Human, vector and parasite Hsp90 proteins: a comparative bioinformatics analysis
- Faya, Ngonidzashe, Penkler, David L, Tastan Bishop, Özlem
- Authors: Faya, Ngonidzashe , Penkler, David L , Tastan Bishop, Özlem
- Date: 2015
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/148038 , vital:38704 , DOI: 10.1016/j.fob.2015.11.003
- Description: The treatment of protozoan parasitic diseases is challenging, and thus identification and analysis of new drug targets is important. Parasites survive within host organisms, and some need intermediate hosts to complete their life cycle. Changing host environment puts stress on parasites, and often adaptation is accompanied by the expression of large amounts of heat shock proteins (Hsps). Among Hsps, Hsp90 proteins play an important role in stress environments. Yet, there has been little computational research on Hsp90 proteins to analyze them comparatively as potential parasitic drug targets. Here, an attempt was made to gain detailed insights into the differences between host, vector and parasitic Hsp90 proteins by large-scale bioinformatics analysis.
- Full Text:
- Date Issued: 2015
- Authors: Faya, Ngonidzashe , Penkler, David L , Tastan Bishop, Özlem
- Date: 2015
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/148038 , vital:38704 , DOI: 10.1016/j.fob.2015.11.003
- Description: The treatment of protozoan parasitic diseases is challenging, and thus identification and analysis of new drug targets is important. Parasites survive within host organisms, and some need intermediate hosts to complete their life cycle. Changing host environment puts stress on parasites, and often adaptation is accompanied by the expression of large amounts of heat shock proteins (Hsps). Among Hsps, Hsp90 proteins play an important role in stress environments. Yet, there has been little computational research on Hsp90 proteins to analyze them comparatively as potential parasitic drug targets. Here, an attempt was made to gain detailed insights into the differences between host, vector and parasitic Hsp90 proteins by large-scale bioinformatics analysis.
- Full Text:
- Date Issued: 2015
Plasmodium falciparum Hop: detailed analysis on complex formation with Hsp70 and Hsp90
- Hatherley, Rowan, Clitheroe, Crystal-Leigh, Faya, Ngonidzashe, Tastan Bishop, Özlem
- Authors: Hatherley, Rowan , Clitheroe, Crystal-Leigh , Faya, Ngonidzashe , Tastan Bishop, Özlem
- Date: 2015
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/163532 , vital:41046 , https://doi.org/10.1016/j.bbrc.2014.11.103
- Description: The heat shock organizing protein (Hop) is important in modulating the activity and co-interaction of two chaperones: heat shock protein 70 and 90 (Hsp70 and Hsp90). Recent research suggested that Plasmodium falciparum Hop (PfHop), PfHsp70 and PfHsp90 form a complex in the trophozoite infective stage. However, there has been little computational research on the malarial Hop protein in complex with other malarial Hsps.
- Full Text:
- Date Issued: 2015
- Authors: Hatherley, Rowan , Clitheroe, Crystal-Leigh , Faya, Ngonidzashe , Tastan Bishop, Özlem
- Date: 2015
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/163532 , vital:41046 , https://doi.org/10.1016/j.bbrc.2014.11.103
- Description: The heat shock organizing protein (Hop) is important in modulating the activity and co-interaction of two chaperones: heat shock protein 70 and 90 (Hsp70 and Hsp90). Recent research suggested that Plasmodium falciparum Hop (PfHop), PfHsp70 and PfHsp90 form a complex in the trophozoite infective stage. However, there has been little computational research on the malarial Hop protein in complex with other malarial Hsps.
- Full Text:
- Date Issued: 2015
SANCDB: a South African natural compound database
- Hatherley, Rowan, Brown, David K, Musyoka, Thommas M, Penkler, David L, Faya, Ngonidzashe, Lobb, Kevin A, Tastan Bishop, Özlem
- Authors: Hatherley, Rowan , Brown, David K , Musyoka, Thommas M , Penkler, David L , Faya, Ngonidzashe , Lobb, Kevin A , Tastan Bishop, Özlem
- Date: 2015
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/162890 , vital:40994 , DOI 10.1186/s13321-015-0080-89
- Description: Natural products (NPs) are important to the drug discovery process. NP research efforts are expanding world-wide and South Africa is no exception to this. While freely-accessible small molecule databases, containing compounds isolated from indigenous sources, have been established in a number of other countries, there is currently no such online database in South Africa.
- Full Text:
- Date Issued: 2015
- Authors: Hatherley, Rowan , Brown, David K , Musyoka, Thommas M , Penkler, David L , Faya, Ngonidzashe , Lobb, Kevin A , Tastan Bishop, Özlem
- Date: 2015
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/162890 , vital:40994 , DOI 10.1186/s13321-015-0080-89
- Description: Natural products (NPs) are important to the drug discovery process. NP research efforts are expanding world-wide and South Africa is no exception to this. While freely-accessible small molecule databases, containing compounds isolated from indigenous sources, have been established in a number of other countries, there is currently no such online database in South Africa.
- Full Text:
- Date Issued: 2015
Plasmodium falciparum Hop: detailed analysis on complex formation with Hsp70 and Hsp90
- Hatherley, Rowan, Clitheroe, Crystal-Leigh, Faya, Ngonidzashe, Tastan Bishop, Özlem
- Authors: Hatherley, Rowan , Clitheroe, Crystal-Leigh , Faya, Ngonidzashe , Tastan Bishop, Özlem
- Date: 2015
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/125708 , vital:35810 , https://doi.10.1016/j.bbrc.2014.11.103
- Description: The heat shock organizing protein (Hop) is important in modulating the activity and co-interaction of two chaperones: heat shock protein 70 and 90 (Hsp70 and Hsp90). Recent research suggested that Plasmodium falciparum Hop (PfHop), PfHsp70 and PfHsp90 form a complex in the trophozoite infective stage. However, there has been little computational research on the malarial Hop protein in complex with other malarial Hsps. Using in silico characterization of the protein, this work showed that individual domains of Hop are evolving at different rates within the protein. Differences between human Hop (HsHop) and PfHop were identified by motif analysis. Homology modeling of PfHop and HsHop in complex with their own cytosolic Hsp90 and Hsp70 C-terminal peptide partners indicated excellent conservation of the Hop concave TPR sites bound to the C-terminal motifs of partner proteins. Further, we analyzed additional binding sites between Hop and Hsp90, and showed, for the first time, that they are distinctly less conserved between human and malaria parasite. These sites are located on the convex surface of Hop TPR2, and involved in interactions with the Hsp90 middle domain. Since the convex sites are less conserved than the concave sites, it makes their potential for malarial inhibitor design extremely attractive (as opposed to the concave sites which have been the focus of previous efforts).
- Full Text:
- Date Issued: 2015
- Authors: Hatherley, Rowan , Clitheroe, Crystal-Leigh , Faya, Ngonidzashe , Tastan Bishop, Özlem
- Date: 2015
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/125708 , vital:35810 , https://doi.10.1016/j.bbrc.2014.11.103
- Description: The heat shock organizing protein (Hop) is important in modulating the activity and co-interaction of two chaperones: heat shock protein 70 and 90 (Hsp70 and Hsp90). Recent research suggested that Plasmodium falciparum Hop (PfHop), PfHsp70 and PfHsp90 form a complex in the trophozoite infective stage. However, there has been little computational research on the malarial Hop protein in complex with other malarial Hsps. Using in silico characterization of the protein, this work showed that individual domains of Hop are evolving at different rates within the protein. Differences between human Hop (HsHop) and PfHop were identified by motif analysis. Homology modeling of PfHop and HsHop in complex with their own cytosolic Hsp90 and Hsp70 C-terminal peptide partners indicated excellent conservation of the Hop concave TPR sites bound to the C-terminal motifs of partner proteins. Further, we analyzed additional binding sites between Hop and Hsp90, and showed, for the first time, that they are distinctly less conserved between human and malaria parasite. These sites are located on the convex surface of Hop TPR2, and involved in interactions with the Hsp90 middle domain. Since the convex sites are less conserved than the concave sites, it makes their potential for malarial inhibitor design extremely attractive (as opposed to the concave sites which have been the focus of previous efforts).
- Full Text:
- Date Issued: 2015
PRIMO: an interactive homology modeling pipeline
- Hatherley, Rowan, Brown, David K, Glenister, Michael, Tastan Bishop, Özlem
- Authors: Hatherley, Rowan , Brown, David K , Glenister, Michael , Tastan Bishop, Özlem
- Date: 2017
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/148282 , vital:38726 , doi: 10.1371/journal.pone.0166698
- Description: The development of automated servers to predict the three-dimensional structure of proteins has seen much progress over the years. These servers make calculations simpler, but largely exclude users from the process. In this study, we present the PRotein Interactive MOdeling (PRIMO) pipeline for homology modeling of protein monomers. The pipeline eases the multi-step modeling process, and reduces the workload required by the user, while still allowing engagement from the user during every step. Default parameters are given for each step, which can either be modified or supplemented with additional external input. PRIMO has been designed for users of varying levels of experience with homology modeling. The pipeline incorporates a user-friendly interface that makes it easy to alter parameters used during modeling.
- Full Text:
- Date Issued: 2017
- Authors: Hatherley, Rowan , Brown, David K , Glenister, Michael , Tastan Bishop, Özlem
- Date: 2017
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/148282 , vital:38726 , doi: 10.1371/journal.pone.0166698
- Description: The development of automated servers to predict the three-dimensional structure of proteins has seen much progress over the years. These servers make calculations simpler, but largely exclude users from the process. In this study, we present the PRotein Interactive MOdeling (PRIMO) pipeline for homology modeling of protein monomers. The pipeline eases the multi-step modeling process, and reduces the workload required by the user, while still allowing engagement from the user during every step. Default parameters are given for each step, which can either be modified or supplemented with additional external input. PRIMO has been designed for users of varying levels of experience with homology modeling. The pipeline incorporates a user-friendly interface that makes it easy to alter parameters used during modeling.
- Full Text:
- Date Issued: 2017
SANCDB: a South African natural compound database
- Hatherley, Rowan, Brown, David K, Musyoka, Thommas M, Penkler, David L, Faya, Ngonidzashe, Lobb, Kevin A, Tastan Bishop, Özlem
- Authors: Hatherley, Rowan , Brown, David K , Musyoka, Thommas M , Penkler, David L , Faya, Ngonidzashe , Lobb, Kevin A , Tastan Bishop, Özlem
- Date: 2015
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/148337 , vital:38730 , DOI: 10.1186/s13321-015-0080-8
- Description: Natural products (NPs) are important to the drug discovery process. NP research efforts are expanding world-wide and South Africa is no exception to this. While freely-accessible small molecule databases, containing compounds isolated from indigenous sources, have been established in a number of other countries, there is currently no such online database in South Africa.
- Full Text:
- Date Issued: 2015
- Authors: Hatherley, Rowan , Brown, David K , Musyoka, Thommas M , Penkler, David L , Faya, Ngonidzashe , Lobb, Kevin A , Tastan Bishop, Özlem
- Date: 2015
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/148337 , vital:38730 , DOI: 10.1186/s13321-015-0080-8
- Description: Natural products (NPs) are important to the drug discovery process. NP research efforts are expanding world-wide and South Africa is no exception to this. While freely-accessible small molecule databases, containing compounds isolated from indigenous sources, have been established in a number of other countries, there is currently no such online database in South Africa.
- Full Text:
- Date Issued: 2015
Probing the structural dynamics of the Plasmodium falciparum tunneling-fold enzyme 6-pyruvoyl tetrahydropterin synthase to reveal allosteric drug targeting sites:
- Khairallah, Afrah, Ross, Caroline J, Tastan Bishop, Özlem
- Authors: Khairallah, Afrah , Ross, Caroline J , Tastan Bishop, Özlem
- Date: 2020
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/163057 , vital:41008 , https://doi.org/10.3389/fmolb.2020.575196
- Description: The de novo folate synthesis pathway is a well-established drug target in the treatment of many infectious diseases. Antimalarial antifolate drugs have proven to be effective against malaria, however, rapid drug resistance has emerged on the two primary targeted enzymes: dihydrofolate reductase and dihydroptoreate synthase. The need to identify alternative antifolate drugs and novel metabolic targets is of imminent importance. The 6-pyruvol tetrahydropterin synthase (PTPS) enzyme belongs to the tunneling fold protein superfamily which is characterized by a distinct central tunnel/cavity. The enzyme catalyzes the second reaction step of the parasite’s de novo folate synthesis pathway and is responsible for the conversion of 7,8-dihydroneopterin to 6-pyruvoyl-tetrahydropterin. In this study, we examine the structural dynamics of Plasmodium falciparum PTPS using the anisotropic network model, to elucidate the collective motions that drive the function of the enzyme and identify potential sites for allosteric modulation of its binding properties.
- Full Text:
- Date Issued: 2020
- Authors: Khairallah, Afrah , Ross, Caroline J , Tastan Bishop, Özlem
- Date: 2020
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/163057 , vital:41008 , https://doi.org/10.3389/fmolb.2020.575196
- Description: The de novo folate synthesis pathway is a well-established drug target in the treatment of many infectious diseases. Antimalarial antifolate drugs have proven to be effective against malaria, however, rapid drug resistance has emerged on the two primary targeted enzymes: dihydrofolate reductase and dihydroptoreate synthase. The need to identify alternative antifolate drugs and novel metabolic targets is of imminent importance. The 6-pyruvol tetrahydropterin synthase (PTPS) enzyme belongs to the tunneling fold protein superfamily which is characterized by a distinct central tunnel/cavity. The enzyme catalyzes the second reaction step of the parasite’s de novo folate synthesis pathway and is responsible for the conversion of 7,8-dihydroneopterin to 6-pyruvoyl-tetrahydropterin. In this study, we examine the structural dynamics of Plasmodium falciparum PTPS using the anisotropic network model, to elucidate the collective motions that drive the function of the enzyme and identify potential sites for allosteric modulation of its binding properties.
- Full Text:
- Date Issued: 2020
AMBER force field parameters for the Zn (II) ions of the tunneling-fold enzymes GTP cyclohydrolase I and 6-pyruvoyl tetrahydropterin synthase:
- Khairallah, Afrah, Tastan Bishop, Özlem, Moses, Vuyani
- Authors: Khairallah, Afrah , Tastan Bishop, Özlem , Moses, Vuyani
- Date: 2020
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/163068 , vital:41009 , DOI: 10.1080/07391102.2020.1796800
- Description: The folate biosynthesis pathway is an essential pathway for cell growth and survival. Folate derivatives serve as a source of the one-carbon units in several intracellular metabolic reactions. Rapidly dividing cells rely heavily on the availability of folate derivatives for their proliferation. As a result, drugs targeting this pathway have shown to be effective against tumor cells and pathogens, but drug resistance against the available antifolate drugs emerged quickly. Therefore, there is a need to develop new treatment strategies and identify alternative metabolic targets. The two de novo folate biosynthesis pathway enzymes, GTP cyclohydrolase I (GCH1) and 6-pyruvoyl tetrahydropterin synthase (PTPS), can provide an alternative strategy to overcome the drug resistance that emerged in the two primary targeted enzymes dihydrofolate reductase and dihydropteroate synthase.
- Full Text:
- Date Issued: 2020
- Authors: Khairallah, Afrah , Tastan Bishop, Özlem , Moses, Vuyani
- Date: 2020
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/163068 , vital:41009 , DOI: 10.1080/07391102.2020.1796800
- Description: The folate biosynthesis pathway is an essential pathway for cell growth and survival. Folate derivatives serve as a source of the one-carbon units in several intracellular metabolic reactions. Rapidly dividing cells rely heavily on the availability of folate derivatives for their proliferation. As a result, drugs targeting this pathway have shown to be effective against tumor cells and pathogens, but drug resistance against the available antifolate drugs emerged quickly. Therefore, there is a need to develop new treatment strategies and identify alternative metabolic targets. The two de novo folate biosynthesis pathway enzymes, GTP cyclohydrolase I (GCH1) and 6-pyruvoyl tetrahydropterin synthase (PTPS), can provide an alternative strategy to overcome the drug resistance that emerged in the two primary targeted enzymes dihydrofolate reductase and dihydropteroate synthase.
- Full Text:
- Date Issued: 2020
No evidence for association between APOL1 kidney disease risk alleles and Human African Trypanosomiasis in two Ugandan populations:
- Kimuda, Magambo P, Noyes, Harry, Mulindwa, Julius, Enyaru, John, Alibu, Vincent P, Sidibe, Issa, Mumba Ngoyi, Dieuodonne, Hertz-Fowler, Christiane, MacLeod, Annette, Tastan Bishop, Özlem, Matovu, Enock
- Authors: Kimuda, Magambo P , Noyes, Harry , Mulindwa, Julius , Enyaru, John , Alibu, Vincent P , Sidibe, Issa , Mumba Ngoyi, Dieuodonne , Hertz-Fowler, Christiane , MacLeod, Annette , Tastan Bishop, Özlem , Matovu, Enock
- Date: 2018
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/162924 , vital:40997 , https://doi.org/10.1371/journal.pntd.0006300
- Description: Human African trypanosomiasis (HAT) manifests as an acute form caused by Trypanosoma brucei rhodesiense (Tbr) and a chronic form caused by Trypanosoma brucei gambiense (Tbg). Previous studies have suggested a host genetic role in infection outcomes, particularly for APOL1. We have undertaken candidate gene association studies (CGAS) in a Ugandan Tbr and a Tbg HAT endemic area, to determine whether polymorphisms in IL10, IL8, IL4, HLAG, TNFA, TNX4LB, IL6, IFNG, MIF, APOL1, HLAA, IL1B, IL4R, IL12B, IL12R, HP, HPR, and CFH have a role in HAT.
- Full Text:
- Date Issued: 2018
- Authors: Kimuda, Magambo P , Noyes, Harry , Mulindwa, Julius , Enyaru, John , Alibu, Vincent P , Sidibe, Issa , Mumba Ngoyi, Dieuodonne , Hertz-Fowler, Christiane , MacLeod, Annette , Tastan Bishop, Özlem , Matovu, Enock
- Date: 2018
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/162924 , vital:40997 , https://doi.org/10.1371/journal.pntd.0006300
- Description: Human African trypanosomiasis (HAT) manifests as an acute form caused by Trypanosoma brucei rhodesiense (Tbr) and a chronic form caused by Trypanosoma brucei gambiense (Tbg). Previous studies have suggested a host genetic role in infection outcomes, particularly for APOL1. We have undertaken candidate gene association studies (CGAS) in a Ugandan Tbr and a Tbg HAT endemic area, to determine whether polymorphisms in IL10, IL8, IL4, HLAG, TNFA, TNX4LB, IL6, IFNG, MIF, APOL1, HLAA, IL1B, IL4R, IL12B, IL12R, HP, HPR, and CFH have a role in HAT.
- Full Text:
- Date Issued: 2018
No evidence for association with APOL1 kidney disease risk alleles and Human African Trypanosomiasis in two Ugandan populations:
- Kimuda, Magambo Phillip, Noyes, Harry, Mulindwa, Julius, Enyaru, John, Alibu, Vincent Pius, Sidibe, Issa, Mumba, Dieuodonne, Hertz-Fowler, Christiane, MacLeod, Annette, Tastan Bishop, Özlem, Matovu, Enock
- Authors: Kimuda, Magambo Phillip , Noyes, Harry , Mulindwa, Julius , Enyaru, John , Alibu, Vincent Pius , Sidibe, Issa , Mumba, Dieuodonne , Hertz-Fowler, Christiane , MacLeod, Annette , Tastan Bishop, Özlem , Matovu, Enock
- Date: 2017
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/148272 , vital:38725 , doi: 10.1371/journal.pntd.0006300
- Description: Human African trypanosomiasis (HAT) manifests as an acute form caused by Trypanosoma brucei rhodesiense (Tbr) and a chronic form caused by Trypanosoma brucei gambiense (Tbg). Previous studies have suggested a host genetic role in infection outcomes, particularly for APOL1. We have undertaken a candidate gene association studies (CGAS) in a Ugandan Tbr and a Tbg HAT endemic area, to determine whether polymorphisms in IL10, IL8, IL4, HLAG, TNFA, TNX4LB, IL6, IFNG, MIF, APOL1, HLAA, IL1B, IL4R, IL12B, IL12R, HP, HPR, and CFH have a role in HAT.
- Full Text:
- Date Issued: 2017
- Authors: Kimuda, Magambo Phillip , Noyes, Harry , Mulindwa, Julius , Enyaru, John , Alibu, Vincent Pius , Sidibe, Issa , Mumba, Dieuodonne , Hertz-Fowler, Christiane , MacLeod, Annette , Tastan Bishop, Özlem , Matovu, Enock
- Date: 2017
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/148272 , vital:38725 , doi: 10.1371/journal.pntd.0006300
- Description: Human African trypanosomiasis (HAT) manifests as an acute form caused by Trypanosoma brucei rhodesiense (Tbr) and a chronic form caused by Trypanosoma brucei gambiense (Tbg). Previous studies have suggested a host genetic role in infection outcomes, particularly for APOL1. We have undertaken a candidate gene association studies (CGAS) in a Ugandan Tbr and a Tbg HAT endemic area, to determine whether polymorphisms in IL10, IL8, IL4, HLAG, TNFA, TNX4LB, IL6, IFNG, MIF, APOL1, HLAA, IL1B, IL4R, IL12B, IL12R, HP, HPR, and CFH have a role in HAT.
- Full Text:
- Date Issued: 2017
Identification of Novel Potential Inhibitors of Pteridine Reductase 1 in Trypanosoma brucei via Computational Structure-Based Approaches and in Vitro Inhibition Assays
- Kimuda, Magambo Phillip, Laming, Dustin, Hoppe, Heinrich C, Tastan Bishop, Özlem
- Authors: Kimuda, Magambo Phillip , Laming, Dustin , Hoppe, Heinrich C , Tastan Bishop, Özlem
- Date: 2019
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/124675 , vital:35647 , https://doi:10.3390/molecules24010142
- Description: Pteridine reductase 1 (PTR1) is a trypanosomatid multifunctional enzyme that provides a mechanism for escape of dihydrofolate reductase (DHFR) inhibition. This is because PTR1 can reduce pterins and folates. Trypanosomes require folates and pterins for survival and are unable to synthesize them de novo. Currently there are no anti-folate based Human African Trypanosomiasis (HAT) chemotherapeutics in use. Thus, successful dual inhibition of Trypanosoma brucei dihydrofolate reductase (TbDHFR) and Trypanosoma brucei pteridine reductase 1 (TbPTR1) has implications in the exploitation of anti-folates. We carried out molecular docking of a ligand library of 5742 compounds against TbPTR1 and identified 18 compounds showing promising binding modes. The protein-ligand complexes were subjected to molecular dynamics to characterize their molecular interactions and energetics, followed by in vitro testing. In this study, we identified five compounds which showed low micromolar Trypanosome growth inhibition in in vitro experiments that might be acting by inhibition of TbPTR1. Compounds RUBi004, RUBi007, RUBi014, and RUBi018 displayed moderate to strong antagonism (mutual reduction in potency) when used in combination with the known TbDHFR inhibitor, WR99210. This gave an indication that the compounds might inhibit both TbPTR1 and TbDHFR. RUBi016 showed an additive effect in the isobologram assay. Overall, our results provide a basis for scaffold optimization for further studies in the development of HAT anti-folates.
- Full Text:
- Date Issued: 2019
- Authors: Kimuda, Magambo Phillip , Laming, Dustin , Hoppe, Heinrich C , Tastan Bishop, Özlem
- Date: 2019
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/124675 , vital:35647 , https://doi:10.3390/molecules24010142
- Description: Pteridine reductase 1 (PTR1) is a trypanosomatid multifunctional enzyme that provides a mechanism for escape of dihydrofolate reductase (DHFR) inhibition. This is because PTR1 can reduce pterins and folates. Trypanosomes require folates and pterins for survival and are unable to synthesize them de novo. Currently there are no anti-folate based Human African Trypanosomiasis (HAT) chemotherapeutics in use. Thus, successful dual inhibition of Trypanosoma brucei dihydrofolate reductase (TbDHFR) and Trypanosoma brucei pteridine reductase 1 (TbPTR1) has implications in the exploitation of anti-folates. We carried out molecular docking of a ligand library of 5742 compounds against TbPTR1 and identified 18 compounds showing promising binding modes. The protein-ligand complexes were subjected to molecular dynamics to characterize their molecular interactions and energetics, followed by in vitro testing. In this study, we identified five compounds which showed low micromolar Trypanosome growth inhibition in in vitro experiments that might be acting by inhibition of TbPTR1. Compounds RUBi004, RUBi007, RUBi014, and RUBi018 displayed moderate to strong antagonism (mutual reduction in potency) when used in combination with the known TbDHFR inhibitor, WR99210. This gave an indication that the compounds might inhibit both TbPTR1 and TbDHFR. RUBi016 showed an additive effect in the isobologram assay. Overall, our results provide a basis for scaffold optimization for further studies in the development of HAT anti-folates.
- Full Text:
- Date Issued: 2019
Computational analysis of missense mutations from the human Macrophage Migration Inhibitory Factor (MIF) protein by Molecular Dynamics Simulations and Dynamic Residue Network Analysis:
- Kimuda, Phillip M, Brown, David K, Amamuddy, Olivier S, Ross, Caroline J, Matovu, Enock, Tastan Bishop, Özlem
- Authors: Kimuda, Phillip M , Brown, David K , Amamuddy, Olivier S , Ross, Caroline J , Matovu, Enock , Tastan Bishop, Özlem
- Date: 2019
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/163238 , vital:41021 , https://doi.org/10.21955/aasopenres.1115054.1
- Description: Missense mutations are changes in the DNA that result in a change in the amino acid sequence. Depending on their location within the protein they can have a negative impact on how the protein functions. This is especially important for proteins involved in the body’s response to infection and diseases. Macrophage migration inhibitory factor (MIF) is one such protein that functions to recruit white blood cells to sites of inflammation.
- Full Text:
- Date Issued: 2019
- Authors: Kimuda, Phillip M , Brown, David K , Amamuddy, Olivier S , Ross, Caroline J , Matovu, Enock , Tastan Bishop, Özlem
- Date: 2019
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/163238 , vital:41021 , https://doi.org/10.21955/aasopenres.1115054.1
- Description: Missense mutations are changes in the DNA that result in a change in the amino acid sequence. Depending on their location within the protein they can have a negative impact on how the protein functions. This is especially important for proteins involved in the body’s response to infection and diseases. Macrophage migration inhibitory factor (MIF) is one such protein that functions to recruit white blood cells to sites of inflammation.
- Full Text:
- Date Issued: 2019
Homology modeling and docking of AahII-Nanobody complexes reveal the epitope binding site on AahII scorpion toxin
- Ksouri, Ayoub, Ghedira, Kais, Abderrazek, Rahma Ben, Shankar, B A Gowri, Benkahla, Alia, Tastan Bishop, Özlem, Bouhaouala-Zahar, Balkis
- Authors: Ksouri, Ayoub , Ghedira, Kais , Abderrazek, Rahma Ben , Shankar, B A Gowri , Benkahla, Alia , Tastan Bishop, Özlem , Bouhaouala-Zahar, Balkis
- Date: 2018
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/124604 , vital:35637 , https://doi.10.1016/j.bbrc.2018.01.036
- Description: Scorpion envenoming and its treatment is a public health problem in many parts of the world due to highly toxic venom polypeptides diffusing rapidly within the body of severely envenomed victims. Recently, 38 AahII-specific Nanobody sequences (Nbs) were retrieved from which the performance of NbAahII10 nanobody candidate, to neutralize the most poisonous venom compound namely AahII acting on sodium channels, was established. Herein, structural computational approach is conducted to elucidate the Nb-AahII interactions that support the biological characteristics, using Nb multiple sequence alignment (MSA) followed by modeling and molecular docking investigations (RosettaAntibody, ZDOCK software tools). Sequence and structural analysis showed two dissimilar residues of NbAahII10 CDR1 (Tyr27 and Tyr29) and an inserted polar residue Ser30 that appear to play an important role. Indeed, CDR3 region of NbAahII10 is characterized by a specific Met104 and two negatively chargedresidues Asp115 and Asp117. Complex dockings reveal that NbAahII17 and NbAahII38 share one common binding site on the surface of the AahII toxin divergent from the NbAahII10 one's. At least, a couple of NbAahII10 e AahII residue interactions (Gln38 e Asn44 and Arg62, His64, respectively) are mainly involved in the toxic AahII binding site. Altogether, this study gives valuable insights in the design and development of next generation of antivenom.
- Full Text:
- Date Issued: 2018
- Authors: Ksouri, Ayoub , Ghedira, Kais , Abderrazek, Rahma Ben , Shankar, B A Gowri , Benkahla, Alia , Tastan Bishop, Özlem , Bouhaouala-Zahar, Balkis
- Date: 2018
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/124604 , vital:35637 , https://doi.10.1016/j.bbrc.2018.01.036
- Description: Scorpion envenoming and its treatment is a public health problem in many parts of the world due to highly toxic venom polypeptides diffusing rapidly within the body of severely envenomed victims. Recently, 38 AahII-specific Nanobody sequences (Nbs) were retrieved from which the performance of NbAahII10 nanobody candidate, to neutralize the most poisonous venom compound namely AahII acting on sodium channels, was established. Herein, structural computational approach is conducted to elucidate the Nb-AahII interactions that support the biological characteristics, using Nb multiple sequence alignment (MSA) followed by modeling and molecular docking investigations (RosettaAntibody, ZDOCK software tools). Sequence and structural analysis showed two dissimilar residues of NbAahII10 CDR1 (Tyr27 and Tyr29) and an inserted polar residue Ser30 that appear to play an important role. Indeed, CDR3 region of NbAahII10 is characterized by a specific Met104 and two negatively chargedresidues Asp115 and Asp117. Complex dockings reveal that NbAahII17 and NbAahII38 share one common binding site on the surface of the AahII toxin divergent from the NbAahII10 one's. At least, a couple of NbAahII10 e AahII residue interactions (Gln38 e Asn44 and Arg62, His64, respectively) are mainly involved in the toxic AahII binding site. Altogether, this study gives valuable insights in the design and development of next generation of antivenom.
- Full Text:
- Date Issued: 2018
Analysis of protein thermostability enhancing factors in industrially important thermus bacteria species
- Kumwenda, Benjamin, Litthauer, Derek, Tastan Bishop, Özlem, Reva, Oleg
- Authors: Kumwenda, Benjamin , Litthauer, Derek , Tastan Bishop, Özlem , Reva, Oleg
- Date: 2013
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/123085 , vital:35404 , https://doi.10.4137/EBO.S12539
- Description: Elucidation of evolutionary factors that enhance protein thermostability is a critical problem and was the focus of this work on Thermus species. Pairs of orthologous sequences of T. scotoductus SA-01 and T. thermophilus HB27, with the largest negative minimum folding energy (MFE) as predicted by the UNAFold algorithm, were statistically analyzed. Favored substitutions of amino acids residues and their properties were determined. Substitutions were analyzed in modeled protein structures to determine their locations and contribution to energy differences using PyMOL and FoldX programs respectively. Dominant trends in amino acid substitutions consistent with differences in thermostability between orthologous sequences were observed. T. thermophilus thermophilic proteins showed an increase in non-polar, tiny, and charged amino acids. An abundance of alanine substituted by serine and threonine, as well as arginine substituted by glutamine and lysine was observed in T. thermophilus HB27. Structural comparison showed that stabilizing mutations occurred on surfaces and loops in protein structures.
- Full Text:
- Date Issued: 2013
- Authors: Kumwenda, Benjamin , Litthauer, Derek , Tastan Bishop, Özlem , Reva, Oleg
- Date: 2013
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/123085 , vital:35404 , https://doi.10.4137/EBO.S12539
- Description: Elucidation of evolutionary factors that enhance protein thermostability is a critical problem and was the focus of this work on Thermus species. Pairs of orthologous sequences of T. scotoductus SA-01 and T. thermophilus HB27, with the largest negative minimum folding energy (MFE) as predicted by the UNAFold algorithm, were statistically analyzed. Favored substitutions of amino acids residues and their properties were determined. Substitutions were analyzed in modeled protein structures to determine their locations and contribution to energy differences using PyMOL and FoldX programs respectively. Dominant trends in amino acid substitutions consistent with differences in thermostability between orthologous sequences were observed. T. thermophilus thermophilic proteins showed an increase in non-polar, tiny, and charged amino acids. An abundance of alanine substituted by serine and threonine, as well as arginine substituted by glutamine and lysine was observed in T. thermophilus HB27. Structural comparison showed that stabilizing mutations occurred on surfaces and loops in protein structures.
- Full Text:
- Date Issued: 2013
How to establish a bioinformatics postgraduate degree programme—a case study from South Africa
- Machanick, Philip, Tastan Bishop, Özlem
- Authors: Machanick, Philip , Tastan Bishop, Özlem
- Date: 2014
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/124641 , vital:35641 , https://doi.10.1093/bib/bbu014
- Description: The Research Unit in Bioinformatics at Rhodes University (RUBi), South Africa, offers a Masters of Science in Bioinformatics.Growing demand for bioinformatics qualifications results in applications from across Africa.Courses aim to bridge gaps in the diverse backgrounds of students who range from biologists with no prior computing exposure to computer scientists with no biology background. The programme is evenly split between coursework and research, with diverse modules from a range of departments coveringmathematics, statistics, computer science and biology, with emphasis on application to bioinformatics research. The early focus on research helps bring students up to speed with working as a researcher. We measure success of the programme by the high rate of subsequent entry to PhD study: 10 of 14 students who completed in the years 2011-2013.
- Full Text:
- Date Issued: 2014
- Authors: Machanick, Philip , Tastan Bishop, Özlem
- Date: 2014
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/124641 , vital:35641 , https://doi.10.1093/bib/bbu014
- Description: The Research Unit in Bioinformatics at Rhodes University (RUBi), South Africa, offers a Masters of Science in Bioinformatics.Growing demand for bioinformatics qualifications results in applications from across Africa.Courses aim to bridge gaps in the diverse backgrounds of students who range from biologists with no prior computing exposure to computer scientists with no biology background. The programme is evenly split between coursework and research, with diverse modules from a range of departments coveringmathematics, statistics, computer science and biology, with emphasis on application to bioinformatics research. The early focus on research helps bring students up to speed with working as a researcher. We measure success of the programme by the high rate of subsequent entry to PhD study: 10 of 14 students who completed in the years 2011-2013.
- Full Text:
- Date Issued: 2014
The PINIT domain of PIAS3: structure-function analysis of its interaction with STAT3
- Mautsa, Nicodemus, Prinsloo, Earl, Tastan Bishop, Özlem, Blatch, Gregory L
- Authors: Mautsa, Nicodemus , Prinsloo, Earl , Tastan Bishop, Özlem , Blatch, Gregory L
- Date: 2011
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/148082 , vital:38708 , DOI: 10.1002/jmr.1111
- Description: The protein inhibitor of activated signal transducer and activator of transcription 3 (PIAS3) regulates the transcriptional activity of signal transducer and activator of transcription 3 (STAT3) which regulates transcription of genes involved in cell growth, proliferation and apoptosis. The conserved proline, isoleucine, asparagine, isoleucine, threonine (PINIT) domain of PIAS3 is thought to promote STAT3–PIAS3 interaction.
- Full Text:
- Date Issued: 2011
- Authors: Mautsa, Nicodemus , Prinsloo, Earl , Tastan Bishop, Özlem , Blatch, Gregory L
- Date: 2011
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/148082 , vital:38708 , DOI: 10.1002/jmr.1111
- Description: The protein inhibitor of activated signal transducer and activator of transcription 3 (PIAS3) regulates the transcriptional activity of signal transducer and activator of transcription 3 (STAT3) which regulates transcription of genes involved in cell growth, proliferation and apoptosis. The conserved proline, isoleucine, asparagine, isoleucine, threonine (PINIT) domain of PIAS3 is thought to promote STAT3–PIAS3 interaction.
- Full Text:
- Date Issued: 2011
The evaluation and validation of copper (II) force field parameters of the Auxiliary Activity family 9 enzymes:
- Moses, Vuyani, Tastan Bishop, Özlem, Lobb, Kevin A
- Authors: Moses, Vuyani , Tastan Bishop, Özlem , Lobb, Kevin A
- Date: 2017
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/148206 , vital:38719 , DOI: 10.1016/j.cplett.2017.04.022
- Description: The Auxiliary Activity family 9 (AA9) proteins are Cu2+ coordinating enzymes which are crucial for the early stages of cellulose degradation. In this study, the force field parameters for copper-containing bonds in the Type 1 AA9 protein active site were established and used in a molecular dynamics simulation on a solvated, neutralized system containing an AA9 protein, Cu2+ and a β-cellulose surface. The copper to cellulose interaction was evident during the dynamics, which could also be accelerated by the use of high Cu O van der Waals parameters. The interaction of AA9, Cu2+ and cellulose is described in detail.
- Full Text:
- Date Issued: 2017
- Authors: Moses, Vuyani , Tastan Bishop, Özlem , Lobb, Kevin A
- Date: 2017
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/148206 , vital:38719 , DOI: 10.1016/j.cplett.2017.04.022
- Description: The Auxiliary Activity family 9 (AA9) proteins are Cu2+ coordinating enzymes which are crucial for the early stages of cellulose degradation. In this study, the force field parameters for copper-containing bonds in the Type 1 AA9 protein active site were established and used in a molecular dynamics simulation on a solvated, neutralized system containing an AA9 protein, Cu2+ and a β-cellulose surface. The copper to cellulose interaction was evident during the dynamics, which could also be accelerated by the use of high Cu O van der Waals parameters. The interaction of AA9, Cu2+ and cellulose is described in detail.
- Full Text:
- Date Issued: 2017
Bioinformatic characterization of type-specific sequence and structural features in auxiliary activity family 9 proteins:
- Moses, Vuyani, Hatherley, Rowan, Tastan Bishop, Özlem
- Authors: Moses, Vuyani , Hatherley, Rowan , Tastan Bishop, Özlem
- Date: 2016
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/148358 , vital:38732 , DOI: 10.1186/s13068-016-0655-2
- Description: Due to the impending depletion of fossil fuels, it has become important to identify alternative energy sources. The biofuel industry has proven to be a promising alternative. However, owing to the complex nature of plant biomass, hence the degradation, biofuel production remains a challenge. The copper-dependent Auxiliary Activity family 9 (AA9) proteins have been found to act synergistically with other cellulose-degrading enzymes resulting in an increased rate of cellulose breakdown. AA9 proteins are lytic polysaccharide monooxygenase (LPMO) enzymes, otherwise known as polysaccharide monooxygenases (PMOs). They are further classified as Type 1, 2 or 3 PMOs, depending on the different cleavage products formed. As AA9 proteins are known to exhibit low sequence conservation, the analysis of unique features of AA9 domains of these enzymes should provide insights for the better understanding of how different AA9 PMO types function.
- Full Text:
- Date Issued: 2016
- Authors: Moses, Vuyani , Hatherley, Rowan , Tastan Bishop, Özlem
- Date: 2016
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/148358 , vital:38732 , DOI: 10.1186/s13068-016-0655-2
- Description: Due to the impending depletion of fossil fuels, it has become important to identify alternative energy sources. The biofuel industry has proven to be a promising alternative. However, owing to the complex nature of plant biomass, hence the degradation, biofuel production remains a challenge. The copper-dependent Auxiliary Activity family 9 (AA9) proteins have been found to act synergistically with other cellulose-degrading enzymes resulting in an increased rate of cellulose breakdown. AA9 proteins are lytic polysaccharide monooxygenase (LPMO) enzymes, otherwise known as polysaccharide monooxygenases (PMOs). They are further classified as Type 1, 2 or 3 PMOs, depending on the different cleavage products formed. As AA9 proteins are known to exhibit low sequence conservation, the analysis of unique features of AA9 domains of these enzymes should provide insights for the better understanding of how different AA9 PMO types function.
- Full Text:
- Date Issued: 2016
The development of computational biology in South Africa: successes achieved and lessons learnt
- Mulder, Nicola J, Christoffels, Alan, De Oliveira, Tulio, Gamieldien, Junaid, Hazelhurst, Scott, Joubert, Fourie, Kumuthini, Judit, Pillay, Ché S, Snoep, Jacky L, Tastan Bishop, Özlem, Tiffin, Nicki
- Authors: Mulder, Nicola J , Christoffels, Alan , De Oliveira, Tulio , Gamieldien, Junaid , Hazelhurst, Scott , Joubert, Fourie , Kumuthini, Judit , Pillay, Ché S , Snoep, Jacky L , Tastan Bishop, Özlem , Tiffin, Nicki
- Date: 2016
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/148347 , vital:38731 , DOI: 10.1371/journal.pcbi.1004395
- Description: Bioinformatics is now a critical skill in many research and commercial environments as biological data are increasing in both size and complexity. South African researchers recognized this need in the mid-1990s and responded by working with the government as well as international bodies to develop initiatives to build bioinformatics capacity in the country. Significant injections of support from these bodies provided a springboard for the establishment of computational biology units at multiple universities throughout the country, which took on teaching, basic research and support roles. Several challenges were encountered, for example with unreliability of funding, lack of skills, and lack of infrastructure. However, the bioinformatics community worked together to overcome these, and South Africa is now arguably the leading country in bioinformatics on the African continent. Here we discuss how the discipline developed in the country, highlighting the challenges, successes, and lessons learnt.
- Full Text:
- Date Issued: 2016
- Authors: Mulder, Nicola J , Christoffels, Alan , De Oliveira, Tulio , Gamieldien, Junaid , Hazelhurst, Scott , Joubert, Fourie , Kumuthini, Judit , Pillay, Ché S , Snoep, Jacky L , Tastan Bishop, Özlem , Tiffin, Nicki
- Date: 2016
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/148347 , vital:38731 , DOI: 10.1371/journal.pcbi.1004395
- Description: Bioinformatics is now a critical skill in many research and commercial environments as biological data are increasing in both size and complexity. South African researchers recognized this need in the mid-1990s and responded by working with the government as well as international bodies to develop initiatives to build bioinformatics capacity in the country. Significant injections of support from these bodies provided a springboard for the establishment of computational biology units at multiple universities throughout the country, which took on teaching, basic research and support roles. Several challenges were encountered, for example with unreliability of funding, lack of skills, and lack of infrastructure. However, the bioinformatics community worked together to overcome these, and South Africa is now arguably the leading country in bioinformatics on the African continent. Here we discuss how the discipline developed in the country, highlighting the challenges, successes, and lessons learnt.
- Full Text:
- Date Issued: 2016
Development of Bioinformatics Infrastructure for Genomics Research:
- Mulder, Nicola J, Adebiyi, Ezekiel, Adebiyi, Marion, Adeyemi, Seun, Ahmed, Azza, Ahmed, Rehab, Akanle, Bola, Alibi, Mohamed, Armstrong, Don L, Aron, Shaun, Ashano, Efejiro, Baichoo, Shakuntala, Benkahla, Alia, Brown, David K, Chimusa, Emile Rugamika, Fadlelmola, Faisal M, Falola, Dare, Fatumo, Segun, Ghedira, Kais, Ghouila, Amel, Hazelhurst, Scott, Itunuoluwa Isewon, Segun Jung, Kassim, Samar Kamal, Kayondo, Jonathan K, Mbiyavanga, Mamana, Meintjes, Ayton, Mohammed, Somia, Mosaku, Abayomi, Moussa, Ahmed, Muhammd, Mustafa, Mungloo-Dilmohamud, Zahra, Nashiru, Oyekanmi, Odia, Trust, Okafor, Adaobi, Oladipo, Olaleye, Osamor, Victor, Oyelade, Jellili, Sadki, Khalid, Salifu, Samson Pandam, Soyemi, Jumoke, Panji, Sumir, Radouani, Fouzia, Souiai, Oussama, Tastan Bishop, Özlem
- Authors: Mulder, Nicola J , Adebiyi, Ezekiel , Adebiyi, Marion , Adeyemi, Seun , Ahmed, Azza , Ahmed, Rehab , Akanle, Bola , Alibi, Mohamed , Armstrong, Don L , Aron, Shaun , Ashano, Efejiro , Baichoo, Shakuntala , Benkahla, Alia , Brown, David K , Chimusa, Emile Rugamika , Fadlelmola, Faisal M , Falola, Dare , Fatumo, Segun , Ghedira, Kais , Ghouila, Amel , Hazelhurst, Scott , Itunuoluwa Isewon , Segun Jung , Kassim, Samar Kamal , Kayondo, Jonathan K , Mbiyavanga, Mamana , Meintjes, Ayton , Mohammed, Somia , Mosaku, Abayomi , Moussa, Ahmed , Muhammd, Mustafa , Mungloo-Dilmohamud, Zahra , Nashiru, Oyekanmi , Odia, Trust , Okafor, Adaobi , Oladipo, Olaleye , Osamor, Victor , Oyelade, Jellili , Sadki, Khalid , Salifu, Samson Pandam , Soyemi, Jumoke , Panji, Sumir , Radouani, Fouzia , Souiai, Oussama , Tastan Bishop, Özlem
- Date: 2017
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/148239 , vital:38722 , DOI: 10.1016/j.gheart.2017.01.005
- Description: Although pockets of bioinformatics excellence have developed in Africa, generally, large-scale genomic data analysis has been limited by the availability of expertise and infrastructure. H3ABioNet, a pan-African bioinformatics network, was established to build capacity specifically to enable H3Africa (Human Heredity and Health in Africa) researchers to analyze their data in Africa. Since the inception of the H3Africa initiative, H3ABioNet's role has evolved in response to changing needs from the consortium and the African bioinformatics community.
- Full Text:
- Date Issued: 2017
- Authors: Mulder, Nicola J , Adebiyi, Ezekiel , Adebiyi, Marion , Adeyemi, Seun , Ahmed, Azza , Ahmed, Rehab , Akanle, Bola , Alibi, Mohamed , Armstrong, Don L , Aron, Shaun , Ashano, Efejiro , Baichoo, Shakuntala , Benkahla, Alia , Brown, David K , Chimusa, Emile Rugamika , Fadlelmola, Faisal M , Falola, Dare , Fatumo, Segun , Ghedira, Kais , Ghouila, Amel , Hazelhurst, Scott , Itunuoluwa Isewon , Segun Jung , Kassim, Samar Kamal , Kayondo, Jonathan K , Mbiyavanga, Mamana , Meintjes, Ayton , Mohammed, Somia , Mosaku, Abayomi , Moussa, Ahmed , Muhammd, Mustafa , Mungloo-Dilmohamud, Zahra , Nashiru, Oyekanmi , Odia, Trust , Okafor, Adaobi , Oladipo, Olaleye , Osamor, Victor , Oyelade, Jellili , Sadki, Khalid , Salifu, Samson Pandam , Soyemi, Jumoke , Panji, Sumir , Radouani, Fouzia , Souiai, Oussama , Tastan Bishop, Özlem
- Date: 2017
- Language: English
- Type: text , article
- Identifier: http://hdl.handle.net/10962/148239 , vital:38722 , DOI: 10.1016/j.gheart.2017.01.005
- Description: Although pockets of bioinformatics excellence have developed in Africa, generally, large-scale genomic data analysis has been limited by the availability of expertise and infrastructure. H3ABioNet, a pan-African bioinformatics network, was established to build capacity specifically to enable H3Africa (Human Heredity and Health in Africa) researchers to analyze their data in Africa. Since the inception of the H3Africa initiative, H3ABioNet's role has evolved in response to changing needs from the consortium and the African bioinformatics community.
- Full Text:
- Date Issued: 2017