&lt;/em&gt;was isolated. This fragment lacks the Ase1&lt;sup&gt;PRC1&lt;/sup&gt; dimerization and microtubule binding domains and retains the conserved C-terminal unstructured regulatory region. Here, we  report that &lt;em&gt;ase1Δ&lt;/em&gt; cells fail to delay entry into mitosis following G&lt;sub&gt;2&lt;/sub&gt; microtubule damage. Microscopy revealed that Rad26&lt;sup&gt;ATRIP&lt;/sup&gt; foci localized alongside Ase1&lt;sup&gt;PRC1&lt;/sup&gt; filaments, although we suggest that this is related to microtubule-dependent double strand break mobility that facilitates homologous recombination events. Indeed, we report that the DNA repair protein Rad52 co-localizes with Rad26&lt;sup&gt;ATRIP &lt;/sup&gt;at these foci, and that localization of Rad26&lt;sup&gt;ATRIP&lt;/sup&gt; to these foci depends on a Rad26&lt;sup&gt;ATRIP&lt;/sup&gt; N-terminal region containing a checkpoint recruitment domain. To our knowledge, this is the first report implicating Ase1&lt;sup&gt;PRC1&lt;/sup&gt; in regulation of the G&lt;sub&gt;2&lt;/sub&gt;/M transition.</Abstract>
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			<Object Type="keyword">
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<ArchiveCopySource DocType="pdf">https://mbrc.shirazu.ac.ir/article_6452_826e9659b69c4e3cf556cefb22a958b2.pdf</ArchiveCopySource>
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