Skeletal muscle involvement in systemic amyloidosis is often overlooked
Aim Systemic amyloidosis is a condition in which misfolded amyloid fibrils are deposited within tissues. Amyloid myopathy is a rare manifestation of systemic amyloidosis. However, whether skeletal muscle involvement is underestimated and whether such deposition guarantees clinical and pathological m...
Uloženo v:
| Vydáno v: | Neuropathology and applied neurobiology Ročník 50; číslo 4; s. e12996 - n/a |
|---|---|
| Hlavní autoři: | , , , , , , , , , , , , |
| Médium: | Journal Article |
| Jazyk: | angličtina |
| Vydáno: |
England
Wiley Subscription Services, Inc
01.08.2024
|
| Témata: | |
| ISSN: | 0305-1846, 1365-2990, 1365-2990 |
| On-line přístup: | Získat plný text |
| Tagy: |
Přidat tag
Žádné tagy, Buďte první, kdo vytvoří štítek k tomuto záznamu!
|
| Abstract | Aim
Systemic amyloidosis is a condition in which misfolded amyloid fibrils are deposited within tissues. Amyloid myopathy is a rare manifestation of systemic amyloidosis. However, whether skeletal muscle involvement is underestimated and whether such deposition guarantees clinical and pathological myopathic features remain to be investigated.
Methods
We retrospectively reviewed patients with systemic amyloidosis, in whom skeletal muscle biopsies were performed at our centre between January 2018 and June 2023. In total, 28 patients with suspected systemic amyloidosis were included. Among these, 21 presented with cardiomyopathy but lacked myopathic symptoms. The clinical and pathological data of these patients were further analysed. The amyloid type was confirmed by immunohistochemistry.
Results
Twenty‐eight patients with suspected systemic amyloidosis underwent muscle biopsy. Amyloid deposition in the skeletal muscle was confirmed in 24 patients, including 22 with light‐chain amyloidosis (AL) and two with transthyretin amyloidosis (ATTR). Among the 24 patients, seven presented with muscle weakness and decreased muscle strength (Group 1, symptomatic myopathy), whereas the remaining 17 exhibited normal muscle strength (Group 2, asymptomatic myopathy). Group 1 included four patients with AL‐λ, one with AL‐κ and two with ATTR. Group 2 included 15 patients with AL‐λ and two patients with AL‐κ. In Group 1, six patients exhibited neuropathy, whereas only one patient in Group 2 presented with subclinical neuropathy on nerve conduction studies. Amyloid deposition in the interstitium was the most obvious change, observed in all 24 patients. Neuropathic changes, including denervation atrophy and muscle fibre grouping, were also common. Except for type 2 fibre atrophy, the other myopathic changes were mild and nonspecific. No sarcolemmal disruption was observed. Immunohistochemical analysis revealed marked positivity for MAC and MHC1 expression in the regions with amyloid deposits. Clinicopathological analysis revealed no significant differences in the extent of muscular amyloid deposition between the two groups. Nevertheless, patients in Group 1 displayed more pronounced neurogenic atrophy on skeletal muscle biopsies.
Conclusions
Our study indicates that amyloid deposition in skeletal muscle is commonly observed but rarely causes symptomatic myopathy in systemic amyloidosis.
Skeletal muscle involvement in systemic amyloidosis is frequently overlooked due to typically silent amyloid deposition. However, skeletal muscle biopsies offer a promising and minimally invasive method for obtaining histopathological evidence in diagnosing systemic amyloidosis. |
|---|---|
| AbstractList | Aim
Systemic amyloidosis is a condition in which misfolded amyloid fibrils are deposited within tissues. Amyloid myopathy is a rare manifestation of systemic amyloidosis. However, whether skeletal muscle involvement is underestimated and whether such deposition guarantees clinical and pathological myopathic features remain to be investigated.
Methods
We retrospectively reviewed patients with systemic amyloidosis, in whom skeletal muscle biopsies were performed at our centre between January 2018 and June 2023. In total, 28 patients with suspected systemic amyloidosis were included. Among these, 21 presented with cardiomyopathy but lacked myopathic symptoms. The clinical and pathological data of these patients were further analysed. The amyloid type was confirmed by immunohistochemistry.
Results
Twenty‐eight patients with suspected systemic amyloidosis underwent muscle biopsy. Amyloid deposition in the skeletal muscle was confirmed in 24 patients, including 22 with light‐chain amyloidosis (AL) and two with transthyretin amyloidosis (ATTR). Among the 24 patients, seven presented with muscle weakness and decreased muscle strength (Group 1, symptomatic myopathy), whereas the remaining 17 exhibited normal muscle strength (Group 2, asymptomatic myopathy). Group 1 included four patients with AL‐λ, one with AL‐κ and two with ATTR. Group 2 included 15 patients with AL‐λ and two patients with AL‐κ. In Group 1, six patients exhibited neuropathy, whereas only one patient in Group 2 presented with subclinical neuropathy on nerve conduction studies. Amyloid deposition in the interstitium was the most obvious change, observed in all 24 patients. Neuropathic changes, including denervation atrophy and muscle fibre grouping, were also common. Except for type 2 fibre atrophy, the other myopathic changes were mild and nonspecific. No sarcolemmal disruption was observed. Immunohistochemical analysis revealed marked positivity for MAC and MHC1 expression in the regions with amyloid deposits. Clinicopathological analysis revealed no significant differences in the extent of muscular amyloid deposition between the two groups. Nevertheless, patients in Group 1 displayed more pronounced neurogenic atrophy on skeletal muscle biopsies.
Conclusions
Our study indicates that amyloid deposition in skeletal muscle is commonly observed but rarely causes symptomatic myopathy in systemic amyloidosis.
Skeletal muscle involvement in systemic amyloidosis is frequently overlooked due to typically silent amyloid deposition. However, skeletal muscle biopsies offer a promising and minimally invasive method for obtaining histopathological evidence in diagnosing systemic amyloidosis. Systemic amyloidosis is a condition in which misfolded amyloid fibrils are deposited within tissues. Amyloid myopathy is a rare manifestation of systemic amyloidosis. However, whether skeletal muscle involvement is underestimated and whether such deposition guarantees clinical and pathological myopathic features remain to be investigated. We retrospectively reviewed patients with systemic amyloidosis, in whom skeletal muscle biopsies were performed at our centre between January 2018 and June 2023. In total, 28 patients with suspected systemic amyloidosis were included. Among these, 21 presented with cardiomyopathy but lacked myopathic symptoms. The clinical and pathological data of these patients were further analysed. The amyloid type was confirmed by immunohistochemistry. Twenty-eight patients with suspected systemic amyloidosis underwent muscle biopsy. Amyloid deposition in the skeletal muscle was confirmed in 24 patients, including 22 with light-chain amyloidosis (AL) and two with transthyretin amyloidosis (ATTR). Among the 24 patients, seven presented with muscle weakness and decreased muscle strength (Group 1, symptomatic myopathy), whereas the remaining 17 exhibited normal muscle strength (Group 2, asymptomatic myopathy). Group 1 included four patients with AL-λ, one with AL-κ and two with ATTR. Group 2 included 15 patients with AL-λ and two patients with AL-κ. In Group 1, six patients exhibited neuropathy, whereas only one patient in Group 2 presented with subclinical neuropathy on nerve conduction studies. Amyloid deposition in the interstitium was the most obvious change, observed in all 24 patients. Neuropathic changes, including denervation atrophy and muscle fibre grouping, were also common. Except for type 2 fibre atrophy, the other myopathic changes were mild and nonspecific. No sarcolemmal disruption was observed. Immunohistochemical analysis revealed marked positivity for MAC and MHC1 expression in the regions with amyloid deposits. Clinicopathological analysis revealed no significant differences in the extent of muscular amyloid deposition between the two groups. Nevertheless, patients in Group 1 displayed more pronounced neurogenic atrophy on skeletal muscle biopsies. Our study indicates that amyloid deposition in skeletal muscle is commonly observed but rarely causes symptomatic myopathy in systemic amyloidosis. Systemic amyloidosis is a condition in which misfolded amyloid fibrils are deposited within tissues. Amyloid myopathy is a rare manifestation of systemic amyloidosis. However, whether skeletal muscle involvement is underestimated and whether such deposition guarantees clinical and pathological myopathic features remain to be investigated.AIMSystemic amyloidosis is a condition in which misfolded amyloid fibrils are deposited within tissues. Amyloid myopathy is a rare manifestation of systemic amyloidosis. However, whether skeletal muscle involvement is underestimated and whether such deposition guarantees clinical and pathological myopathic features remain to be investigated.We retrospectively reviewed patients with systemic amyloidosis, in whom skeletal muscle biopsies were performed at our centre between January 2018 and June 2023. In total, 28 patients with suspected systemic amyloidosis were included. Among these, 21 presented with cardiomyopathy but lacked myopathic symptoms. The clinical and pathological data of these patients were further analysed. The amyloid type was confirmed by immunohistochemistry.METHODSWe retrospectively reviewed patients with systemic amyloidosis, in whom skeletal muscle biopsies were performed at our centre between January 2018 and June 2023. In total, 28 patients with suspected systemic amyloidosis were included. Among these, 21 presented with cardiomyopathy but lacked myopathic symptoms. The clinical and pathological data of these patients were further analysed. The amyloid type was confirmed by immunohistochemistry.Twenty-eight patients with suspected systemic amyloidosis underwent muscle biopsy. Amyloid deposition in the skeletal muscle was confirmed in 24 patients, including 22 with light-chain amyloidosis (AL) and two with transthyretin amyloidosis (ATTR). Among the 24 patients, seven presented with muscle weakness and decreased muscle strength (Group 1, symptomatic myopathy), whereas the remaining 17 exhibited normal muscle strength (Group 2, asymptomatic myopathy). Group 1 included four patients with AL-λ, one with AL-κ and two with ATTR. Group 2 included 15 patients with AL-λ and two patients with AL-κ. In Group 1, six patients exhibited neuropathy, whereas only one patient in Group 2 presented with subclinical neuropathy on nerve conduction studies. Amyloid deposition in the interstitium was the most obvious change, observed in all 24 patients. Neuropathic changes, including denervation atrophy and muscle fibre grouping, were also common. Except for type 2 fibre atrophy, the other myopathic changes were mild and nonspecific. No sarcolemmal disruption was observed. Immunohistochemical analysis revealed marked positivity for MAC and MHC1 expression in the regions with amyloid deposits. Clinicopathological analysis revealed no significant differences in the extent of muscular amyloid deposition between the two groups. Nevertheless, patients in Group 1 displayed more pronounced neurogenic atrophy on skeletal muscle biopsies.RESULTSTwenty-eight patients with suspected systemic amyloidosis underwent muscle biopsy. Amyloid deposition in the skeletal muscle was confirmed in 24 patients, including 22 with light-chain amyloidosis (AL) and two with transthyretin amyloidosis (ATTR). Among the 24 patients, seven presented with muscle weakness and decreased muscle strength (Group 1, symptomatic myopathy), whereas the remaining 17 exhibited normal muscle strength (Group 2, asymptomatic myopathy). Group 1 included four patients with AL-λ, one with AL-κ and two with ATTR. Group 2 included 15 patients with AL-λ and two patients with AL-κ. In Group 1, six patients exhibited neuropathy, whereas only one patient in Group 2 presented with subclinical neuropathy on nerve conduction studies. Amyloid deposition in the interstitium was the most obvious change, observed in all 24 patients. Neuropathic changes, including denervation atrophy and muscle fibre grouping, were also common. Except for type 2 fibre atrophy, the other myopathic changes were mild and nonspecific. No sarcolemmal disruption was observed. Immunohistochemical analysis revealed marked positivity for MAC and MHC1 expression in the regions with amyloid deposits. Clinicopathological analysis revealed no significant differences in the extent of muscular amyloid deposition between the two groups. Nevertheless, patients in Group 1 displayed more pronounced neurogenic atrophy on skeletal muscle biopsies.Our study indicates that amyloid deposition in skeletal muscle is commonly observed but rarely causes symptomatic myopathy in systemic amyloidosis.CONCLUSIONSOur study indicates that amyloid deposition in skeletal muscle is commonly observed but rarely causes symptomatic myopathy in systemic amyloidosis. AimSystemic amyloidosis is a condition in which misfolded amyloid fibrils are deposited within tissues. Amyloid myopathy is a rare manifestation of systemic amyloidosis. However, whether skeletal muscle involvement is underestimated and whether such deposition guarantees clinical and pathological myopathic features remain to be investigated.MethodsWe retrospectively reviewed patients with systemic amyloidosis, in whom skeletal muscle biopsies were performed at our centre between January 2018 and June 2023. In total, 28 patients with suspected systemic amyloidosis were included. Among these, 21 presented with cardiomyopathy but lacked myopathic symptoms. The clinical and pathological data of these patients were further analysed. The amyloid type was confirmed by immunohistochemistry.ResultsTwenty‐eight patients with suspected systemic amyloidosis underwent muscle biopsy. Amyloid deposition in the skeletal muscle was confirmed in 24 patients, including 22 with light‐chain amyloidosis (AL) and two with transthyretin amyloidosis (ATTR). Among the 24 patients, seven presented with muscle weakness and decreased muscle strength (Group 1, symptomatic myopathy), whereas the remaining 17 exhibited normal muscle strength (Group 2, asymptomatic myopathy). Group 1 included four patients with AL‐λ, one with AL‐κ and two with ATTR. Group 2 included 15 patients with AL‐λ and two patients with AL‐κ. In Group 1, six patients exhibited neuropathy, whereas only one patient in Group 2 presented with subclinical neuropathy on nerve conduction studies. Amyloid deposition in the interstitium was the most obvious change, observed in all 24 patients. Neuropathic changes, including denervation atrophy and muscle fibre grouping, were also common. Except for type 2 fibre atrophy, the other myopathic changes were mild and nonspecific. No sarcolemmal disruption was observed. Immunohistochemical analysis revealed marked positivity for MAC and MHC1 expression in the regions with amyloid deposits. Clinicopathological analysis revealed no significant differences in the extent of muscular amyloid deposition between the two groups. Nevertheless, patients in Group 1 displayed more pronounced neurogenic atrophy on skeletal muscle biopsies.ConclusionsOur study indicates that amyloid deposition in skeletal muscle is commonly observed but rarely causes symptomatic myopathy in systemic amyloidosis. |
| Author | Lv, Huixia Zhang, Dong Dai, Tingjun Li, Wei Liu, Wenzhu Liu, Fuchen Yan, Chuanzhu Shan, Yi Zhou, Xiaoyu Zhao, Yuying Xu, Jingwen Wang, Yingxin Zhao, Dandan |
| Author_xml | – sequence: 1 givenname: Jingwen surname: Xu fullname: Xu, Jingwen organization: Shandong University – sequence: 2 givenname: Xiaoyu surname: Zhou fullname: Zhou, Xiaoyu organization: Shandong University – sequence: 3 givenname: Yingxin surname: Wang fullname: Wang, Yingxin organization: Shandong University – sequence: 4 givenname: Wenzhu surname: Liu fullname: Liu, Wenzhu organization: Shandong University – sequence: 5 givenname: Yi surname: Shan fullname: Shan, Yi organization: Shandong University – sequence: 6 givenname: Dong surname: Zhang fullname: Zhang, Dong organization: Shandong University – sequence: 7 givenname: Huixia surname: Lv fullname: Lv, Huixia organization: Qilu Hospital of Shandong University – sequence: 8 givenname: Dandan surname: Zhao fullname: Zhao, Dandan organization: Shandong University – sequence: 9 givenname: Tingjun surname: Dai fullname: Dai, Tingjun organization: Shandong University – sequence: 10 givenname: Yuying surname: Zhao fullname: Zhao, Yuying organization: Shandong University – sequence: 11 givenname: Wei orcidid: 0000-0002-8600-6088 surname: Li fullname: Li, Wei organization: Shandong University – sequence: 12 givenname: Fuchen surname: Liu fullname: Liu, Fuchen email: fuchen.liu@email.sdu.edu.cn organization: Shandong University – sequence: 13 givenname: Chuanzhu surname: Yan fullname: Yan, Chuanzhu email: chuanzhuyan@163.com organization: Shandong University |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/38982616$$D View this record in MEDLINE/PubMed |
| BookMark | eNp1kcFLwzAUxoMouqkH_wEpeNFDZ9IsaXOUoVMYelDPIU1fIVuaaNNO-t-buXkZGgJ5kN_38d77xujQeQcIXRA8IfHcOuUmJBOCH6ARoZylscaHaIQpZikppvwEjUNYYoxZzsUxOqGFKDJO-AjNX1dgoVM2afqgLSTGrb1dQwOui3UShtBBY3SimsF6U_lgQhKvrztwiV9Da71fQXWGjmplA5zv3lP0_nD_NntMFy_zp9ndItWUUZ5qTrXIdFlO61LQjFSEs7LIoGJFmSmdE0FJVm_apAxKQkHzsqIiDkXiZ67oKbre-n60_rOH0MnGBA3WKge-D5LiPBeCsCmO6NUeuvR962J3kRKRKnKSRepyR_VlA5X8aE2j2kH-rigCt1tAtz6EFmqpTac6413XKmMlwXITgowhyJ8QouJmT_Fr-he7c_8yFob_Qfl897xVfANBFpUT |
| CitedBy_id | crossref_primary_10_1093_jnen_nlaf088 crossref_primary_10_1016_j_jacadv_2025_101784 crossref_primary_10_1212_WNL_0000000000214101 |
| Cites_doi | 10.1186/1750‐1172‐8‐31 10.2169/internalmedicine.2742‐23 10.1111/j.0954‐6820.1983.tb08576.x 10.3390/surgeries4020028 10.1002/mus.26723 10.1212/WNL.0000000000007143 10.5414/NPP29059 10.1590/S0004‐282X2001000400018 10.1002/mus.20169 10.1016/0022‐510X(88)90158‐X 10.1016/j.tibs.2015.10.002 10.1007/BF00190993 10.3109/13506129.2014.927759 10.1126/science.aac4354 10.1016/j.nmd.2018.12.010 10.17161/rrnmf.v1i4.13699 10.1096/fj.04‐2022fje 10.1002/mus.27150 10.1111/bjh.12286 10.1523/JNEUROSCI.21‐19‐07576.2001 10.1016/j.xocr.2017.11.002 10.1038/nmeth.2019 10.1212/WNL.27.1.47 10.1016/j.mayocp.2016.06.027 10.1111/j.1468‐3083.2006.02062.x 10.1038/s41408‐021‐00483‐7 10.1016/0002‐9343(87)90516‐X 10.1136/jnnp.60.5.591 10.3389/fneur.2019.00554 10.1016/j.pmr.2012.06.006 10.1002/mus.20185 10.1080/13506129.2022.2147636 10.1016/S0046‐8177(98)90061‐2 10.1159/000506617 10.2147/DNND.S340117 10.1016/j.ymgme.2013.01.015 10.1002/mus.24771 10.1002/wsbm.1462 10.1212/01.wnl.0000182297.15699.2e 10.1007/s00415‐016‐8264‐3 10.1007/s00415‐010‐5642‐0 10.1002/ana.410430606 10.1080/13506129.2019.1646639 10.1080/13506129.2018.1491398 |
| ContentType | Journal Article |
| Copyright | 2024 British Neuropathological Society. Copyright © 2024 British Neuropathological Society |
| Copyright_xml | – notice: 2024 British Neuropathological Society. – notice: Copyright © 2024 British Neuropathological Society |
| DBID | AAYXX CITATION CGR CUY CVF ECM EIF NPM 7TK K9. 7X8 |
| DOI | 10.1111/nan.12996 |
| DatabaseName | CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed Neurosciences Abstracts ProQuest Health & Medical Complete (Alumni) MEDLINE - Academic |
| DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) ProQuest Health & Medical Complete (Alumni) Neurosciences Abstracts MEDLINE - Academic |
| DatabaseTitleList | MEDLINE MEDLINE - Academic ProQuest Health & Medical Complete (Alumni) |
| Database_xml | – sequence: 1 dbid: NPM name: PubMed url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: 7X8 name: MEDLINE - Academic url: https://search.proquest.com/medline sourceTypes: Aggregation Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Medicine |
| EISSN | 1365-2990 |
| EndPage | n/a |
| ExternalDocumentID | 38982616 10_1111_nan_12996 NAN12996 |
| Genre | article Research Support, Non-U.S. Gov't Journal Article |
| GrantInformation_xml | – fundername: National Nature Science Foundation of China funderid: 81901278 – fundername: National Nature Science Foundation of China grantid: 81901278 |
| GroupedDBID | --- .3N .GA .GJ .Y3 05W 0R~ 10A 123 1OB 1OC 29N 31~ 33P 36B 3SF 3UE 4.4 50Y 50Z 51W 51X 52M 52N 52O 52P 52R 52S 52T 52U 52V 52W 52X 53G 5HH 5LA 5RE 5VS 66C 702 7PT 8-0 8-1 8-3 8-4 8-5 8UM 930 A01 A03 AAESR AAEVG AAHHS AAHQN AAIPD AAMNL AANHP AANLZ AAONW AASGY AAXRX AAYCA AAZKR ABCQN ABCUV ABDBF ABEML ABJNI ABPVW ABQWH ABXGK ACAHQ ACBWZ ACCFJ ACCZN ACGFS ACGOF ACMXC ACPOU ACPRK ACRPL ACSCC ACUHS ACXBN ACXQS ACYXJ ADBBV ADBTR ADEOM ADIZJ ADKYN ADMGS ADNMO ADOZA ADXAS ADZMN AEEZP AEIGN AEIMD AENEX AEQDE AEUQT AEUYR AFBPY AFEBI AFFNX AFFPM AFGKR AFPWT AFWVQ AFZJQ AHBTC AHEFC AHMBA AIACR AITYG AIURR AIWBW AJBDE ALAGY ALMA_UNASSIGNED_HOLDINGS ALUQN ALVPJ AMBMR AMYDB ASPBG ATUGU AVWKF AZBYB AZFZN AZVAB BAFTC BDRZF BFHJK BHBCM BMXJE BROTX BRXPI BY8 C45 CAG COF CS3 D-6 D-7 D-E D-F DCZOG DPXWK DR2 DRFUL DRMAN DRSTM DU5 EAD EAP EAS EBC EBD EBS EBX EJD EMB EMK EMOBN ESX EX3 F00 F01 F04 F5P FEDTE FUBAC G-S G.N GODZA GSXLS H.X HF~ HGLYW HVGLF HZI HZ~ IHE IX1 J0M K48 KBYEO L7B LATKE LC2 LC3 LEEKS LH4 LITHE LOXES LP6 LP7 LUTES LW6 LYRES MEWTI MK4 MRFUL MRMAN MRSTM MSFUL MSMAN MSSTM MXFUL MXMAN MXSTM N04 N05 N9A NF~ O66 O9- OIG OVD P2P P2W P2X P2Z P4B P4D PALCI PQQKQ Q.N Q11 QB0 Q~Q R.K RIWAO RJQFR ROL RX1 SAMSI SUPJJ SV3 TEORI TUS UB1 W8V W99 WBKPD WH7 WHWMO WIH WIJ WIK WOHZO WOW WQJ WRC WUP WVDHM WXI WXSBR XG1 YFH ZGI ZXP ZZTAW ~IA ~WT AAMMB AAYXX AEFGJ AEYWJ AGHNM AGQPQ AGXDD AGYGG AIDQK AIDYY AIQQE CITATION O8X CGR CUY CVF ECM EIF NPM 7TK K9. 7X8 |
| ID | FETCH-LOGICAL-c3536-c63c92cbb4fb9321d165b82ed58b2ac719312f057635eb13ec6bd391361c717a3 |
| IEDL.DBID | DRFUL |
| ISICitedReferencesCount | 4 |
| ISICitedReferencesURI | http://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=Summon&SrcAuth=ProQuest&DestLinkType=CitingArticles&DestApp=WOS_CPL&KeyUT=001268141300001&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D |
| ISSN | 0305-1846 1365-2990 |
| IngestDate | Sat Nov 01 15:07:48 EDT 2025 Sat Nov 29 14:55:46 EST 2025 Tue Sep 09 02:33:16 EDT 2025 Tue Nov 18 21:19:28 EST 2025 Sat Nov 29 06:09:50 EST 2025 Wed Jan 22 17:14:48 EST 2025 |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 4 |
| Keywords | amyloid skeletal muscle light‐chain amyloidosis transthyretin amyloidosis |
| Language | English |
| License | 2024 British Neuropathological Society. |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-c3536-c63c92cbb4fb9321d165b82ed58b2ac719312f057635eb13ec6bd391361c717a3 |
| Notes | Funding information This study was supported by grants from the National Nature Science Foundation of China (81901278). ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 |
| ORCID | 0000-0002-8600-6088 |
| PMID | 38982616 |
| PQID | 3097998712 |
| PQPubID | 1096364 |
| PageCount | 12 |
| ParticipantIDs | proquest_miscellaneous_3077991540 proquest_journals_3097998712 pubmed_primary_38982616 crossref_citationtrail_10_1111_nan_12996 crossref_primary_10_1111_nan_12996 wiley_primary_10_1111_nan_12996_NAN12996 |
| PublicationCentury | 2000 |
| PublicationDate | August 2024 2024-08-00 20240801 |
| PublicationDateYYYYMMDD | 2024-08-01 |
| PublicationDate_xml | – month: 08 year: 2024 text: August 2024 |
| PublicationDecade | 2020 |
| PublicationPlace | England |
| PublicationPlace_xml | – name: England – name: Oxford |
| PublicationTitle | Neuropathology and applied neurobiology |
| PublicationTitleAlternate | Neuropathol Appl Neurobiol |
| PublicationYear | 2024 |
| Publisher | Wiley Subscription Services, Inc |
| Publisher_xml | – name: Wiley Subscription Services, Inc |
| References | 1998; 29 1983; 214 2021; 64 2019; 92 2023; 4 2013; 108 2020; 143 2020; 61 1977; 27 2019; 10 2015; 52 2005; 65 2020; 12 2008; 77 2016; 91 2013; 8 2013; 161 1998; 43 2016; 263 2022; 29 2018; 25 2014; 21 2001; 21 2018; 6 2023; 63 2005; 19 2020; 1 2021; 11 1987; 83 2010; 29 2015; 40 2010; 257 2019; 26 1996; 60 2005; 31 2018 2016; 353 2019; 29 2001; 59 1988; 85 1992; 21 2007; 21 2012; 23 2012; 9 e_1_2_10_23_1 e_1_2_10_46_1 e_1_2_10_45_1 e_1_2_10_21_1 e_1_2_10_44_1 e_1_2_10_22_1 e_1_2_10_43_1 e_1_2_10_42_1 e_1_2_10_20_1 e_1_2_10_41_1 e_1_2_10_40_1 e_1_2_10_2_1 e_1_2_10_4_1 e_1_2_10_18_1 e_1_2_10_3_1 e_1_2_10_19_1 e_1_2_10_6_1 e_1_2_10_16_1 e_1_2_10_39_1 e_1_2_10_5_1 e_1_2_10_17_1 e_1_2_10_38_1 e_1_2_10_8_1 e_1_2_10_14_1 e_1_2_10_7_1 e_1_2_10_15_1 e_1_2_10_36_1 e_1_2_10_12_1 e_1_2_10_35_1 e_1_2_10_9_1 e_1_2_10_13_1 e_1_2_10_34_1 e_1_2_10_10_1 e_1_2_10_33_1 e_1_2_10_11_1 e_1_2_10_32_1 e_1_2_10_31_1 e_1_2_10_30_1 Estefania PA (e_1_2_10_47_1) 2018 e_1_2_10_29_1 Lima I (e_1_2_10_37_1) 2008; 77 Azevedo EP (e_1_2_10_24_1) 2018 e_1_2_10_27_1 e_1_2_10_28_1 e_1_2_10_25_1 e_1_2_10_48_1 e_1_2_10_26_1 |
| References_xml | – volume: 29 start-page: 463 issue: 5 year: 1998 end-page: 468 article-title: Amyloid myopathy: clinicopathologic study of 16 cases publication-title: Hum Pathol – volume: 63 start-page: 1575 issue: 11 year: 2023 end-page: 1584 article-title: A gluteus medius muscle biopsy to confirm amyloid transthyretin deposition in wild‐type transthyretin cardiac amyloidosis: a report of two cases publication-title: Intern Med – volume: 65 start-page: 1670 issue: 10 year: 2005 article-title: Gross muscle pseudohypertrophy in myeloma‐associated light chain amyloidosis publication-title: Neurology – volume: 60 start-page: 591 issue: 5 year: 1996 end-page: 592 article-title: Amyloid associated muscle pseudohypertrophy: amelioration of motor dysfunction with plasmapheresis and dimethylsulphoxide publication-title: J Neurol Neurosurg Psychiatry – volume: 27 start-page: 47 issue: 1 year: 1977 end-page: 54 article-title: Skeletal muscle pseudohypertrophy in primary amyloidosis publication-title: Neurology – volume: 77 start-page: 831 year: 2008 end-page: 832 article-title: Recent‐onset muscle hypertrophy unrelated to exercise publication-title: Amyloidosis am Fam Phys – volume: 64 start-page: 23 issue: 1 year: 2021 end-page: 36 article-title: Neuromuscular amyloidosis: unmasking the master of disguise publication-title: Muscle Nerve – volume: 29 start-page: 150 issue: 2 year: 2019 end-page: 151 article-title: Muscle hypertrophy in amyloid myopathy publication-title: Neuromuscul Disord – year: 2018 article-title: The role of inflammation in amyloid diseases publication-title: Amyloid Dis – volume: 31 start-page: 266 issue: 2 year: 2005 end-page: 272 article-title: Amyloid myopathy: characteristic features of a still underdiagnosed disease publication-title: Muscle Nerve – volume: 85 start-page: 223 issue: 2 year: 1988 end-page: 232 article-title: Skeletal muscle amyloid deposition in AL‐ (primary or myeloma‐associated), AA‐ (secondary), and prealbumin‐type amyloidosis publication-title: J Neurol Sci – volume: 263 start-page: 2332 issue: 11 year: 2016 end-page: 2335 article-title: Isaacs' syndrome with overlapping myopathy as the first manifestation of AL amyloidosis publication-title: J Neurol – volume: 214 start-page: 87 issue: 1 year: 1983 end-page: 91 article-title: Amyloid‐associated muscle pseudohypertrophy and multiple myeloma in a man with hypernephroma publication-title: Acta Med Scand – volume: 10 start-page: 554 year: 2019 article-title: Biomarkers in inflammatory myopathies—an expanded definition publication-title: Front Neurol – volume: 4 start-page: 275 issue: 2 year: 2023 end-page: 282 article-title: ATTR variant amyloidosis in patients with dysphagia publication-title: Surgeries – volume: 1 start-page: 28 issue: 4 year: 2020 end-page: 32 article-title: Amyloid myopathy as an inclusion body myositis mimic publication-title: RRNMF Neuromuscular J – volume: 257 start-page: 2091 issue: 12 year: 2010 end-page: 2093 article-title: Amyloid myopathy: a therapeutic trial for the rare and underdiagnosed myopathy with bortezomib publication-title: J Neurol – volume: 83 start-page: 175 issue: 1 year: 1987 end-page: 178 article-title: Respiratory muscle weakness and ventilatory failure in AL amyloidosis with muscular pseudohypertrophy publication-title: Am J Med – volume: 19 start-page: 124 issue: 1 year: 2005 end-page: 126 article-title: Up‐regulation of the extracellular matrix remodeling genes, biglycan, neutrophil gelatinase‐associated lipocalin, and matrix metalloproteinase‐9 in familial amyloid polyneuropathy publication-title: FASEB j – year: 2018 – volume: 8 start-page: 31 issue: 1 year: 2013 article-title: Guideline of transthyretin‐related hereditary amyloidosis for clinicians publication-title: Orphanet J Rare Dis – volume: 12 issue: 1 year: 2020 article-title: Skeletal muscle: a review of molecular structure and function, in health and disease publication-title: Wiley Interdiscip Rev Syst Biol Med – volume: 29 start-page: 213 issue: 4 year: 2022 end-page: 219 article-title: Amyloid nomenclature 2022: update, novel proteins, and recommendations by the International Society of Amyloidosis (ISA) Nomenclature Committee publication-title: Amyloid – volume: 91 start-page: 1354 year: 2016 end-page: 1361 – volume: 21 start-page: 7576 issue: 19 year: 2001 end-page: 7586 article-title: Familial amyloid polyneuropathy: receptor for advanced glycation end products‐dependent triggering of neuronal inflammatory and apoptotic pathways publication-title: J Neurosci – volume: 40 start-page: 719 issue: 12 year: 2015 end-page: 727 article-title: Amyloid fibres: inert end‐stage aggregates or key players in disease? publication-title: Trends Biochem Sci – volume: 43 start-page: 719 issue: 6 year: 1998 end-page: 728 article-title: Amyloid myopathy: an underdiagnosed entity publication-title: Ann Neurol – volume: 353 issue: 6294 year: 2016 article-title: In vivo aspects of protein folding and quality control publication-title: Science – volume: 21 start-page: 463 issue: 7 year: 1992 end-page: 465 article-title: MRI evaluation of amyloid myopathy publication-title: Skeletal Radiol – volume: 11 start-page: 90 issue: 5 year: 2021 article-title: Immunoglobulin light chain amyloidosis diagnosis and treatment algorithm 2021 publication-title: Blood Cancer J – volume: 11 start-page: 61 year: 2021 end-page: 68 article-title: The assessment of major histocompatibility complex (MHC) class‐I expression in different neuromuscular diseases publication-title: Degener Neurol Neuromuscul Dis – volume: 52 start-page: 1113 issue: 6 year: 2015 end-page: 1117 article-title: Myopathy in a patient with systemic AA amyloidosis possibly induced by psoriasis vulgaris: an autopsy case publication-title: Muscle Nerve – volume: 161 start-page: 525 issue: 4 year: 2013 end-page: 532 article-title: Systemic amyloidosis in England: an epidemiological study publication-title: Br J Haematol – volume: 23 start-page: 609 issue: 3 year: 2012 end-page: 631 article-title: Muscle biopsy evaluation in neuromuscular disorders publication-title: Phys Med Rehabil Clin N am – volume: 26 start-page: 216 issue: 4 year: 2019 end-page: 224 article-title: Pharyngo‐laryngeal involvement in systemic amyloidosis with cardiac involvement: a prospective observational study publication-title: Amyloid – volume: 6 start-page: 4 year: 2018 end-page: 6 article-title: Dysphagia due to systemic light chain amyloidosis revealed by videoendoscopic and videofluorographic swallowing examinations publication-title: Otolaryngology Case Reports – volume: 21 start-page: 175 issue: 3 year: 2014 end-page: 184 article-title: Interleukin‐1 signaling pathway as a therapeutic target in transthyretin amyloidosis publication-title: Amyloid – volume: 143 start-page: 304 issue: 4 year: 2020 end-page: 311 article-title: When to suspect a diagnosis of amyloidosis publication-title: Acta Haematol – volume: 61 start-page: 95 issue: 1 year: 2020 end-page: 100 article-title: Transthyretin amyloidosis: putting myopathy on the map publication-title: Muscle Nerve – volume: 29 start-page: 59 issue: 03 year: 2010 end-page: 64 article-title: Usefulness of combined nerve and muscle biopsy in the diagnosis of amyloid neuropathy—a study of 6 new cases publication-title: Clin Neuropathol – volume: 31 start-page: 41 issue: 1 year: 2005 end-page: 45 article-title: Muscular amyloid angiopathy with amyloidgenic transthyretin Ser50Ile and Tyr114Cys publication-title: Muscle Nerve – volume: 21 start-page: 986 issue: 7 year: 2007 end-page: 988 article-title: A ‘muscle’ man without exercise: muscle pseudohypertrophy in myeloma‐associated generalized amyloidosis publication-title: J Eur Acad Dermatol Venereol – volume: 9 start-page: 676 issue: 7 year: 2012 end-page: 682 article-title: Fiji: an open‐source platform for biological‐image analysis publication-title: Nat Methods – volume: 59 start-page: 582 issue: 3A year: 2001 end-page: 586 article-title: Amyloidotic muscle pseudohypertrophy: case report publication-title: Arq Neuropsiquiatr – volume: 92 start-page: e1403 issue: 12 year: 2019 end-page: e1404 article-title: Teaching NeuroImages: neuromyopathy in a patient with hereditary transthyretin Thr60Ala amyloidosis publication-title: Neurology – volume: 108 start-page: 249 issue: 4 year: 2013 end-page: 254 article-title: Chronic myopathy due to immunoglobulin light chain amyloidosis publication-title: Mol Genet Metab – volume: 25 start-page: 211 issue: 3 year: 2018 end-page: 212 article-title: A case of transthyretin amyloidosis with myopathy, neuropathy, and cardiomyopathy resulting from an exceedingly rare mutation transthyretin Ala120Ser (c.418G > T, p.Ala140Ser) publication-title: Amyloid – ident: e_1_2_10_4_1 doi: 10.1186/1750‐1172‐8‐31 – ident: e_1_2_10_20_1 doi: 10.2169/internalmedicine.2742‐23 – ident: e_1_2_10_34_1 doi: 10.1111/j.0954‐6820.1983.tb08576.x – ident: e_1_2_10_13_1 doi: 10.3390/surgeries4020028 – ident: e_1_2_10_6_1 doi: 10.1002/mus.26723 – ident: e_1_2_10_17_1 doi: 10.1212/WNL.0000000000007143 – ident: e_1_2_10_41_1 doi: 10.5414/NPP29059 – ident: e_1_2_10_35_1 doi: 10.1590/S0004‐282X2001000400018 – ident: e_1_2_10_8_1 doi: 10.1002/mus.20169 – ident: e_1_2_10_28_1 doi: 10.1016/0022‐510X(88)90158‐X – ident: e_1_2_10_44_1 doi: 10.1016/j.tibs.2015.10.002 – ident: e_1_2_10_39_1 doi: 10.1007/BF00190993 – ident: e_1_2_10_46_1 doi: 10.3109/13506129.2014.927759 – ident: e_1_2_10_45_1 doi: 10.1126/science.aac4354 – ident: e_1_2_10_29_1 doi: 10.1016/j.nmd.2018.12.010 – ident: e_1_2_10_18_1 doi: 10.17161/rrnmf.v1i4.13699 – ident: e_1_2_10_26_1 doi: 10.1096/fj.04‐2022fje – ident: e_1_2_10_14_1 doi: 10.1002/mus.27150 – ident: e_1_2_10_3_1 doi: 10.1111/bjh.12286 – ident: e_1_2_10_25_1 doi: 10.1523/JNEUROSCI.21‐19‐07576.2001 – ident: e_1_2_10_12_1 doi: 10.1016/j.xocr.2017.11.002 – ident: e_1_2_10_21_1 doi: 10.1038/nmeth.2019 – ident: e_1_2_10_32_1 doi: 10.1212/WNL.27.1.47 – ident: e_1_2_10_10_1 doi: 10.1016/j.mayocp.2016.06.027 – ident: e_1_2_10_40_1 doi: 10.1111/j.1468‐3083.2006.02062.x – ident: e_1_2_10_22_1 doi: 10.1038/s41408‐021‐00483‐7 – ident: e_1_2_10_30_1 doi: 10.1016/0002‐9343(87)90516‐X – ident: e_1_2_10_38_1 doi: 10.1136/jnnp.60.5.591 – ident: e_1_2_10_42_1 doi: 10.3389/fneur.2019.00554 – ident: e_1_2_10_48_1 doi: 10.1016/j.pmr.2012.06.006 – ident: e_1_2_10_15_1 doi: 10.1002/mus.20185 – ident: e_1_2_10_2_1 doi: 10.1080/13506129.2022.2147636 – volume-title: Amyloid Diseases year: 2018 ident: e_1_2_10_47_1 – ident: e_1_2_10_16_1 doi: 10.1016/S0046‐8177(98)90061‐2 – year: 2018 ident: e_1_2_10_24_1 article-title: The role of inflammation in amyloid diseases publication-title: Amyloid Dis – ident: e_1_2_10_5_1 doi: 10.1159/000506617 – ident: e_1_2_10_27_1 doi: 10.2147/DNND.S340117 – ident: e_1_2_10_31_1 doi: 10.1016/j.ymgme.2013.01.015 – ident: e_1_2_10_23_1 doi: 10.1002/mus.24771 – ident: e_1_2_10_19_1 doi: 10.1002/wsbm.1462 – ident: e_1_2_10_36_1 doi: 10.1212/01.wnl.0000182297.15699.2e – volume: 77 start-page: 831 year: 2008 ident: e_1_2_10_37_1 article-title: Recent‐onset muscle hypertrophy unrelated to exercise publication-title: Amyloidosis am Fam Phys – ident: e_1_2_10_33_1 doi: 10.1007/s00415‐016‐8264‐3 – ident: e_1_2_10_43_1 doi: 10.1007/s00415‐010‐5642‐0 – ident: e_1_2_10_9_1 doi: 10.1002/ana.410430606 – ident: e_1_2_10_11_1 doi: 10.1080/13506129.2019.1646639 – ident: e_1_2_10_7_1 doi: 10.1080/13506129.2018.1491398 |
| SSID | ssj0005769 |
| Score | 2.428404 |
| Snippet | Aim
Systemic amyloidosis is a condition in which misfolded amyloid fibrils are deposited within tissues. Amyloid myopathy is a rare manifestation of systemic... Systemic amyloidosis is a condition in which misfolded amyloid fibrils are deposited within tissues. Amyloid myopathy is a rare manifestation of systemic... AimSystemic amyloidosis is a condition in which misfolded amyloid fibrils are deposited within tissues. Amyloid myopathy is a rare manifestation of systemic... |
| SourceID | proquest pubmed crossref wiley |
| SourceType | Aggregation Database Index Database Enrichment Source Publisher |
| StartPage | e12996 |
| SubjectTerms | Adult Aged Aged, 80 and over amyloid Amyloidosis Amyloidosis - complications Amyloidosis - metabolism Amyloidosis - pathology Atrophy Biopsy Cardiomyopathy Denervation Female Fibrils Humans Immunoglobulin Light-chain Amyloidosis - complications Immunoglobulin Light-chain Amyloidosis - metabolism Immunoglobulin Light-chain Amyloidosis - pathology Immunohistochemistry light‐chain amyloidosis Male Middle Aged Muscle strength Muscle, Skeletal - metabolism Muscle, Skeletal - pathology Muscular Diseases - metabolism Muscular Diseases - pathology Musculoskeletal system Myopathy Nerve conduction Neuropathy Retrospective Studies Skeletal muscle Transthyretin transthyretin amyloidosis |
| Title | Skeletal muscle involvement in systemic amyloidosis is often overlooked |
| URI | https://onlinelibrary.wiley.com/doi/abs/10.1111%2Fnan.12996 https://www.ncbi.nlm.nih.gov/pubmed/38982616 https://www.proquest.com/docview/3097998712 https://www.proquest.com/docview/3077991540 |
| Volume | 50 |
| WOSCitedRecordID | wos001268141300001&url=https%3A%2F%2Fcvtisr.summon.serialssolutions.com%2F%23%21%2Fsearch%3Fho%3Df%26include.ft.matches%3Dt%26l%3Dnull%26q%3D |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| journalDatabaseRights | – providerCode: PRVWIB databaseName: Wiley Online Library Full Collection 2020 customDbUrl: eissn: 1365-2990 dateEnd: 99991231 omitProxy: false ssIdentifier: ssj0005769 issn: 0305-1846 databaseCode: DRFUL dateStart: 19970101 isFulltext: true titleUrlDefault: https://onlinelibrary.wiley.com providerName: Wiley-Blackwell |
| link | http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3dS8MwED_2IeKL3x_TOar4sJfKmrRpi09DnT7MIepgbyVJUyhunaybf7-XtqsOFQShD4Fcm3K5u_yuuf4CcBFyLriMlEkkxQQFIbPp-R43CUJrBAy2tHOSpL47GHijkf9YgavlvzA5P0T5wU17RhavtYNzkX5x8oQnl7hY-awKdYJ2a9egfvPUG_Y_Kzzc7EQ7bdImJjKsIBbShTzlzavL0TeMuQpZszWnt_Wvt92GzQJqGt3cNnagopJdWH8oNtP34O75FdccBN_GZJGihBEnGKsy_vA5to2c5DmWBp9gVh-H0zRODbwwcKvE0KWfY83XGe7DsHf7cn1vFucqmJI6lJmSUekTKYQdCYRvVmgxR3hEhY4nCJcuYjqLRFp91MFQTpVkIqS-RZmFnS6nB1BLpok6AqPjcNunPpVcODYTynek8Cw7ImFEQ-aRBrSX6g1kQTquz74YB8vkAxUTZIppwHkp-pYzbfwk1FzOUVA4WxrQjt6bxMwPhzsru9FN9N4HT9R0oWVclEG82GnAYT635SiI2TDJsvDh7WwKfx8-GHQHWeP476InsEEQCOVFg02ozWcLdQpr8n0ep7MWVN2R1yos9wNiRO8R |
| linkProvider | Wiley-Blackwell |
| linkToHtml | http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV3dS8MwED_mJuqL3x_TqVV88KWyJm3agi-izomziB_gW0nSFIpbJ-vm3--l7aqigiD0IdBrUy53l98l118AjiLOBZexMomkmKAgZDY93-MmQWiNgMGWdkGS1HODwHt-9u9qcDr9F6bgh6gW3LRn5PFaO7hekP7k5SlPT3C28tkMNGw0I6cOjYv7zlPvo8TDzY-00zZtYibDSmYhXclTPfx1PvoGMr9i1nzS6Sz973OXYbEEm8ZZYR0rUFPpKszdltvpa3D18IKzDsJvYzDJUMJIUoxWOYP4GNtGQfOcSIMPMK9PomGWZAZeGLpVaujiz75m7IzW4alz-XjeNcuTFUxJHcpMyaj0iRTCjgUCOCuymCM8oiLHE4RLF1GdRWKtP-pgMKdKMhFR36LMwpsupxtQT4ep2gKj7XDbpz6VXDg2E8p3pPAsOyZRTCPmkSYcT_UbypJ2XJ9-0Q-n6QcqJswV04TDSvS14Nr4Sag1HaSwdLcspG29O4m5H3Z3UN1GR9G7HzxVw4mWcVEGEWO7CZvF4Fa9IGrDNMvClx_nY_h792FwFuSN7b-L7sN89_G2F_aug5sdWCAIi4oSwhbUx6OJ2oVZ-TZOstFeacDvE0fyGQ |
| linkToPdf | http://cvtisr.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwpV1ZS8QwEB68EF-8j_Ws4oMvlW3Spg34IuqquBbxAN9KrkJx7Yrd9fc7abtVUUEQ-hDItCmTzMw3zfQLwL4WQgqVGpcoigkKQmY34pFwCUJrBAy-8iuSpG4Yx9HjI78Zg6PRvzAVP0Tzwc1aRumvrYGbF51-svJc5IcYrTgbh0k_4AzNcvL0tvPQ_SjxCMsj7eyadjGTYTWzkK3kaW7-Go--gcyvmLUMOp25_73uPMzWYNM5rlbHAoyZfBGmr-vt9CU4v3vCqIPw23keFijhZDl6q5JBfIBtp6J5zpQjnjGvz3S_yAoHL3TdJnds8WfPMnbqZXjonN2fXLj1yQquogFlrmJUcaKk9FOJAM7THgtkRIwOIkmEChHVeSS1-qMBOnNqFJOaco8yDztDQVdgIu_nZg2cdiB8TjlVQgY-k4YHSkaenxKdUs0i0oKDkX4TVdOO29Mvesko_UDFJKViWrDXiL5UXBs_CW2OJimpza1IaNvuTmLuh8PtNt1oKHb3Q-SmP7QyIcogYmy3YLWa3GYURG2YZnn48INyDn8fPomP47Kx_nfRHZi-Oe0k3cv4agNmCKKiqoJwEyYGr0OzBVPqbZAVr9v1-n0HsrjxlA |
| openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Skeletal+muscle+involvement+in+systemic+amyloidosis+is+often+overlooked&rft.jtitle=Neuropathology+and+applied+neurobiology&rft.au=Xu%2C+Jingwen&rft.au=Zhou%2C+Xiaoyu&rft.au=Wang%2C+Yingxin&rft.au=Liu%2C+Wenzhu&rft.date=2024-08-01&rft.issn=1365-2990&rft.eissn=1365-2990&rft.volume=50&rft.issue=4&rft.spage=e12996&rft_id=info:doi/10.1111%2Fnan.12996&rft.externalDBID=NO_FULL_TEXT |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0305-1846&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0305-1846&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0305-1846&client=summon |