{"title":"Wine-related flavonols for therapeutic use in Alzheimer’s disease, an in-silico investigation","authors":"S. Gopal, I. Jahan","doi":"10.1007/s42485-022-00094-1","DOIUrl":"https://doi.org/10.1007/s42485-022-00094-1","url":null,"abstract":"","PeriodicalId":73910,"journal":{"name":"Journal of proteins and proteomics","volume":"83 1","pages":"133 - 148"},"PeriodicalIF":0.0,"publicationDate":"2022-08-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"87371969","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
A. Mahanty, S. Lenka, T. Adak, L. Behera, S. R. Prabhukarthikeyan, S. Raghu, P. Rath
{"title":"In silico screening of phytogenic compounds against Rhizoctonia solani trehalase enzyme","authors":"A. Mahanty, S. Lenka, T. Adak, L. Behera, S. R. Prabhukarthikeyan, S. Raghu, P. Rath","doi":"10.1007/s42485-022-00093-2","DOIUrl":"https://doi.org/10.1007/s42485-022-00093-2","url":null,"abstract":"","PeriodicalId":73910,"journal":{"name":"Journal of proteins and proteomics","volume":"15 1","pages":"127 - 132"},"PeriodicalIF":0.0,"publicationDate":"2022-07-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"81858070","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"In silico identification of potential inhibitors of MPS1 from edible mushroom (Pleurotus ostreatus) to prevent aneuploidy and tumorigenesis","authors":"D. Mishra, A. Mishra, Pramod Katara, M. Singh","doi":"10.1007/s42485-022-00091-4","DOIUrl":"https://doi.org/10.1007/s42485-022-00091-4","url":null,"abstract":"","PeriodicalId":73910,"journal":{"name":"Journal of proteins and proteomics","volume":"107 1","pages":"175 - 185"},"PeriodicalIF":0.0,"publicationDate":"2022-06-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"77427240","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"α-synuclein enfolds tyrosine hydroxylase and dopamine ß-hydroxylase, potentially reducing dopamine and norepinephrine synthesis.","authors":"Steven Lehrer, Peter H Rheinstein","doi":"10.1007/s42485-022-00088-z","DOIUrl":"https://doi.org/10.1007/s42485-022-00088-z","url":null,"abstract":"<p><strong>Background: </strong>Parkinson's disease (PD) results from degeneration of dopamine and norepinephrine neurons due to α-synuclein aggregates that likely have their origin in the gut. Tyrosine hydroxylase (TH) catalyses the formation of L-DOPA, the rate-limiting step in the biosynthesis of dopamine. A second enzyme, DOPA decarboxylase (DDC), catalyzes the conversion of L-DOPA to dopamine. A third enzyme, dopamine ß-hydroxylase (DBH), catalyzes the conversion of dopamine to norepinephrine. To analyze possible interactions of α-synuclein with TH, DDC and DBH, we performed in silico protein-protein docking.</p><p><strong>Methods: </strong>Protein data bank (pdb) entries were searched on the RCSB Protein Data Bank. We identified four structures that allowed us to examine the relationship of α-synuclein with TH, DDC, and DBH: (1) Human micelle-bound alpha-synuclein, (2) solution structure of the regulatory domain of tyrosine hydroxylase (<i>Rattus norvegicus</i>), (3) crystal structure of human aromatic L-amino acid decarboxylase (DOPA decarboxylase) in the apo form and (4) crystal structure of human dopamine ß-hydroxylase at 2.9 angstrom resolution. We used the ClusPro server (https://cluspro.org) for protein-protein docking. The protein structures were visualized with PyMOL v 2.3.4.</p><p><strong>Results: </strong>α-synuclein partially enfolds tyrosine hydroxylase and dopamine ß-hydroxylase, potentially reducing dopamine and norepinephrine synthesis. α-synuclein may dock too far away from DOPA decarboxylase to affect its function directly.</p><p><strong>Conclusions: </strong>Our in silico finding of α-synuclein partly enfolding tyrosine hydroxylase and dopamine ß-hydroxylase suggests that α-synuclein docking inhibition could increase dopamine and norepinephrine biosynthesis, ameliorating PD symptoms. Small molecules that bind to α-synuclein have already been identified. Further studies may lead to new small molecule drugs that block α-synuclein enfolding of tyrosine hydroxylase and dopamine ß-hydroxylase.</p>","PeriodicalId":73910,"journal":{"name":"Journal of proteins and proteomics","volume":" ","pages":"109-115"},"PeriodicalIF":0.0,"publicationDate":"2022-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9585989/pdf/nihms-1809942.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40567752","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
R. A. Rohman, S. Maryanto, W. M. Sudania, C. Utomo, T. Liwang
{"title":"Nitrogen uptake efficiency induced fumarate hydratase activity in oil palm seedlings","authors":"R. A. Rohman, S. Maryanto, W. M. Sudania, C. Utomo, T. Liwang","doi":"10.1007/s42485-022-00087-0","DOIUrl":"https://doi.org/10.1007/s42485-022-00087-0","url":null,"abstract":"","PeriodicalId":73910,"journal":{"name":"Journal of proteins and proteomics","volume":"152 7 1","pages":"117 - 124"},"PeriodicalIF":0.0,"publicationDate":"2022-05-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83169746","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Kulwinder Singh Sran, Yogita Sharma, Tejinder Kaur, A. Rao
{"title":"Post-translational modifications and glycoprofiling of palivizumab by UHPLC–RPLC/HILIC and mass spectrometry","authors":"Kulwinder Singh Sran, Yogita Sharma, Tejinder Kaur, A. Rao","doi":"10.1007/s42485-022-00086-1","DOIUrl":"https://doi.org/10.1007/s42485-022-00086-1","url":null,"abstract":"","PeriodicalId":73910,"journal":{"name":"Journal of proteins and proteomics","volume":"11 1","pages":"95 - 108"},"PeriodicalIF":0.0,"publicationDate":"2022-05-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"76480370","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
P. Gopinath, Gopal Gopisetty, S. Veluswami, S. Sundersingh, Rajkumar Thangarajan
{"title":"Mass spectrometric profiling of tryptic digests of trifluoroethanol extracts from core needle biopsies of breast cancer tissues is a viable sample screening tool for biomarker discovery","authors":"P. Gopinath, Gopal Gopisetty, S. Veluswami, S. Sundersingh, Rajkumar Thangarajan","doi":"10.1007/s42485-022-00085-2","DOIUrl":"https://doi.org/10.1007/s42485-022-00085-2","url":null,"abstract":"","PeriodicalId":73910,"journal":{"name":"Journal of proteins and proteomics","volume":"1 1","pages":"79 - 94"},"PeriodicalIF":0.0,"publicationDate":"2022-02-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"73322911","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Mahwish Javed, Muhammad Bilal, B. Tabassum, Arif Malik, O. Adeyinka, M. Tariq, I. Nasir
{"title":"Purification and functional characterization of lectin from Chenopodium album","authors":"Mahwish Javed, Muhammad Bilal, B. Tabassum, Arif Malik, O. Adeyinka, M. Tariq, I. Nasir","doi":"10.1007/s42485-022-00084-3","DOIUrl":"https://doi.org/10.1007/s42485-022-00084-3","url":null,"abstract":"","PeriodicalId":73910,"journal":{"name":"Journal of proteins and proteomics","volume":"73 1","pages":"55 - 62"},"PeriodicalIF":0.0,"publicationDate":"2022-02-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"86876983","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Transposon mutagenesis of ACC deamination gene alters the proteomic analysis of wheat plant under non-saline and saline stress","authors":"R. Singh, P. Jha","doi":"10.1007/s42485-022-00083-4","DOIUrl":"https://doi.org/10.1007/s42485-022-00083-4","url":null,"abstract":"","PeriodicalId":73910,"journal":{"name":"Journal of proteins and proteomics","volume":"64 2","pages":"39 - 53"},"PeriodicalIF":0.0,"publicationDate":"2022-01-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"72439021","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Nithya Rathinam, Madhana Priya Nanda Kumar, Charles Emmanuel Jebaraj Walter, M. Ramasamy
{"title":"Analyzing the effect of deleterious non-synonymous SNPs causing CHARGE syndrome associated with the CHD7 protein using computational approaches","authors":"Nithya Rathinam, Madhana Priya Nanda Kumar, Charles Emmanuel Jebaraj Walter, M. Ramasamy","doi":"10.1007/s42485-021-00082-x","DOIUrl":"https://doi.org/10.1007/s42485-021-00082-x","url":null,"abstract":"","PeriodicalId":73910,"journal":{"name":"Journal of proteins and proteomics","volume":"17 1","pages":"63 - 77"},"PeriodicalIF":0.0,"publicationDate":"2022-01-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"83468296","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}