Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Mohsin Vahid Khan"'
Publikováno v:
International Journal of Biological Macromolecules. 112:217-229
The newly synthesized unfolded polypeptide attains its functional and unique three-dimensional conformation through the process of protein folding for which several models have been proposed. The protein misfolding diseases include Alzheimer's, Parki
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c1c0c6e12ebfbac5619126a8926e3850
https://doi.org/10.1016/j.ijbiomac.2018.01.099
https://doi.org/10.1016/j.ijbiomac.2018.01.099
Autor:
Mohsin Vahid Khan, Rizwan Hasan Khan, Mohammad Khursheed Siddiqi, Parvez Alam, Saima Nusrat, Sadia Malik, Sumit Kumar Chaturvedi
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1866:549-557
Protein aggregation and amyloid fibrillation are responsible for several serious pathological conditions (like type II diabetes, Alzheimer's and Parkinson's diseases etc.) and protein drugs ineffectiveness. Therefore, a molecule that can inhibit the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5cfb291c514c8dfea79323e06fd1c92a
https://doi.org/10.1016/j.bbapap.2018.02.005
https://doi.org/10.1016/j.bbapap.2018.02.005
Autor:
Maroof Ali, Mohsin Vahid Khan, Mohd Ishtikhar, Masihuz Zaman, Gulam Rabbani, Tajalli Ilm Chandel, Rizwan Hasan Khan
Publikováno v:
International Journal of Biological Macromolecules. 106:1115-1129
This review article summarises the possible mechanisms of the protein-ligand interaction, folding, misfolding, aggregation and inhibition of protein aggregates. Under certain stressed condition the folding process deviates from its path and results i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::746ab6adc354cf003bf281ab8e89e30b
https://doi.org/10.1016/j.ijbiomac.2017.07.185
https://doi.org/10.1016/j.ijbiomac.2017.07.185
Autor:
Rizwan Hasan Khan, Mohsin Vahid Khan, Arif Tasleem Jan, Inho Choi, Mohammad Hassan Baig, Gulam Rabbani, Masihuz Zaman, Eun Ju Lee, Abd-ElAziem Farouk
Publikováno v:
International Journal of Biological Macromolecules. 105:1572-1580
Erucic acid (EA) is one of the key fatty acids usually found in canola oil, mustard oil and rapeseed oil. Consumption of EA in primates was found to cause myocardial lipidosis and cardiac steatosis. To have an insight of the effect of EA in humans, w
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::056e945858f2824875e3e05077c0b3e2
https://doi.org/10.1016/j.ijbiomac.2017.04.051
https://doi.org/10.1016/j.ijbiomac.2017.04.051
Autor:
Masihuz Zaman, Ali S. Abdelhameed, Mohsin Vahid Khan, Mohammad Khursheed Siddiqui, Tajalli Ilm Chandel, Rizwan Hasan Khan, Mohd Rehan Ajmal
Publikováno v:
Journal of Biomolecular Structure and Dynamics. 36:2543-2557
Protein aggregation into oligomers and mature fibrils are associated with more than 20 diseases in humans. The interactions between cationic surfactants dodecyltrimethylammonium bromide (DTAB) and tetradecyltrimethylammonium bromide (TTAB) with varyi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a78d49e3ffc2487b15cf1f675330974
https://doi.org/10.1080/07391102.2017.1363085
https://doi.org/10.1080/07391102.2017.1363085
Autor:
Ali S. Abdelhameed, Masihuz Zaman, Mohd Rehan Ajmal, Mohammad Khursheed Siddiqui, Yasser E. Shahein, Rizwan Hasan Khan, Mohd Ishtikhar, Mohsin Vahid Khan, Nabeela Majid, Tajalli Ilm Chandel
Publikováno v:
Journal of Biomolecular Structure and Dynamics. 36:1261-1273
The aggregation phenomenon (amyloid and amorphous) is associated with several pathological complications in human, such as Alzheimer's, Parkinson's, Huntington, Cataract diseases, and Diabetes mellitus type 2. In the present study we are offering evi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f2a758f37645168239dce751915c9ca2
https://doi.org/10.1080/07391102.2017.1318718
https://doi.org/10.1080/07391102.2017.1318718
Autor:
Rizwan Hasan Khan, Ali S. Abdelhameed, Mohsin Vahid Khan, Gulam Rabbani, Masihuz Zaman, Mohd Ishtikhar
Publikováno v:
International Journal of Biological Macromolecules
Highlights • Conalbumin aggregates at 65 °C and denaturation occur at above this temperature. • The nature of aggregates was identified as amorphous. • The polyols inhibits the aggregation of conalbumin via protecting the secondary structure.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::90763f6bf952a967f6a75f017ef36214
https://doi.org/10.1016/j.ijbiomac.2016.10.023
https://doi.org/10.1016/j.ijbiomac.2016.10.023
Autor:
Mohsin Vahid Khan, Saima Nusrat, Sumit Kumar Chaturvedi, Mohd Khursheed Siddiqi, Rizwan Hasan Khan, Parvez Alam, Sadia Malik
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1868:140407
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c8112fc5940e3216527e76bceebe80c9
https://doi.org/10.1016/j.bbapap.2020.140407
https://doi.org/10.1016/j.bbapap.2020.140407
Autor:
Sumit Kumar Chaturvedi, Mohsin Vahid Khan, Nabeela Majid, Vladimir N. Uversky, Sadia Malik, Parvez Alam, Mohammad Khursheed Siddiqi, Mohd Rehan Ajmal, Sudeepa Rajan, Rizwan Hasan Khan
Publikováno v:
Journal of cellular biochemistry.
Amyloid fibrillation is associated with several human maladies, such as Alzheimer's, Parkinson's, Huntington's diseases, prions, amyotrophic lateral sclerosis, and type 2 diabetes diseases. Gaining insights into the mechanism of amyloid fibril format
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d7868e95c92593929f4a5b1ada835be6
https://pubmed.ncbi.nlm.nih.gov/30242891
https://pubmed.ncbi.nlm.nih.gov/30242891
Publikováno v:
RSC Advances. 5:20115-20131
The effect of pH on the conformational behavior of Candida antartica lipase B (CaLB) has been monitored by spectroscopic and calorimetric studies. The results obtained from far and near-UV CD, intrinsic fluorescence and ANS binding studies indicate t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a7aaf5a897580a6e0870b37a5e37f08b
https://doi.org/10.1039/c4ra17093h
https://doi.org/10.1039/c4ra17093h