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Article ; Online: Glycosides constituents from

Cheng, Yan-Gang / Yang, Si-Qi / Li, Pei / Wang, Yan / Li, Hui-Feng / Kong, Xiang-Peng / Tan, Jin-Yan / Wang, Ying-Li

2024 , Page(s) 1–4

Abstract: A new glycoside ( ...

Abstract	A new glycoside (
Language	English
Publishing date	2024-04-29
Publishing country	England
Document type	Journal Article
ZDB-ID	2185747-7
ISSN	1478-6427 ; 1478-6419
ISSN (online)	1478-6427
ISSN	1478-6419
DOI	10.1080/14786419.2024.2344738
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Article: Single-Domain Antibody-Based Protein Degrader for Synucleinopathies.

Jiang, Yixiang / Lin, Yan / Tetlow, Amber M / Pan, Ruimin / Ji, Changyi / Kong, Xiang-Peng / Congdon, Erin E / Sigurdsson, Einar M

bioRxiv : the preprint server for biology

2024

Abstract: Synucleinopathies are a group of neurodegenerative diseases characterized by the accumulation of α-synuclein (α-syn) in the brain, leading to motor and neuropsychiatric symptoms. Currently, there are no known cures for synucleinopathies, and treatments ... ...

Abstract	Synucleinopathies are a group of neurodegenerative diseases characterized by the accumulation of α-synuclein (α-syn) in the brain, leading to motor and neuropsychiatric symptoms. Currently, there are no known cures for synucleinopathies, and treatments mainly focus on symptom management. In this study, we developed a single-domain antibody (sdAb)-based protein degrader with features designed to enhance proteasomal degradation of α-syn. This sdAb derivative targets both α-syn and Cereblon (CRBN), a substrate-receptor for the E3-ubiquitin ligase CRL4
Language	English
Publishing date	2024-04-30
Publishing country	United States
Document type	Preprint
DOI	10.1101/2024.03.11.584473
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Article: Combination of Fusiform Capsulectomy of the Posterior Capsule and Percutaneous Flexion Tendon Release in the Treatment of Fused Knee with Severe Flexion Contracture During Total Knee Arthroplasty-A Report of Six Cases.

Chen, Qun-Qun / He, Min-Cong / Cao, Zheng / Kong, Xiang-Peng / Wang, Hai-Bin / Chai, Wei

Frontiers in surgery

2022 Volume 9, Page(s) 859426

Abstract: Purpose: This clinical research aims to assess the safety and efficacy of a combination of fusiform capsulectomy of the posterior capsule and percutaneous flexion tendon release in the treatment of a fused knee with severe flexion contracture during ... ...

Abstract	Purpose: This clinical research aims to assess the safety and efficacy of a combination of fusiform capsulectomy of the posterior capsule and percutaneous flexion tendon release in the treatment of a fused knee with severe flexion contracture during total knee arthroplasty (TKA). Methods: A retrospective analysis was performed in three patients (six knees) who had preoperative severe bony fused flexion contracture (>80°) prior to TKA and received a combination of fusiform capsulectomy of posterior capsule and percutaneous flexion tendon release during TKA between January 2016 and December 2019. The range of motion (ROM), knee functional score, postoperative complications, and radiographic results were evaluated. Result: Three patients (six knees) were enrolled in this study. The mean duration of follow-up was 42.83 ± 15.77 months. The postoperative knee ROM was 100.0 (76.0, 102.75) ( Conclusion: The technique of a combination of fusiform capsulectomy of the posterior capsule and percutaneous flexion tendon release is an effective and safe method during primary TKA for a fused knee with severe flexion contracture.
Language	English
Publishing date	2022-05-23
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2773823-1
ISSN	2296-875X
ISSN	2296-875X
DOI	10.3389/fsurg.2022.859426
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Article ; Online: Revision Total Hip Arthroplasty with Severe Acetabular Defect: A Preliminary Exploration and Attempt of Robotic-Assisted Technology.

Zhang, Shuai / Liu, Yu-Bo / Ma, Ming-Yang / Cao, Zheng / Kong, Xiang-Peng / Chai, Wei

Orthopaedic surgery

2022 Volume 14, Issue 8, Page(s) 1912–1917

Abstract: Background: Robotic-assisted technology may be useful in hip revision cases with acetabular defects. However, data on the use of robotic-assisted technology for such complex diseases is lacking.: Case presentation: This case study described the ... ...

Abstract	Background: Robotic-assisted technology may be useful in hip revision cases with acetabular defects. However, data on the use of robotic-assisted technology for such complex diseases is lacking. Case presentation: This case study described the adoption of MAKO robotic-assisted treatment of revision total hip arthroplasty (THA) combined with severe acetabular defect (Paprosky type IIIB). Robotic-assisted technology accurately achieved preoperative planning; the acetabular component and augment were placed in the original position and angle as planned. Robotic-assisted acetabular reaming was successful in a single pass, preserving the remaining acetabular bone mass very well with no procedure-related complications. The Harris Hip Score (HHS) at 6 months postoperatively was 84 and the Western Ontario and McMaster Universities (WOMAC) Osteoarthritis Index was 24. Conclusion: Robotic-assisted technology can help in the accurate reconstruction of acetabular defect in complex hip revision surgery.
MeSH term(s)	Acetabulum/surgery ; Arthroplasty, Replacement, Hip ; Hip Prosthesis ; Humans ; Prosthesis Failure ; Reoperation ; Retrospective Studies ; Robotic Surgical Procedures ; Treatment Outcome
Language	English
Publishing date	2022-07-06
Publishing country	Australia
Document type	Case Reports
ZDB-ID	2503162-4
ISSN	1757-7861 ; 1757-7853 ; 1757-7861
ISSN (online)	1757-7861 ; 1757-7853
ISSN	1757-7861
DOI	10.1111/os.13368
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Article: Dual-Metal Hetero-Single-Atoms with Different Coordination for Efficient Synergistic Catalysis

Zhao, Xin / Wang, Fengliang / Kong, Xiang-Peng / Fang, Ruiqi / Li, Yingwei

Journal of the American Chemical Society. 2021 Sept. 23, v. 143, no. 39

2021

Abstract: Rationally tailoring the coordination environments of metal single atoms (SAs) is an effective approach to promote their catalytic performances, which, however, remains as a challenge to date. Here, we report a novel misplaced deposition strategy for the ...

Abstract	Rationally tailoring the coordination environments of metal single atoms (SAs) is an effective approach to promote their catalytic performances, which, however, remains as a challenge to date. Here, we report a novel misplaced deposition strategy for the fabrication of differently coordinated dual-metal hetero-SAs. Systematic characterization results imply that the as-synthesized dual-metal hetero-SAs (exemplified by Cu and Co) are affixed to a hierarchical carbon support via Cu–C₄ and Co–N₄ coordination bonds. Density functional theory studies reveal that the strong synergistic interactions between the asymmetrically deployed CuC₄ and CoN₄ sites lead to remarkably polarized charge distributions, i.e., electron accumulation and deficiency around CuC₄ and CoN₄ sites, respectively. The obtained CuC₄/CoN₄@HC catalyst exhibits significantly enhanced capability in substrate adsorption and O₂ activation, achieving superior catalytic performances in the oxidative esterification of aromatic aldehydes in comparison with the Cu- and Co-based SA counterparts.
Keywords	adsorption ; carbon ; catalysts ; catalytic activity ; density functional theory ; esterification
Language	English
Dates of publication	2021-0923
Size	p. 16068-16077.
Publishing place	American Chemical Society
Document type	Article
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.1c06349
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Article: A large repertoire of B cell lineages targeting one cluster of epitopes in a vaccinated rhesus macaque

Li, Liuzhe / Hessell, Ann J. / Kong, Xiang-Peng / Haigwood, Nancy L. / Gorny, Miroslaw K.

Vaccine. 2021 Sept. 15, v. 39, no. 39

2021

Abstract: The repertoire of antibodies (Abs) produced upon vaccination against a particular antigenic site is rarely studied due to the complexity of the immunogens. We received such an opportunity when one rhesus macaque was immunized six times at 0, 4, 10, 16, ... ...

Abstract	The repertoire of antibodies (Abs) produced upon vaccination against a particular antigenic site is rarely studied due to the complexity of the immunogens. We received such an opportunity when one rhesus macaque was immunized six times at 0, 4, 10, 16, 32, and 143 weeks with C4-447 peptide containing the 8-mer epitope for human monoclonal Ab (mAb) 447-52D specific to the V3 region of gp120 HIV-1. Strong anti-V3 antibody responses reached 50% binding titer in serum of 10⁻⁵ at week 10 that declined to 10⁻³ by week 70. After an additional boost of C4-447 peptide at week 143, titers rebounded to 10⁻⁵ at week 146, or 2.7 years after the first immunization. Using the blood sample at week 146, we produced 41 V3-specific recombinant mAbs by single B cell isolation and cloning. Sequence analysis revealed 21B cell lineages, single and clonally related, based on immunoglobulin gene usage and CDR3s. The broad repertoire of Abs directed to a small antigenic site shows the targeting potency of a vaccine-elicited immune response in rhesus macaques.
Keywords	B-lymphocytes ; Macaca mulatta ; antibodies ; blood sampling ; blood serum ; epitopes ; humans ; immunoglobulin genes ; peptides ; sequence analysis ; vaccination ; vaccines
Language	English
Dates of publication	2021-0915
Size	p. 5607-5614.
Publishing place	Elsevier Ltd
Document type	Article
ZDB-ID	605674-x
ISSN	1873-2518 ; 0264-410X
ISSN (online)	1873-2518
ISSN	0264-410X
DOI	10.1016/j.vaccine.2021.08.015
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Article ; Online: Computational-guided determination of the functional role of 447-52D long CDRH3.

Kamau, Edwin / Bonneau, Richard / Kong, Xiang-Peng

Protein engineering, design & selection : PEDS

2019 Volume 31, Issue 12, Page(s) 479–487

Abstract: 447-52D (447) is a human monoclonal antibody that recognizes a conserved epitope in the crown region of the third variable loop (V3) of HIV-1 gp120, and like many anti-HIV-1 antibodies with broad neutralization capabilities, it has a long heavy-chain ... ...

Abstract	447-52D (447) is a human monoclonal antibody that recognizes a conserved epitope in the crown region of the third variable loop (V3) of HIV-1 gp120, and like many anti-HIV-1 antibodies with broad neutralization capabilities, it has a long heavy-chain complementarity determining region (CDRH3). Here, we use a combination of computational mutagenesis and modeling in tandem with fluorescence polarization assays to interrogate the molecular basis of 447 CDRH3 length and the individual contribution of selected CDRH3 residues to affinity. We observe that 447 CDRH3 length provides a large binding surface area and the best enthalpic contributions derived from hydrophobic packing, main-chain hydrogen bonds, electrostatic and van der Waals interactions. We also found out that CDRH3 residue Try100I is critical to 447 binding affinity.
MeSH term(s)	Amino Acid Sequence ; Antibodies, Monoclonal/chemistry ; Antibodies, Monoclonal/genetics ; Antibodies, Monoclonal/immunology ; Complementarity Determining Regions/chemistry ; Complementarity Determining Regions/genetics ; HIV Envelope Protein gp120/chemistry ; HIV Envelope Protein gp120/immunology ; Models, Molecular ; Mutagenesis, Site-Directed/methods ; Mutation ; Protein Conformation, beta-Strand
Chemical Substances	Antibodies, Monoclonal ; Complementarity Determining Regions ; HIV Envelope Protein gp120
Language	English
Publishing date	2019-04-25
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1466729-0
ISSN	1741-0134 ; 1741-0126
ISSN (online)	1741-0134
ISSN	1741-0126
DOI	10.1093/protein/gzz007
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Article ; Online: Antigenic landscape of the HIV-1 envelope and new immunological concepts defined by HIV-1 broadly neutralizing antibodies.

Wu, Xueling / Kong, Xiang-Peng

Current opinion in immunology

2016 Volume 42, Page(s) 56–64

Abstract: The isolation of HIV-1 broadly neutralizing antibodies (bnAbs) has demonstrated the ability of the human immune system to mount effective antibody responses against the virus. To harness this immune potential to elicit similar antibody responses by ... ...

Abstract	The isolation of HIV-1 broadly neutralizing antibodies (bnAbs) has demonstrated the ability of the human immune system to mount effective antibody responses against the virus. To harness this immune potential to elicit similar antibody responses by vaccination, it is important to understand the immunological processes that produce them. Here we review recent advances in crystal structural determinations of HIV-1 bnAb epitopes that directly portray the antigenic landscape of the HIV-1 envelope glycoprotein. We also summarize new immunological concepts implicated in bnAb sequences and their lineage studies.
MeSH term(s)	Animals ; Antibodies, Neutralizing/immunology ; Antigenic Variation ; Epitopes/metabolism ; HIV Antibodies/immunology ; HIV Infections/immunology ; HIV-1/immunology ; Humans ; Immunogenicity, Vaccine ; Primates ; Somatic Hypermutation, Immunoglobulin ; env Gene Products, Human Immunodeficiency Virus/metabolism
Chemical Substances	Antibodies, Neutralizing ; Epitopes ; HIV Antibodies ; env Gene Products, Human Immunodeficiency Virus
Language	English
Publishing date	2016-06-10
Publishing country	England
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural
ZDB-ID	1035767-1
ISSN	1879-0372 ; 0952-7915
ISSN (online)	1879-0372
ISSN	0952-7915
DOI	10.1016/j.coi.2016.05.013
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Article ; Online: A site of vulnerability at V3 crown defined by HIV-1 bNAb M4008_N1.

Chan, Kun-Wei / Luo, Christina C / Lu, Hong / Wu, Xueling / Kong, Xiang-Peng

Nature communications

2021 Volume 12, Issue 1, Page(s) 6464

Abstract: Identification of vulnerable sites defined by broadly neutralizing antibodies (bNAbs) on HIV-1 envelope (Env) is crucial for vaccine design, and we present here a vulnerable site defined by bNAb M4008_N1, which neutralizes about 40% of a tier-2 virus ... ...

Abstract	Identification of vulnerable sites defined by broadly neutralizing antibodies (bNAbs) on HIV-1 envelope (Env) is crucial for vaccine design, and we present here a vulnerable site defined by bNAb M4008_N1, which neutralizes about 40% of a tier-2 virus panel. A 3.2 Å resolution cryo-EM structure of M4008_N1 in complex with BG505 DS-SOSIP reveals a large, shallow protein epitope surface centered at the V3 crown of gp120 and surrounded by key glycans. M4008_N1 interacts with gp120 primarily through its hammerhead CDR H3 to form a β-sheet interaction with the V3 crown hairpin. This makes M4008_N1 compatible with the closed conformation of the prefusion Env trimer, and thus distinct from other known V3 crown mAbs. This mode of bNAb approaching the immunogenic V3 crown in the native Env trimer suggests a strategy for immunogen design targeting this site of vulnerability.
MeSH term(s)	AIDS Vaccines/therapeutic use ; Antibodies, Neutralizing/immunology ; Antibodies, Neutralizing/metabolism ; Broadly Neutralizing Antibodies/immunology ; Broadly Neutralizing Antibodies/metabolism ; HIV Antibodies/immunology ; HIV Antibodies/metabolism ; HIV-1/metabolism ; Humans
Chemical Substances	AIDS Vaccines ; Antibodies, Neutralizing ; Broadly Neutralizing Antibodies ; HIV Antibodies
Language	English
Publishing date	2021-11-09
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-021-26846-z
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Article ; Online: Dual-Metal Hetero-Single-Atoms with Different Coordination for Efficient Synergistic Catalysis.

Zhao, Xin / Wang, Fengliang / Kong, Xiang-Peng / Fang, Ruiqi / Li, Yingwei

Journal of the American Chemical Society

2021 Volume 143, Issue 39, Page(s) 16068–16077

Abstract	Rationally tailoring the coordination environments of metal single atoms (SAs) is an effective approach to promote their catalytic performances, which, however, remains as a challenge to date. Here, we report a novel misplaced deposition strategy for the fabrication of differently coordinated dual-metal hetero-SAs. Systematic characterization results imply that the as-synthesized dual-metal hetero-SAs (exemplified by Cu and Co) are affixed to a hierarchical carbon support via Cu-C
Language	English
Publishing date	2021-09-23
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3155-0
ISSN	1520-5126 ; 0002-7863
ISSN (online)	1520-5126
ISSN	0002-7863
DOI	10.1021/jacs.1c06349
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