Noah’s Ark and Internet Institutes: When and Why?

Kuo-Chen Chou

Gordon Life Science Institute, Boston, Massachusetts 02478, United States of America.

DOI: 10.4236/ns.2020.127037                

Abstract

The damage of coronavirus to our Earth is unprecedented that is going to kill the entire human beings. Facing this kind of situation, there are two completely different kinds of viewpoints. According to the philosophy of “Atheists” Karl Max and Friedrich Engels, “there is a Bigging, there must be an End”, meaning our Earth will eventually collide with the other planet and be destroyed completely. According to Holly Bible, however, Jesus, will come down again to bring Godly people to the Heaven and leave the remaining in the coronavirus-hell. During this waiting period, the “Internet Institutes” can provide the most useful knowledge for the other planets.

Keywords

Pandemic COVID-19, The End of World, The Prophecy of Revelation in Bible, The Internet Institutes

1. INTRODUCTION

As of July-03-2020, more than 230 countries on the Earth have been attacked by the coronavirus disease 2019 (COVID-19): for USA alone with reported 2,803,454 cases of which 130,995 result in deaths; for United Kingdom with 283,757 cases and 43,995 to deaths.

2. FACTS AND DISCUSSIONS

The damage power of COVID-19 is overwhelmingly stronger than “atomic bombs” (2^nd World War, 1945) or any kind of terrorists (“911”, 2001). The death number has also far beyond the reach of the death of military persons killed in any of war involved with USA.

Obviously, the unprecedented power must come from God and certainly not from human beings.

Coronavirus disease 2019 (COVID-19) is an infectious disease caused by severe acute respiratory syndrome, which was first identified in December 2019 in Wuhan, Hubei, China. After April 2020 and causing about 4000 deaths, although no remarkable infectious cases reported in Wuhan. Unfortunately, the 2^nd-wave coronavirus diseases have been found on Beijing during May 2020. This kind of originally from “Eastern countries” to Western Countries” and then back from the West to the East, very much like playing “Tennis” or “ping-pong” ball. It is the “Coronavirus” for the ball.

Since all the scientists working in a sharing laboratory of the Universities or most conversional Institutes must wear masks except those working in the “Internet Institute” such as the “Gordon Life Scient Institute” [1,2]. And the results thus obtained will be of real usage for the other planet as indicated in [3] as well as widely and increasingly agreeable as supported by many papers from different angles or aspects, particularly for the idea of “Pseudo Amino Acid Composition” or PseAAC” [4-74], the “5-steps Rule” [75-97], the “Wenxiang Diagram” [98-100], the “HIV protease inhibitor prediction” [101-106], and the “Graphic Rules” [107-115]. Using graphic approaches to study biological and medical systems can provide an intuitive vision and useful insights for helping analyze complicated relations therein as shown by the eight master pieces of pioneering papers from the then Chairman of Nobel Prize Committee Sture Forsen (see, e.g., [107,116] and many follow-up papers [67,98,99,113,115,117-160].

3. CONCLUSIONS

For our Earth, after several waves of the killings as described in the Section 2, the time of its “End” will become much faster according to the exponential mode. Before its “End”, it will provide the most useful knowledge to do the science with the “Internet Institutes”.

Conflicts of Interest

The authors declare no conflicts of interest.

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[81]	Khan, S., Khan, M., Iqbal, N., Hussain, T., Khan, S.A. and Chou, K.C. (2020) A Two-Level Computation Model Based on Deep Learning Algorithm for Identification of piRNA and Their Functions via Chou’s 5-Steps Rule. International Journal of Peptide Research and Therapeutics, 26, 795-809. https://doi.org/10.1007/s10989-019-09887-3
[82]	Lan, J., Liu, J., Liao, C., Merkler, D.J., Han, Q. and Li, J. (2019) A Study for Therapeutic Treatment against Parkinson’s Disease via Chou’s 5-Steps Rule. Current Topics in Medicinal Chemistry, 19, 2318-2333. http://www.eurekaselect.com/175887/article https://doi.org/10.2174/1568026619666191019111528
[83]	Liang, R., Xie, J., Zhang, C., Zhang, M., Huang, H., Huo, H., Cao, X. and Niu, B. (2019) Identifying Cancer Targets Based on Machine Learning Methods via Chou’s 5-Steps Rule and General Pseudo Components. Current Topics in Medicinal Chemistry, 19, 2301-2317. https://doi.org/10.2174/1568026619666191016155543
[84]	Liang, Y. and Zhang, S. (2019) Identifying DNase I Hypersensitive Sites Using Multi-Features Fusion and F-Score Features Selection via Chou’s 5-Steps Rule. Biophysical Chemistry, 253, Article ID: 106227. https://doi.org/10.1016/j.bpc.2019.106227
[85]	Wiktorowicz, A., Wit, A., Dziewierz, A., Rzeszutko, L., Dudek, D. and Kleczynski, P. (2019) Calcium Pattern Assessment in Patients with Severe Aortic Stenosis via the Chou’s 5-Steps Rule. Current Pharmaceutical Design, 25, 3769-3775. https://doi.org/10.2174/1381612825666190930101258
[86]	Yang, L., Lv, Y., Wang, S., Zhang, Q., Pan, Y., Su, D., Lu, Q. and Zuo, Y. (2019) Identifying FL11 Subtype by Characterizing Tumor Immune Microenvironment in Prostate Adenocarcinoma via Chou’s 5-Steps Rule. Genomics, 112, 1500-1515. https://doi.org/10.1016/j.ygeno.2019.08.021
[87]	Akmal, M.A., Hussain, W., Rasool, N., Khan, Y.D., Khan, S.A. and Chou, K.C. (2020) Using Chou’s 5-Steps Rule to Predict O-Linked Serine Glycosylation Sites by Blending Position Relative Features and Statistical Moment. IEEE/ACM Transactions on Computational Biology and Bioinformatics, in press. https://doi.org/10.1109/TCBB.2020.2968441
[88]	Charoenkwan, P., Schaduangrat, N., Nantasenamat, C., Piacham, T. and Shoombuatong, W. (2020) iQSP: A Sequence-Based Tool for the Prediction and Analysis of Quorum Sensing Peptides via Chou’s 5-Steps Rule and Informative Physicochemical Properties. International Journal of Molecular Sciences, 21, 75. https://doi.org/10.3390/ijms21010075
[89]	Charoenkwan, P., Schaduangrat, N., Nantasenamat, C., Piacham, T. and Shoombuatong, W. (2020) Correction: Shoombuatong, W., et al. iQSP: A Sequence-Based Tool for the Prediction and Analysis of Quorum Sensing Peptides via Chou’s 5-Steps Rule and Informative Physicochemical Properties. Int. J. Mol. Sci. 2020, 21, 75. International Journal of Molecular Sciences, 21, 2629. https://doi.org/10.3390/ijms21072629
[90]	Chen, Y. and Fan, X. (2020) Use of Chou’s 5-Steps Rule to Reveal Active Compound and Mechanism of Shuangshen Pingfei San on Idiopathic Pulmonary Fibrosis. Current Molecular Medicine, 20, 220-230. https://doi.org/10.2174/1566524019666191011160543
[91]	Du, L., Meng, Q., Jiang, H. and Li, Y. (2020) Using Evolutionary Information and Multi-Label Linear Discriminant Analysis to Predict the Subcellular Location of Multi-Site Bacterial Proteins via Chou’s 5-Steps Rule. IEEE Access, 8, 56452-56461. https://doi.org/10.1109/ACCESS.2020.2982160
[92]	Dutta, A., Dalmia, A., A. R, Singh, K.K. and Anand, A. (2020) Using the Chou’s 5-Steps Rule to Predict Splice Junctions with Interpretable Bidirectional Long Short-Term Memory Networks. Computers in Biology and Medicine, 116, Article ID: 103558. https://doi.org/10.1016/j.compbiomed.2019.103558
[93]	Ju, Z. and Wang, S.Y. (2020) Prediction of Lysine Formylation Sites Using the Composition of k-Spaced Amino Acid Pairs via Chou’s 5-Steps Rule and General Pseudo Components. Genomics, 112, 859-866. https://doi.org/10.1016/j.ygeno.2019.05.027
[94]	Kabir, M., Ahmad, S., Iqbal, M. and Hayat, M. (2020) iNR-2L: A Two-Level Sequence-Based Predictor Developed via Chou’s 5-Steps Rule and General PseAAC for Identifying Nuclear Receptors and Their Families. Genomics, 112, 276-285. https://doi.org/10.1016/j.ygeno.2019.02.006
[95]	Lin, W., Xiao, X., Qiu, W. and Chou, K.C. (2020) Use Chou’s 5-Steps Rule to Predict Remote Homology Proteins by Merging Grey Incidence Analysis and Domain Similarity Analysis. Natural Science, 12, 181-198. https://doi.org/10.4236/ns.2020.123016
[96]	Vundavilli, H., Datta, A., Sima, C., Hua, J., Lopes, R. and Bittner, M. (2020) Using Chou’s 5-Steps Rule to Model Feedback in Lung Cancer. IEEE Journal of Biomedical and Health Informatics, 21, 1-24. https://doi.org/10.1109/JBHI.2019.2958042
[97]	Yang, L., Lv, Y., Wang, S., Zhang, Q., Pan, Y., Su, D., Lu, Q. and Zuo, Y. (2020) Identifying FL11 Subtype by Characterizing Tumor Immune Microenvironment in Prostate Adenocarcinoma via Chou’s 5-Steps Rule. Genomics, 112, 1500-1515. https://doi.org/10.1016/j.ygeno.2019.08.021
[98]	Chou, K.C., Lin, W.Z. and Xiao, X. (2011) Wenxiang: A Web-Server for Drawing Wenxiang Diagrams. Natural Science, 3, 862-865. https://doi.org/10.4236/ns.2011.310111
[99]	Zhou, G.P. (2011) The Disposition of the LZCC Protein Residues in Wenxiang Diagram Provides New Insights into the Protein-Protein Interaction Mechanism. Journal of Theoretical Biology, 284, 142-148. https://doi.org/10.1016/j.jtbi.2011.06.006
[100]	Zhou, G.P., Chen, D., Liao, S. and Huang, R.B. (2016) Recent Progresses in Studying Helix-Helix Interactions in Proteins by Incorporating the Wenxiang Diagram into the NMR Spectroscopy. Current Topics in Medicinal Chemistry, 16, 581-590. https://doi.org/10.2174/1568026615666150819104617
[101]	Chou, K.C. (1993) A Vectorized Sequence-Coupling Model for Predicting HIV Protease Cleavage Sites in Proteins. The Journal of Biological Chemistry, 268, 16938-16948.
[102]	Chou, K.C. and Zhang, C.T. (1992) Diagrammatization of Codon Usage in 339 HIV Proteins and Its Biological Implication. AIDS Research and Human Retroviruses, 8, 1967-1976. https://doi.org/10.1089/aid.1992.8.1967
[103]	Chou, J.J. (1993) Predicting Cleavability of Peptide Sequences by HIV Protease via Correlation-Angle Approach. Journal of Protein Chemistry, 12, 291-302. https://doi.org/10.1007/BF01028191
[104]	Chou, K.C., Tomasselli, A.L., Reardon, I.M. and Heinrikson, R.L. (1996) Predicting HIV Protease Cleavage Sites in Proteins by a Discriminant Function Method. Proteins: Structure, Function, and Bioinformatics, 24, 51-72. https://doi.org/10.1002/(SICI)1097-0134(199601)24:1<51::AID-PROT4>3.0.CO;2-R
[105]	Chou, K.C. and Zhang, C.T. (1993) Studies on the Specificity of HIV Protease: An Application of Markov Chain Theory. Journal of Protein Chemistry, 12, 709-724. https://doi.org/10.1007/BF01024929
[106]	Chou, K.C., Zhang, C.T. and Kezdy, F.J. (1993) A Vector Approach to Predicting HIV Protease Cleavage Sites in Proteins. Proteins: Structure, Function, and Bioinformatics, 16, 195-204. https://doi.org/10.1002/prot.340160206
[107]	Chou, K.C. and Forsen, S. (1980) Graphical Rules for Enzyme-Catalyzed Rate Laws. Biochemical Journal, 187, 829-835. https://doi.org/10.1042/bj1870829
[108]	Chou, K.C. (1981) A New Graphical Rule for Rate Laws of Enzyme Reactions with Branched Pathways. Canadian Journal of Biochemistry, 59, 757-761. https://doi.org/10.1139/o81-105
[109]	Chou, K.C., Carter, R.E. and Forsen, S. (1981) A New Graphical Method for Deriving Rate Equations for Complicated Mechanisms. Chemica Scripta, 18, 82-86.
[110]	Chou, K.C. and Forsen, S. (1981) Graphical Rules of Steady-State Reaction Systems. Canadian Journal of Chemistry, 59, 737-755. https://doi.org/10.1139/v81-107
[111]	Chou, K.C. and Liu, W.M. (1981) Graphical Rules for Non-Steady State Enzyme Kinetics. Journal of Theoretical Biology, 91, 637-654. https://doi.org/10.1016/0022-5193(81)90215-0
[112]	Chou, K.C. (1983) Advances in Graphical Methods of Enzyme Kinetics. Biophysical Chemistry, 17, 51-55. https://doi.org/10.1016/0301-4622(83)87013-6
[113]	Chou, K.C. (1989) Graphic Rules in Steady and Non-Steady Enzyme Kinetics. The Journal of Biological Chemistry, 264, 12074-12079.
[114]	Chou, K.C. (1993) Graphic Rule for Non-Steady-State Enzyme Kinetics and Protein Folding Kinetics. Journal of Mathematical Chemistry, 12, 97-108. https://doi.org/10.1007/BF01164628
[115]	Chou, K.C. (2010) Graphic Rule for Drug Metabolism Systems. Current Drug Metabolism, 11, 369-378. https://doi.org/10.2174/138920010791514261
[116]	Chou, K.C. and Forsen, S. (1980) Diffusion-Controlled Effects in Reversible Enzymatic Fast Reaction System: Critical Spherical Shell and Proximity Rate Constants. Biophysical Chemistry, 12, 255-263. https://doi.org/10.1016/0301-4622(80)80002-0
[117]	Chou, K.C. (1983) Low-Frequency Vibrations of Helical Structures in Protein Molecules. Biochemical Journal, 209, 573-580. https://doi.org/10.1042/bj2090573
[118]	Chou, K.C. (1983) Identification of Low-Frequency Modes in Protein Molecules. Biochemical Journal, 215, 465-469. https://doi.org/10.1042/bj2150465
[119]	Zhou, G.P. and Deng, M.H. (1984) An Extension of Chou’s Graphic Rules for Deriving Enzyme Kinetic Equations to Systems Involving Parallel Reaction Pathways. Biochemical Journal, 222, 169-176. https://doi.org/10.1042/bj2220169
[120]	Chou, K.C. (1984) Biological Functions of Low-Frequency Vibrations (Phonons). III. Helical Structures and Microenvironment. Biophysical Journal, 45, 881-889. https://doi.org/10.1016/S0006-3495(84)84234-4
[121]	Chou, K.C. (1984) The Biological Functions of Low-Frequency Phonons. 4. Resonance Effects and Allosteric Transition. Biophysical Chemistry, 20, 61-71. https://doi.org/10.1016/0301-4622(84)80005-8
[122]	Chou, K.C. (1984) Low-Frequency Vibrations of DNA Molecules. Biochemical Journal, 221, 27-31. https://doi.org/10.1042/bj2210027
[123]	Chou, K.C. (1985) Low-Frequency Motions in Protein Molecules: Beta-Sheet and Beta-Barrel. Biophysical Journal, 48, 289-297. https://doi.org/10.1016/S0006-3495(85)83782-6
[124]	Chou, K.C. (1985) Prediction of a Low-Frequency Mode in Bovine Pancreatic Trypsin Inhibitor Molecule. International Journal of Biological Macromolecules, 7, 77-80. https://doi.org/10.1016/0141-8130(85)90035-2
[125]	Chou, K.C. and Kiang, Y.S. (1985) The Biological Functions of Low-Frequency Phonons: 5. A Phenomenological Theory. Biophysical Chemistry, 22, 219-235. https://doi.org/10.1016/0301-4622(85)80045-4
[126]	Chou, K.C. (1986) Origin of Low-Frequency Motion in Biological Macromolecules: A View of Recent Progress of Quasi-Continuity Model. Biophysical Chemistry, 25, 105-116. https://doi.org/10.1016/0301-4622(86)87001-6
[127]	Chou, K.C. (1987) The Biological Functions of Low-Frequency Phonons: 6. A Possible Dynamic Mechanism of Allosteric Transition in Antibody Molecules. Biopolymers, 26, 285-295. https://doi.org/10.1002/bip.360260209
[128]	Chou, K.C. (1988) Review: Low-Frequency Collective Motion in Biomacromolecules and Its Biological Functions. Biophysical Chemistry, 30, 3-48. https://doi.org/10.1016/0301-4622(88)85002-6
[129]	Chou, K.C. and Maggiora, G.M. (1988) The Biological Functions of Low-Frequency Phonons: 7. The Impetus for DNA to Accommodate Intercalators. British Polymer Journal, 20, 143-148. https://doi.org/10.1002/pi.4980200209
[130]	Chou, K.C. (1989) Low-Frequency Resonance and Cooperativity of Hemoglobin. Trends in Biochemical Sciences, 14, 212-213. https://doi.org/10.1016/0968-0004(89)90026-1
[131]	Chou, K.C., Maggiora, G.M. and Mao, B. (1989) Quasi-Continuum Models of Twist-Like and Accordion-Like Low-Frequency Motions in DNA. Biophysical Journal, 56, 295-305. https://doi.org/10.1016/S0006-3495(89)82676-1
[132]	Chou, K.C. (1990) Review: Applications of Graph Theory to Enzyme Kinetics and Protein Folding Kinetics. Steady and Non-Steady State Systems. Biophysical Chemistry, 35, 1-24. https://doi.org/10.1016/0301-4622(90)80056-D
[133]	Althaus, I.W., Chou, J.J., Gonzales, A.J., Diebel, M.R., Chou, K.C., Kezdy, F.J., Romero, D.L., Aristoff, P.A., Tarpley, W.G. and Reusser, F. (1993) Steady-State Kinetic Studies with the Non-Nucleoside HIV-1 Reverse Transcriptase Inhibitor U-87201E. The Journal of Biological Chemistry, 268, 6119-6124.
[134]	Althaus, I.W., Gonzales, A.J., Chou, J.J., Diebel, M.R., Chou, K.C., Kezdy, F.J., Romero, D.L., Aristoff, P.A., Tarpley, W.G. and Reusser, F. (1993) The Quinoline U-78036 Is a Potent Inhibitor of HIV-1 Reverse Transcriptase. The Journal of Biological Chemistry, 268, 14875-14880.
[135]	Althaus, I.W., Chou, J.J., Gonzales, A.J., Diebel, M.R., Chou, K.C., Kezdy, F.J., Romero, D.L., Aristoff, P.A., Tarpley, W.G. and Reusser, F. (1993) Kinetic Studies with the Nonnucleoside HIV-1 Reverse Transcriptase Inhibitor U-88204E. Biochemistry, 32, 6548-6554. https://doi.org/10.1021/bi00077a008
[136]	Althaus, I.W., Chou, J.J., Gonzales, A.J., Diebel, M.R., Chou, K.C., Kezdy, F.J., Romero, D.L., Aristoff, P.A., Tarpley, W.G. and Reusser, F. (1994) Steady-State Kinetic Studies with the Polysulfonate U-9843, an HIV Reverse Transcriptase Inhibitor. Experientia, 50, 23-28. https://doi.org/10.1007/BF01992044
[137]	Althaus, I.W., Chou, J.J., Gonzales, A.J., Diebel, M.R., Chou, K.C., Kezdy, F.J., Romero, D.L., Thomas, R.C., Aristoff, P.A., Tarpley, W.G. and Reusser, F. (1994) Kinetic Studies with the Non-Nucleoside Human Immunodeficiency Virus Type-1 Reverse Transcriptase Inhibitor U-90152E. Biochemical Pharmacology, 47, 2017-2028. https://doi.org/10.1016/0006-2952(94)90077-9
[138]	Chou, K.C., Kezdy, F.J. and Reusser, F. (1994) Review: Kinetics of Processive Nucleic Acid Polymerases and Nucleases. Analytical Biochemistry, 221, 217-230. https://doi.org/10.1006/abio.1994.1405
[139]	Chou, K.C., Zhang, C.T. and Maggiora, G.M. (1994) Solitary Wave Dynamics as a Mechanism for Explaining the Internal Motion during Microtubule Growth. Biopolymers, 34, 143-153. https://doi.org/10.1002/bip.360340114
[140]	Althaus, I.W., Chou, K.C., Franks, K.M., Diebel, M.R., Kezdy, F.J., Romero, D.L., Thomas, R.C., Aristoff, P.A., Tarpley, W.G. and Reusser, F. (1996) The Benzylthio-Pyrididine U-31,355, a Potent Inhibitor of HIV-1 Reverse Transcriptase. Biochemical Pharmacology, 51, 743-750. https://doi.org/10.1016/0006-2952(95)02390-9
[141]	Liu, H., Wang, M. and Chou, K.C. (2005) Low-Frequency Fourier Spectrum for Predicting Membrane Protein Types. Biochemical and Biophysical Research Communications (BBRC), 336, 737-739. https://doi.org/10.1016/j.bbrc.2005.08.160
[142]	Gordon, G. (2007) Designed Electromagnetic Pulsed Therapy: Clinical Applications. Journal of Cellular Physiology, 212, 579-582. https://doi.org/10.1002/jcp.21025
[143]	Andraos, J. (2008) Kinetic Plasticity and the Determination of Product Ratios for Kinetic Schemes Leading to Multiple Products without Rate Laws: New Methods Based on Directed Graphs. Canadian Journal of Chemistry, 86, 342-357. https://doi.org/10.1139/v08-020
[144]	Chou, K.C. and Shen, H.B. (2009) FoldRate: A Web-Server for Predicting Protein Folding Rates from Primary Sequence. The Open Bioinformatics Journal, 3, 31-50. https://doi.org/10.2174/1875036200903010031
[145]	Shen, H.B., Song, J.N. and Chou, K.C. (2009) Prediction of Protein Folding Rates from Primary Sequence by Fusing Multiple Sequential Features. Journal of Biomedical Science and Engineering (JBiSE), 2, 136-143. https://doi.org/10.4236/jbise.2009.23024
[146]	Wang, J.F. and Chou, K.C. (2009) Insight into the Molecular Switch Mechanism of Human Rab5a from Molecular Dynamics Simulations. Biochemical and Biophysical Research Communications (BBRC), 390, 608-612. https://doi.org/10.1016/j.bbrc.2009.10.014
[147]	Gordon, G. (2008) Extrinsic Electromagnetic Fields, Low Frequency (Phonon) Vibrations, and Control of Cell Function: A Non-Linear Resonance System. Journal of Biomedical Science and Engineering (JBiSE), 1, 152-156. https://doi.org/10.4236/jbise.2008.13025
[148]	Madkan, A., Blank, M., Elson, E., Chou, K.C., Geddis, M.S. and Goodman, R. (2009) Steps to the Clinic with ELF EMF. Natural Science, 1, 157-165. https://doi.org/10.4236/ns.2009.13020
[149]	Lian, P., Wei, D.Q., Wang, J.F. and Chou, K.C. (2011) An Allosteric Mechanism Inferred from Molecular Dynamics Simulations on Phospholamban Pentamer in Lipid Membranes. PLoS ONE, 6, e18587. https://doi.org/10.1371/journal.pone.0018587
[150]	Liao, Q.H., Gao, Q.Z., Wei, J. and Chou, K.C. (2011) Docking and Molecular Dynamics Study on the Inhibitory Activity of Novel Inhibitors on Epidermal Growth Factor Receptor (EGFR). Medicinal Chemistry, 7, 24-31. https://doi.org/10.2174/157340611794072698
[151]	Li, J., Wei, D.Q., Wang, J.F., Yu, Z.T. and Chou, K.C. (2012) Molecular Dynamics Simulations of CYP2E1. Medicinal Chemistry, 8, 208-221. https://doi.org/10.2174/157340612800493692
[152]	Wang, J.F. and Chou, K.C. (2012) Recent Advances in Computational Studies on Influenza a Virus M2 Proton Channel. Mini Reviews in Medicinal Chemistry, 12, 971-978. https://doi.org/10.2174/138955712802762275
[153]	Zhang, T., Wei, D.Q. and Chou, K.C. (2012) A Pharmacophore Model Specific to Active Site of CYP1A2 with a Novel Molecular Modeling Explorer and CoMFA. Medicinal Chemistry, 8, 198-207. https://doi.org/10.2174/157340612800493601
[154]	Jia, J., Liu, Z., Xiao, X. and Chou, K.C. (2015) iPPI-Esml: An Ensemble Classifier for Identifying the Interactions of Proteins by Incorporating Their Physicochemical Properties and Wavelet Transforms into PseAAC. Journal of Theoretical Biology, 377, 47-56. https://doi.org/10.1016/j.jtbi.2015.04.011
[155]	Jia, J., Liu, Z., Xiao, X., Liu, B. and Chou, K.C. (2016) Identification of Protein-Protein Binding Sites by Incorporating the Physicochemical Properties and Stationary Wavelet Transforms into Pseudo Amino Acid Compo sition (iPPBS-PseAAC). Journal of Biomolecular Structure and Dynamics (JBSD), 34, 1946-1961. https://doi.org/10.1080/07391102.2015.1095116
[156]	Chou, K.C. (2019) Proposing Pseudo Amino Acid Components Is an Important Milestone for Proteome and Genome Analyses. International Journal for Peptide Research and Therapeutics (IJPRT), 26, 1085-1098. https://doi.org/10.1007/s10989-019-09910-7
[157]	Chou, K.C. (2019) Artificial Intelligence (AI) Tools Constructed via the 5-Steps Rule for Predicting Post-Translational Modifications. Trends in Artificial Intelligence (TIA), 3, 60-74. https://doi.org/10.36959/643/304
[158]	Chou, K.C. (2019) Impacts of Pseudo Amino Acid Components and 5-Steps Rule to Proteomics and Proteome Analysis. Current Topics in Medicinal Chemistry, 19, 2283-2300. https://doi.org/10.2174/1568026619666191018100141
[159]	Chou, K.C. (2019) An Insightful Recollection for Predicting Protein Subcellular Locations in Multi-Label Systems. Genomics. (In Press) https://doi.org/10.1016/j.ygeno.2019.08.022
[160]	Chou, K.C. (2019) Advance in Predicting Subcellular Localization of Multi-Label Proteins and Its Implication for Developing Multi-Target Drugs. Current Medicinal Chemistry, 26, 4918-4943. https://doi.org/10.2174/0929867326666190507082559