New Springer Book: Molecular Dynamics and Optimization Studies of α-Synuclein Protein Structures
https://link.springer.com/book/10.1007/978-981-10-8815-5
https://link.springer.com/book/10.1007/978-94-017-7318-8
https://link.springer.com/book/9783031367724
https://youtu.be/ikL0gh7jYJM, https://youtu.be/5PrSq-xBr5Y
Zhang JP (2025) 张家普博士百篇科普论文集(卷一),II+xx+565页, https://youtu.be/qVJv2h8m4f4, ⓒsciencenet.
Teaching experiences
1. Theory of Computation
2. Advanced Algebra
3. Mathematics Modeling
4. Model Building and Solving and Software
5. Programming Languages, and Data Structures
6. Computing Chemistry and Advanced Organic Chemistry
7. Tutoring experiences in many courses of Mathematics, Statistics, and Computer Computing
8. ..
Publications
PhD thesis
Zhang JP, Derivative-Free Hybrid Methods in Global Optimization and Their Applications, PhD thesis, The University of Ballarat (Australia), February 2005. (Identifier http://researchonline.federation.edu.au/vital/access/HandleResolver/1959.17/34054
Identifier vital:3522 Identifier https://library.federation.edu.au/search/a?searchtype=t&searcharg=Derivative-free+hybrid+methods+in+global+optimization+and+their+&searchscope=4&SORT=D) "Revolutionary optimization methods that pushed the boundaries of global optimization, forever changing the game." - a review from KW.
MSc thesis
Zhang JP, A global and superlinearly convergent algorithm for nonlinear nondifferential convex programming problems with a generalized Armijo line-search, Masters (rsearch) degree thesis, Institute of Operations Research (at Qufu Normal University China), 1996, arXiv1309.0931
Springer Monographs - (Reviews-from中国海洋大学.PDF)
Zhang JP (2026) Molecular Dynamics and Optimization Studies of α-Synuclein Protein Structures - Mechanism Underlying the Parkinson's Disease and Movement Disorders,
Zhang JP (2023) Optimization-based Molecular Dynamics Studies of SARS-CoV-2 Molecular Structures - Research on COVID-19, Springer Cham, ISBN 978-3-031-36772-4, xx+953 pages, NLM Unique ID 9918863688806676. (Hardcover ISBN 978-3-031-36772-4 published on 17/10/2023, Softcover ISBN 978-3-031-36775-5 published on 30/10/2024, eBook ISBN 978-3-031-36773-1 published on 16/10/2023, DOI: 10.1007/978-3-031-36773-1). A book review from ACM Computing Reviews
https://www.computingreviews.com/review/review_review.cfm?review_id=147951; Support Material 1
Zhang JP (2018) Molecular Dynamics Analyses of Prion Protein Structures - The Resistance to Prion Diseases Down Under, Springer Singapore, ISBN 978-981-10-8814-8, xxix+375 pages, NLM Unique ID 101746134. (Hardcover ISBN 978-981-10-8814-8 published on 07/08/2018, Softcover ISBN 978-981-13-4247-9 published on 23/12/2018, eBook ISBN 978-981-10-8815-5 published on 20/07/2018, MyCopy softcover ISBN 978-981-10-8816-2, DOI: 10.1007/978-981-10-8815-5) "Unlocking the secrets of prion proteins, revealing insights into the resistance against prion disesese." - a review from KW
Zhang JP (2015) Molecular Structures and Structural Dynamics of Prion Proteins and Prions - Mechanism Underlying the Resistance to Prion Diseases, Springer Dordrecht, ISBN 978-94-017-7317-1, xix+355 pages (Association for Computing Machinery wrote 2 pages' Book Review), NLM Unique ID 101676710. (Hardcover ISBN 978-94-017-7317-1 published on 25/09/2015, Softcover ISBN 978-94-024-0445-6 published on 29/10/2016, eBook ISBN 978-94-017-7318-8 published on 14/09/2015, MyCopy softcover ISBN 978-94-017-7319-5, DOI: 10.1007/978-94-017-7318-8). A book review from ACM Computing Reviews
https://www.computingreviews.com/review/review_review.cfm?review_id=144750
Journal Papers (selected)
Zhang JP (2024) Classifications of Mathematical Studies of Prion(s).
This article is to do research on the classifications of prions in the MathSciNet database. Observations from the discussion of this article allow us to obtain at least six classes of MathSciNet study for prion(s). These classes are at different levels of study: (i) at disease population level, (ii) at brain or neurons-nerves-or-spine level, (iii) at cell level, (iv) at molecule level, (v) at polymer level, and (vi) with presence of others. These classifications may be helpful to us for the prion disease treatments.
(i) At disease population level [1, 13, 19, 31, 33, 47, 49], the populations of Sup35 prion yeast [1], with Parkinson’s disease (PD) [13], prion Creutzfeldt-Jacob Disease (CJD) [19], Chronic wasting disease (CWD) [33], etc. are studied. (ii) The studies at at brain or neurons-nerves-or-spine level can be seen from [3, 5, 2, 42-43, 59]. (iii) The studies at cell level are mainly considering yeast prion cells [20, 34, 36, 38, 48, 60]. Most of the models are in the class that is at molecule level [2, 14, 15, 16, 21, 23, 25, 27-29, 37,40-41, 44, 46, 50-57, 61]; some models are prions in the presence of chaperone [4, 6, 8, 11, 24, 51], interferons [10], suPrP [12], strains/variants [17, 22, 35, 40, 45, 46], interacting with Aβ [7, 13, 18, 30], and evolution with impulse effects [32]; prions are also used as a test/detecting/diagnosis to MD, optimization, PMCA technologies [9, 26, 35, 39].
Zhang JP (2024) Molecular dynamics, optimisation, and AlphaFold studies of wild-type frog prion proteins (frog-PrPCs), (invited paper).
In Section 5.3 of Springer eBook ISBN 978-981-10-8815-5 entitled "Molecular Dynamics Analyses of Prion Protein Structures", the molecular dynamics (MD) studies on the NMR structure of African clawed frog (Xenopus laevis) prion protein (frog-PrPC, with PDB entry 1XU0) are presented; where the author found that for frog-PrPC its α-helix 1 is not stable and the two β-strands are longer than usual. This research article is to present furthermore MD, optimisation, and AlphaFold results of frog-PrPCs.
Zhang JP (2024) Molecular dynamics and optimization studies of horse prion protein wild type and its S167D mutant (invited paper), arXiv:2110.00365, MDPI journal Zoonotic Diseases 4(3): 187-200, DOI:10.3390/zoonoticdis4030017. https://www.mdpi.com/2813-0227/4/3/17 Études de dynamique moléculaire de la protéine prion de cheval de type sauvage et de son mutant S167D By Jiapu Zhang Les maladies à prions, ou encéphalopathies spongiformes transmissibles (EST), sont des maladies neurodégénératives mortelles. Cependant, la maladie à prions n'a pas été signalée chez les chevaux jusqu'à présent; par conséquent, les chevaux sont connus pour être une espèce résistante aux maladies à prions. Le résidu S167 dans la protéine prion du cheval a été cité comme résidu protecteur essentiel pour les chevaux contre les maladies à prions. Comprendre la dynamique conformationnelle des protéines prions est essentiel pour développer des thérapies efficaces. Cet article vise à faire des études de dynamique moléculaire sur la protéine prion de cheval de type sauvage (WT) et son mutant S167D (Mutant) pour comprendre leur dynamique conformationnelle; des résultats intéressants seront discutés. Молекулярно-динамические исследования прионного белка лошади дикого типа и его мутанта S167D By Jiapu Zhang Прионные заболевания, или так называемые трансмиссивные губчатые энцефалопатии (ТГЭ), являются смертельными нейродегенеративными заболеваниями. Однако до настоящего времени о прионных заболеваниях у лошадей не сообщалось, поэтому известно, что лошади являются видом, устойчивым к прионным заболеваниям. Остаток S167 в прионном белке лошади считается важнейшим защитным элементом для лошадей от прионных заболеваний. Понимание конформационной динамики прионных белков является ключом к разработке эффективных методов лечения. Цель этой статьи - провести молекулярно-динамические исследования лошадиного прионного белка дикого типа (WT) и его мутанта S167D (Mutant), чтобы понять их конформационную динамику; будут обсуждаться интересные результаты. Prion diseases or called transmissible spongiform encephalopathies are fatal neurodegenerative diseases characterised by the accumulation of an abnormal prion protein isoform (rich in beta-sheets - about 30% alpha-helix and 43% beta-sheet), which is converted from the normal prion protein (predominant in alpha-helix - about 42% alpha-helix and 3% beta-sheet). However, prion disease has not been reported in horses up to now; therefore, horses are known to be a species resistant to prion diseases. Residue S167 in horse has been cited as critical protective residue for encoding prion protein conformational stability in prion-resistance. According to the protein-only hypothesis, abnormal prion protein is responsible for both spongiform degeneration of the brain and disease transmissibility. Thus, understanding the conformational dynamics of abnormal prion protein from normal prion protein is a key to developing effective therapies. This article is to do molecular dynamics and optimization studies on the horse normal prion protein wild-type and its S167D mutant respectively to understand their conformational dynamics and optimized confirmation; interesting results will be discussed. 野生型马朊病毒蛋白及其突变体S167D的分子动力学研究 by Jiapu Zhang 朊病毒病或传染性海绵状脑病 (TSE) 是致命的神经退行性疾病。然而，迄今为止，还没有关于马感染朊病毒病的报道。因此，马被认为是对朊病毒疾病有抵抗力的物种。马朊病毒蛋白中的残基S167被认为是马对抗朊病毒疾病的重要保护残基。了解朊病毒蛋白的构象动力学对于开发有效的疗法至关重要。本文旨在对野生型（WT）马朊病毒蛋白及其突变体S167D（Mutant）进行分子动力学研究，了解其构象动力学；将讨论有趣的结果。Molekulardynamische Untersuchungen des Pferde-Prionenproteins Wildtyp und seiner S167D-Mutante by Jiapu Zhang Prionenkrankheiten oder transmissible spongiforme Enzephalopathien (TSE) genannt, sind tödliche neurodegenerative Erkrankungen. Eine Prionenkrankheit wurde jedoch bisher bei Pferden nicht gemeldet; Daher ist bekannt, dass Pferde eine Spezies sind, die gegen Prionenkrankheiten resistent ist. Der Rückstand S167 im Prionenprotein von Pferden wurde als kritischer Schutzrückstand für Pferde gegen Prionenkrankheiten angeführt. Das Verständnis der Konformationsdynamik von Prionproteinen ist der Schlüssel zur Entwicklung wirksamer Therapien. Dieser Artikel soll molekulardynamische Studien am Pferde-Prionenprotein-Wildtyp (WT) und seiner S167D-Mutante (Mutante) durchführen, um ihre Konformationsdynamik zu verstehen; Interessante Ergebnisse werden diskutiert. Estudios de dinámica molecular de la proteína priónica de caballo de tipo salvaje y su mutante S167D by Jiapu Zhang. Las enfermedades priónicas, o llamadas encefalopatías espongiformes transmisibles (EET), son enfermedades neurodegenerativas fatales. Sin embargo, hasta ahora no se ha informado de enfermedades priónicas en caballos; por lo tanto, se sabe que los caballos son una especie resistente a las enfermedades priónicas. El residuo S167 en la proteína priónica de caballo se ha citado como residuo protector crítico para caballos contra enfermedades priónicas. Comprender la dinámica conformacional de las proteínas priónicas es clave para desarrollar terapias efectivas. El objetivo de este artículo es realizar estudios de dinámica molecular en la proteína priónica de caballo de tipo silvestre (WT) y su mutante S167D (Mutante) para comprender su dinámica conformacional; se discutirán resultados interesantes./ウマプリオン蛋白質野生型とそのS167D変異体の分子動力学と最適化研究 by Jiapu Zhang 感染性海綿状脳症と呼ばれるプリオン病は,正常なプリオン蛋白質(主にαヘリックス~約42%のαヘリックスと3%のβシート)から変換される異常なプリオン蛋白質アイソフォーム(βシート~約30%のαヘリックスと43%のβシートに富む)の蓄積により特徴付けられる致死的神経変性疾患である。しかし,プリオン病は現在までウマで報告されていない;したがって,ウマはプリオン病に抵抗性の種であることが知られている。ウマの残基S167はプリオン耐性におけるプリオン蛋白質立体配座安定性をコードする重要な保護残基として挙げられている。蛋白質のみの仮説によると,異常なプリオン蛋白質は脳の海綿状変性と疾患伝達性の両方に関与する。したがって,正常プリオン蛋白質由来の異常プリオン蛋白質の立体配座動力学の理解は効果的な治療法開発の鍵である。本論文は,ウマ正常プリオン蛋白質野生型とそのS167D突然変異体に関する分子動力学と最適化研究を,それぞれ,それらの立体配座動力学を理解し,確認を最適化することである。興味深い結果を論じた。
Zhang JP (2023) Two polar contacts between GLU290 and ARG4 linking the two monomers of SARS-CoV-2 3CLpro, arXiv: 5182254. Current Topics in Biotechnology 14: 19-33. RT/BT/151, http://www.researchtrends.net/tia/abstract.asp?in=0&vn=14&tid=48&aid=7232&pub=2023&type=3
Zhang JP (2021) Molecular dynamics studies of dog prion protein wild-type and its D159N mutant, Journal of Biomolecular Structure and Dynamics 39 (12): 4234-4242, PMID 32496928, DOI: 10.1080/07391102.2020.1776155. https://www.tandfonline.com/eprint/XEJ6FRKGEUFFY8IM6R7A/full?target=10.1080/07391102.2020.1776155
Zhang JP (2020) Molecular dynamics studies of the bufallo prion protein structured region at higher temperatures, The Open Bioinformatics Journal 13: 129-136. DOI: 10.2174/1875036202013010129 (Associate Editorial Board Membership annual paper) https://benthamopen.com/contents/pdf/TOBIOIJ/TOBIOIJ-13-129.pdf, https://youtu.be/5PrSq-xBr5Y
Zhang JP (2020) The classical Minkowski problem: an optimization description, Asia-Pacific Journal of Mathematics and Statistics 2(1):1-4, DOI: 10.11648/10045508 (Editorial Board Membership paper)
Zhang JP (2019) The polar clasps of a bank vole PrP(168–176) prion protofibril revisiting, Journal of Molecular Modeling 25 (5) 108, PMID 30937536, DOI: 10.1007/s00894-019-3981-z https://rdcu.be/buml4
Zhang JP (2018) Molecular Dynamics Analyses of Prion Protein Structures (1st ed. 2018 Edition) Springer, ISBN 978-981-10-8814-8, 2018, DOI: 10.1007/978-981-10-8815-5, NLM ID 101746134.
Zhang JP, Chatterjee S, Wang F (2017) Using graph theory and optimization theory to do data mining the large-scale buffalo prion protein structure database, Operations Research Transactions 21 (2) 73-83, DOI: 10.15960/j.cnki.issn.1007-6093.2017.02.009
Zhang JP, Wang F (2016) A review on the salt bridge ASP177-ARG163 (O-N) of wild-type rabbit prion protein, Journal of Biomolecular Structure and Dynamics 34 (5) 1020-1028, PMID 26103085, DOI: 10.1080/07391102.2015.1064832. arXiv1408.5269
Zhang JP, Chatterjee S, Wang F (2016) Molecular dynamics studies on the buffalo prion protein, Journal of Biomolecular Structure and Dynamics 34 (4) 762-777, PMID 26043781, DOI: 10.1080/07391102.2015.1052849. arXiv1503.00051
Zhang JP, Wang F, Zhang YL (2015) Molecular dynamics studies on the NMR structures of rabbit prion protein wild type and mutants: surface electrostatic charge distributions, Journal of Biomolecular Structure and Dynamics 33 (6) 1326-1335, PMID 25105226, DOI: 10.1080/07391102.2014.947325. arXiv1407.6221
Zhang JP (2015) Molecular Structures and Structural Dynamics of Prion Proteins and Prions, Springer, ISBN 978-94-017-7317-1, 2015, DOI: 10.1007/978-94-017-7318-8, NLM ID 101676710.
Zhang JP, Zhang YL (2014) Molecular dynamics studies on the NMR and X-ray structures of rabbit prion proteins, Journal of Theoretical Biology 343 (1) 70-82, PMID 24184221, DOI: 10.1016/j.jtbi.2013.10.005. arXiv1304.7633
Zhang JP, Wang F (2014) A survey and a molecular dynamics study on the (central) hydrophobic region of prion proteins, Current Pharmaceutical Biotechnology 15 (11) 1026-1048, PMID 25373387, DOI: 10.2174/1389201015666141103020004 https://youtu.be/ikL0gh7jYJM. arXiv1409.6104
Zhang JP, Zhang YL (2013) Molecular dynamics studies on 3D structures of the hydrophobic region PrP(109-136), Acta Biochimica et Biophysica Sinica 45(6) 509-519, PMID 23563221, DOI: 10.1093/abbs/gmt031 Free. arXiv1301.0117
Zhang JP, Hou YT, Wang YJ, Wang CY, Zhang XS (2012) The LBFGS quasi-Newtonian method for molecular modeling prion AGAAAAGA amyloid fibrils, Natural Science 4(12A) 1097-1108, DOI: 10.4236/ns.2012.412A138. arXiv1206.1755
Zhang JP (2011) The structural stability of wild-type horse prion protein, Journal of Biomolecular Structure and Dynamics 29 (2) 369-377, PMID 21875155, DOI: 10.1080/07391102.2011.10507391. arXiv1104.4616
Zhang JP, Gao DY, Yearwood J (2011) A novel canonical dual computational approach for prion AGAAAAGA amyloid fibril molecular modeling, Journal of Theoretical Biology 284 (1) 149-157, PMID 21723301, DOI: 10.1016/j.jtbi.2011.06.024. arXiv1107.4104
Zhang JP, Sun J, Wu CZ (2011) Optimal atomic-resolution structures of prion AGAAAAGA amyloid fibrils, Journal of Theoretical Biology 279 (1) 17-28, PMID 21420420, DOI: 10.1016/j.jtbi.2011.02.012. arXiv1012.2504
Zhang JP, Liu DDW (2011) Molecular dynamics studies on the structural stability of wild-type dog prion protein, Journal of Biomolecular Structure and Dynamics 28 (6) 861-869, PMID 21469747, DOI: 10.1080/07391102.2011.10508613
Zhang JP (2011) An effective simulated annealing refined replica exchange Markov chain Monte Carlo Algorithm for the infectious disease model of H1N1 influenza pandemic, World Journal of Modelling and Simulation 7(1) 29-39.
Zhang JP (2011) Comparison studies of the structural stability of rabbit prion protein with human and mouse prion proteins, Journal of Theoretical Biology 269(1) 88-95, PMID 20970434, DOI: 10.1016/j.jtbi.2010.10.020
Zhang JP (2011) Optimal molecular structures of prion AGAAAAGA amyloid fibrils formatted by simulated annealing, Journal Molecular Modelling 17 (1) 173-179, PMID 20411399, DOI: 10.1007/s00894-010-0691-y
Zhang JP (2010) Studies on the structural stability of rabbit prion protein probed by molecular dynamics simulations of its wild-type and mutants, Journal of Theoretical Biology 264 (1) 119-122, PMID 20109469, DOI: 10.1016/j.jtbi.2010.01.024
Bagirov AM, Rubinov AM, Zhang JP (2009) A multidimensional descent method for global optimization, Optimization 58 (5) 611-625, DOI: 10.1080/02331930902943483
Zhang JP (2009) Studies on the structural stability of rabbit prion protein probed by molecular dynamics simulations, Journal of Biomolecular Structure and Dynamics 27 (2) 159-162, PMID 19583441, DOI: 10.1080/07391102.2009.10507305. with corrections
Bagirov AM, Rubinov AM, Zhang JP (2005) Local optimization method with global multidimensional search, Journal of Global Optimization 32 (2) 161-179, DOI: 10.1007/s10898-004-2700-0.
Ghosh R, Rubinov AM, Zhang JP (2005) Optimization approach for clustering datasets with weights, Optimization Methods and Software 20 335-351, DOI: 10.1080/10556780512331318191
Bagirov AM, Rubinov AM, Zhang JP (2004) Local Optimization Method with Global Multidimensional Search for Descent, Optimization Online 2004. http://www.optimization-online.org/DB_FILE/2004/01/808.pdf
Abbass HA, Bagirov AM, Zhang JP (2003) The discrete gradient evolutionary strategy method for global optimization, IEEE The 2003 Congress on Evolutionary Computation, 2003 (CEC '03) Vol 1, pp. 435-442, DOI: 10.1109/CEC.2003.1299608
Bagirov AM, Zhang JP (2003) Comparative analyses of the cutting angle and simulated annealing methods in global optimization, Optimization 52 (4-5) 363-378, DOI: 10.1080/02331930310001611565
Sun J, Zhang JP (2001) Global convergence of conjugate gradient methods without line search, Annals of Operations Research 103 161-173 DOI: 10.1023/A:1012903105391
Ten short articles invited and published by some open access journals:
Five invited book-chapters by the NOVA Science Publishers:
Two invited book-chapters by the InTech Open Publisher (http://www.intechopen.com/):
Some Papers Linking PubMed:
Molecular dynamics studies of dog prion protein wild-type and its D159N mutant.
Zhang J. J Biomol Struct Dyn. 2021 Aug;39(12):4234-4242. doi: 10.1080/07391102.2020.1776155. Epub 2020 Jun 16.
PMID: 32496928 https://www.tandfonline.com/eprint/XEJ6FRKGEUFFY8IM6R7A/full?target=10.1080/07391102.2020.1776155
The polar clasps of a bank vole PrP(168-176) prion protofibril revisiting.
Zhang J. J Mol Model. 2019 Apr 2;25(5):108. doi: 10.1007/s00894-019-3981-z.
PMID: 30937536 https://rdcu.be/buml4
A review on the salt bridge ASP177-ARG163 (O-N) of wild-type rabbit prion protein.
Zhang J, Wang F. J Biomol Struct Dyn. 2016 May;34(5):1020-8. doi: 10.1080/07391102.2015.1064832. Epub 2016 Jan 26.
PMID: 26103085
Molecular dynamics studies on the buffalo prion protein.
Zhang J, Wang F, Chatterjee S. J Biomol Struct Dyn. 2016;34(4):762-77. doi: 10.1080/07391102.2015.1052849. Epub 2015 Jul 10.
PMID: 26043781
A survey and a molecular dynamics study on the (central) hydrophobic region of prion proteins.
Zhang J, Wang F. Curr Pharm Biotechnol. 2014;15(11):1026-48. doi: 10.2174/1389201015666141103020004.
PMID: 25373387 https://youtu.be/ikL0gh7jYJM
Molecular dynamics studies on the NMR structures of rabbit prion protein wild type and mutants: surface electrostatic charge distributions.
Zhang J, Wang F, Zhang Y. J Biomol Struct Dyn. 2015;33(6):1326-35. doi: 10.1080/07391102.2014.947325. Epub 2014 Aug 8.
PMID: 25105226
Molecular dynamics studies on the NMR and X-ray structures of rabbit prion proteins.
Zhang J, Zhang Y. J Theor Biol. 2014 Feb 7;342:70-82. doi: 10.1016/j.jtbi.2013.10.005. Epub 2013 Oct 31.
PMID: 24184221
Molecular dynamics studies on 3D structures of the hydrophobic region PrP(109-136).
Zhang J, Zhang Y. Acta Biochim Biophys Sin (Shanghai). 2013 Jun;45(6):509-19. doi: 10.1093/abbs/gmt031. Epub 2013 Apr 5.
The structural stability of wild-type horse prion protein.
Zhang J. J Biomol Struct Dyn. 2011 Oct;29(2):369-77. doi: 10.1080/07391102.2011.10507391.
PMID: 21875155
A novel canonical dual computational approach for prion AGAAAAGA amyloid fibril molecular modeling.
Zhang J, Gao DY, Yearwood J. J Theor Biol. 2011 Sep 7;284(1):149-57. doi: 10.1016/j.jtbi.2011.06.024. Epub 2011 Jun 28.
PMID: 21723301
Molecular dynamics studies on the structural stability of wild-type dog prion protein.
Zhang J, Liu DD. J Biomol Struct Dyn. 2011 Jun;28(6):861-9. doi: 10.1080/07391102.2011.10508613.
PMID: 21469747
Optimal atomic-resolution structures of prion AGAAAAGA amyloid fibrils.
Zhang J, Sun J, Wu C. J Theor Biol. 2011 Jun 21;279(1):17-28. doi: 10.1016/j.jtbi.2011.02.012. Epub 2011 Mar 21.
PMID: 21420420
Comparison studies of the structural stability of rabbit prion protein with human and mouse prion proteins.
Zhang J. J Theor Biol. 2011 Jan 21;269(1):88-95. doi: 10.1016/j.jtbi.2010.10.020. Epub 2010 Oct 21.
PMID: 20970434
Optimal molecular structures of prion AGAAAAGA amyloid fibrils formatted by simulated annealing.
Zhang J. J Mol Model. 2011 Jan;17(1):173-9. doi: 10.1007/s00894-010-0691-y. Epub 2010 Apr 22.
PMID: 20411399
Studies on the structural stability of rabbit prion probed by molecular dynamics simulations of its wild-type and mutants.
Zhang J. J Theor Biol. 2010 May 7;264(1):119-22. doi: 10.1016/j.jtbi.2010.01.024. Epub 2010 Jan 28.
PMID: 20109469
Studies on the structural stability of rabbit prion probed by molecular dynamics simulations.
Zhang J. J Biomol Struct Dyn. 2009 Oct;27(2):159-62. doi: 10.1080/07391102.2009.10507305.
PMID: 19583441
In Japanese
イヌプリオンタンパク質野生型とそのD159N変異体の分子動力学研究
Molecular Dynamics Studies of Dog Prion Protein Wild-type and Its D159N Mutant. Zhang Jiapu. Journal of biomolecular structure & dynamics(J. Biomol. Struct. Dyn.)2020Jun04
銀行のボールPRP（168-176）プリオンプロトフィブリルの再訪の極地留め金
The polar clasps of a bank vole PrP(168-176) prion protofibril revisiting. Zhang Jiapu. Journal of molecular modeling(J Mol Model)2019Apr02
野生型ウサギプリオンタンパク質の塩橋Asp177-Arg163（O - N）のレビュー
A review on the salt bridge ASP177-ARG163 (O-N) of wild-type rabbit prion protein. Zhang Jiapu, Wang Feng. Journal of biomolecular structure & dynamics(J Biomol Struct Dyn)2016May01
バッファロープリオンタンパク質の分子動力学研究
Molecular dynamics studies on the buffalo prion protein. Zhang Jiapu, Wang Feng, Chatterjee Subhojyoti. Journal of biomolecular structure & dynamics(J. Biomol. Struct. Dyn.)2016
プリオンタンパク質の（中央）疎水性領域に関する調査と分子動力学研究
A survey and a molecular dynamics study on the (central) hydrophobic region of prion proteins. Zhang Jiapu, Wang Feng. Current pharmaceutical biotechnology(Curr Pharm Biotechnol)2014
ウサギプリオンタンパク質野生型および変異体のNMR構造に関する分子動力学研究：表面静電荷分布。
Molecular dynamics studies on the NMR structures of rabbit prion protein wild type and mutants: surface electrostatic charge distributions. Zhang Jiapu, Wang Feng, Zhang Yuanli. Journal of biomolecular structure & dynamics(J. Biomol. Struct. Dyn.)2015
ウサギプリオンタンパク質のNMRおよびX線構造に関する分子動力学研究
Molecular dynamics studies on the NMR and X-ray structures of rabbit prion proteins. Zhang Jiapu, Zhang Yuanli. Journal of theoretical biology(J. Theor. Biol.)2014Feb07
疎水性領域PRP（109~136）の3D構造に関する分子動力学研究
Molecular dynamics studies on 3D structures of the hydrophobic region PrP(109-136). Zhang Jiapu, Zhang Yuanli. Acta biochimica et biophysica Sinica(Acta Biochim. Biophys. Sin. (Shanghai))2013Jun01
野生型馬プリオンタンパク質の構造安定性
The structural stability of wild-type horse prion protein. Zhang Jiapu. Journal of biomolecular structure & dynamics(J. Biomol. Struct. Dyn.)2011Oct01
プリオンAGAAAAGAアミロイドフィブリル分子モデリングのための新しい標準的な二重計算アプローチ。
A novel canonical dual computational approach for prion AGAAAAGA amyloid fibril molecular modeling. Zhang Jiapu, Gao David Y, Yearwood John. Journal of theoretical biology(J. Theor. Biol.)2011Sep07
野生型イヌプリオンタンパク質の構造安定性に関する分子動力学研究
Molecular dynamics studies on the structural stability of wild-type dog prion protein. Zhang Jiapu, Liu David D W. Journal of biomolecular structure & dynamics(J. Biomol. Struct. Dyn.)2011Jun01
プリオンAGAAAAGAアミロイドフィブリルの最適な原子分解能構造。
Optimal atomic-resolution structures of prion AGAAAAGA amyloid fibrils. Zhang Jiapu, Sun Jie, Wu Changzhi. Journal of theoretical biology(J. Theor. Biol.)2011Jun21
ウサギプリオンタンパク質とヒトおよびマウスプリオンタンパク質の構造安定性の比較研究。
Comparison studies of the structural stability of rabbit prion protein with human and mouse prion proteins. Zhang Jiapu. Journal of theoretical biology(J. Theor. Biol.)2011Jan21
シミュレーテッドアニーリングによってフォーマットされたプリオンAGAAAAGAアミロイドフィブリルの最適な分子構造。
Optimal molecular structures of prion AGAAAAGA amyloid fibrils formatted by simulated annealing. Zhang Jiapu. Journal of molecular modeling(J Mol Model)2011Jan01
野生型および変異体の分子動力学シミュレーションによって調査されたウサギプリオンの構造安定性に関する研究。
Studies on the structural stability of rabbit prion probed by molecular dynamics simulations of its wild-type and mutants. Zhang Jiapu. Journal of theoretical biology(J. Theor. Biol.)2010May07
分子動力学シミュレーションによって調べられたウサギプリオンの構造安定性に関する研究。
Studies on the structural stability of rabbit prion probed by molecular dynamics simulations. Zhang Jiapu. Journal of biomolecular structure & dynamics(J. Biomol. Struct. Dyn.)2009Oct01
-----------------Literatures: ------------------
Zhang JP (2023) My Father's Diaries 1966-1971: A Cherish Literature and History Material - now published (ISBN 978-620-2-41346-6, ISBN-10 6202413468) by the Golden iris, Golden Light Academic Publishing, on 2023-02-08, ii+82 pages. It's English version's ISBN number is 978-620-0-64379-7 by the Globe EDIT Publishing on 2023-03-17, ii+112 pages.
Zhang JP (2025) 张家普博士百篇科普论文集(卷一),II+xx+565页, https://youtu.be/qVJv2h8m4f4, ⓒsciencenet . - A recent youtube 关于Hopfield神经网络的一个小注解(张家普)
