Skip to main content
October 1, 1995
Free Access

Guidelines on the detection of paraneoplastic anti-neuronal-specific antibodies
Report from the Workshop to the Fourth Meeting of the International Society of Neuro-Immunology on paraneoplastic neurological disease, held October 22-23, 1994, in Rotterdam, The Netherlands

October 1995 issue
45 (10) 1937-1941
Paraneoplastic syndromes of the central nervous system (PNS) consist of a variety of neurologic disorders including encephalomyelitis (limbic encephalitis, brainstem encephalitis, and acute myelitis), sensory neuronopathy, subacute cerebellar degeneration, visual paraneoplastic syndrome, stiffman syndrome, and motor neuron disease. [1-3]
For the clinician, it is often difficult to arrive at a reliable diagnosis of the neurologic syndrome and to detect the underlying tumor. Neurologic signs and symptoms, although often stereotypic, are not specific. In two-thirds of cases the underlying tumor is not discovered until after the first neurologic symptoms. [4] Furthermore, the neoplasm may be small and difficult to detect. [5-7] PNS are frequently associated with serum autoantibodies reactive with neuronal antigens that are also present in the underlying tumor. These antibodies include (1) the anti-Yo antibody, also called "type 1 anti-Purkinje cell antibody" (PCA-1), "APCA-1," or "type I antibody"; (2) the anti-Hu antibody, also called "type 1 anti-neuronal nuclear antibody" (ANNA-1) or "type IIa antibody"; and (3) the anti-Ri antibody, also called "type 2 anti-neuronal nuclear antibody" (ANNA-2) or "type IIb antibody" Table 1. A clinical diagnosis of PNS is supported by the finding of these specific anti-neuronal antibodies. The detection of these antibodies should also lead to a focused search for specific underlying neoplasms. [8-12]
Table 1. Criteria for identification of paraneoplastic anti-neuronal antibodies
A major problem in comparing results obtained by different groups of investigators has been that individual laboratories have employed different laboratory techniques for detection of these antibodies. Although identification of these antibodies has rested on immunohistochemistry and Western blot analysis, not all laboratories have used Western blot analysis to identify the molecular weight of detected antigens. Furthermore, material from a number of animal species has been used, methods of preparing substrates for Western blot are not always spelled out, and concentrations of serum and end-point staining have not always been defined. In some cases, this has resulted in substantial differences in the sensitivity and specificity of these techniques for antibody detection. [12-17] Some early publications and recent reports on several incompletely characterized novel anti-neuronal antibodies have complicated this situation and make it even more difficult for the clinician to interpret the diagnostic value of these antibodies. [18-22]

Approach to consensus.

In view of these uncertainties and the existing controversy between some research groups on the techniques for proper detection and on the terminology of anti-neuronal antibodies in paraneoplastic neurologic disease, a workshop on this topic was organized during an international symposium on paraneoplastic neurologic disease held October 22-23, 1994, in Rotterdam, The Netherlands. The primary aim of the workshop was to develop a consensus report that contained generally accepted guidelines in order to make laboratory testing of anti-neuronal antibody detection more uniform and easily interpretable and to clarify the terminology.
This paper reports on the work of 11 international research groups that formed a consensus group to discuss the terminology, methodology of detection, and interpretation of paraneoplastic anti-neuronal antibodies.


Since the initial description of a paraneoplastic anti-neuronal antibody by Wilkinson and Zeromski in 1965, [23] different terminologies for paraneoplastic antibodies have been proposed by different groups working in this field.
It is important to realize that during a relatively short period of time both the designations and the methods of detection have been refined and the techniques and disclosure of antibody characteristics have improved. We first present a brief survey of the terminology.
In 1982 an anti-Purkinje cell antibody was identified by Greenlee and later by Jaeckle et al and by Greenlee and Brashear in patients with paraneoplastic cerebellar degeneration and gynecologic malignancies. [8,10,24,25] Neither group designated a specific name but both described the antibody as an anti-Purkinje cell antibody. Various names were designated later. The name "anti-Yo" was introduced in 1990 for those anti-Purkinje cell antibodies reacting with 34- and 62-kD proteins from isolated Purkinje cells on Western blot. [26] The abbreviations "PCA" and "PCAb" were used by Lennon in 1989 [12] using immunohistochemical criteria and were modified to "PCA-1" in 1994 solely on the basis of immunohistochemical criteria. [15,16] The term "APCA-1" was introduced in 1989. [27]
The original description of possible anti-neuronal nuclear antibodies mainly emphasized the cytoplasmic staining by the antibody. [23] Graus et al noted the nuclear reactivity and described reactivity with 37- to 40-kD molecular weight proteins on Western blotting. [9,28] In 1986, this antibody was designated "anti-Hu" (after the first patient in whom it was discovered). [28]
The anti-Ri antibody was first described in 1988 using both immunohistochemical and Western immunoblot characterization, [29] and its name was introduced in 1991. [11]
The term "ANNA" was introduced by Lennon in 1989 [12] and was modified to "ANNA-1" and "ANNA-2" in 1994 on the basis of immunohistochemistry alone. [15,16] Earlier others already identified differences in ANNA reactivity as "anti-Hu" and "anti-Ri" by additional testing on Western blots. [28,29]
The designations "type I" for anti-Purkinje cell antibodies and "type II" for the anti-neuronal nuclear antibodies were assigned in 1983 and in 1991 respectively, and the type II antibodies were further specified as "type IIa" and "type IIb" in 1993, based on a combination of immunohistochemistry and Western blotting. [10,25,30-32]
Although each of these teams of investigators has made valuable contributions to current understanding of this area, it is clear that unequivocal definition and terminology is necessary to enable comparison of results from different laboratories and to avoid confusion on the part of the clinician. Obviously, the main point is not so much how these antibodies are being named as how to formulate criteria for the proper methods of detection and classification of these antibodies.

Methods of detection.

The nomenclatures with numerical designations, such as ANNA-1 and -2, PCA-1, and types I, IIa, and IIb Table 1, were originally given to those antibodies determined by immunohistochemical assays only. [12,25,30-32] The terms "anti-Hu," "anti-Ri," and "anti-Yo" are based on determination by both immunohistochemistry and Western blotting. [11,26,28,33] Hence, strictly speaking, these terminologies cannot be considered interchangeable. Nevertheless, all nomenclatures are intended to refer to equivalent antibodies and should therefore preferably be regarded as synonymous, as recommended in the December 1994 issue of Neurology. [15-17,34] However, to allow them to be regarded as such, identical methods and criteria should be used, which implies redefinition of the criteria in such a way that both immunohistochemical and Western immunoblot assays are required for proper detection of all three PNS-associated anti-neuronal antibodies. The consensus group agrees that identification by immunohistochemistry alone, even when performed in experienced laboratories and according to previously issued recommendations, [15,16] cannot be considered a sufficiently reliable test for the characterization of these antibodies. If anti-Purkinje cell cytoplasmic antibodies or anti-neuronal nuclear antibodies are detected solely by immunohistochemistry, one should speak of anti-Purkinje cell antibody (APCA or PCA) or anti-neuronal nuclear antibody (ANNA) without further specification. In line with the recommendations of Neurology, we consider the anti-Yo antibody synonymous with APCA-1 or PCA-1, anti-Hu synonymous with ANNA-1, and anti-Ri synonymous with ANNA-2, provided that both immunohistochemical and Western immunoblot assays are used.
A specimen yielding no reactivity on immunohistochemistry is interpreted as negative for anti-neuronal antibodies, although Western blot analysis may detect low titers of anti-Hu antibodies in serum samples from neurologically normal patients with small-cell lung cancer using highly affinitypurified recombinant proteins.
To provide noncontroversial and accurate criteria for the definition of these antibodies, we outline here some general guidelines on the appropriate methods as well as some technical details. We expect that following these guidelines will make identification of novel antibodies more easily comparable and interpretable.


The first screening for anti-neuronal antibodies in serum or CSF consists of an immunohistochemical assay. Immunohistochemical screening can also detect other atypical (non-anti-Yo, non-anti-Hu, and non-anti-Ri) antineuronal antibodies. Patients' serum samples should be sent overnight and tested within 48 hours or can be stored at 4 degrees C for several weeks. For longer delays, samples should preferably be stored at minus 80 degrees C until tested.
Human cerebellar and cerebral cortex are preferentially used as tissue substrates for immunohistochemistry. Occasionally, dorsal root ganglia, myenteric plexus, medulla, spinal cord, and control tissues such as liver, muscle, and kidney can be used for special interests, although on indirect immunohistochemistry some background staining may be found because of the presence of irrelevant IgG in systemic tissues. If obtaining human tissue is difficult, mouse or rat tissue can be used for avidin-biotin or peroxidase-antiperoxidase methods since these species express most human PNS antigens. However, misleading results may be obtained when fluorescence staining is used in nonhuman tissue. [35] For novel antibody screening, one should always employ human tissue, and it may well prove valuable to use nonhuman tissue as well.
Criteria for positive immunohistochemical identification of antibodies are presented in the Table 1.
It is possible to discriminate immunohistochemically between anti-Hu and anti-Ri by using peripheral neurons--for example, myenteric plexus or dorsal root ganglion cells--as substrate. [15,36] In contrast to the Hu antigen, the Ri antigen is not expressed in peripheral neurons.
Antibody titers should be determined by serial dilutional titration. In each series of tests, parallel control sections should include a section without use of primary serum, a section using a known positive serum, and a section with a known negative serum. The secondary antibody can be labeled with either fluorescein isothiocyanate (FITC), horseradish peroxidase, alkaline phosphatase, biotin, or other enzymes to visualize bound antibodies. Either polyclonal or monoclonal secondary antibodies against total human Ig or IgG may be chosen. Titers of antibodies depend on many factors, among which are the purity of the antigen, concentration of the secondary antibody, time of incubation, quality of tissues, and type of secondary antibody. Dilution and diluent of the secondary antibody are of great importance in this respect. The secondary antibody should be diluted in the same medium used as blocking agent. Initial assays from the early groups used the FITC-labeled secondary antibody, [8-10,37] which is easy to work with and reliable. Other frequently used techniques are avidin-biotin-peroxidase and streptavidin-peroxidase methods. [38] Different labeling techniques will often lead to differences in end-point staining. In general, immunoperoxidase and avidin-biotin methods give higher end-point titers than does indirect immunofluorescence. Therefore, each laboratory should critically establish dilution and method of visualization of secondary antibody, using appropriate positive and negative controls.
Ideally, a set of positive reference control serum samples is assembled by exchange of various serum samples between experienced laboratories.
End-point staining titers for positive identification of antibody should be determined using large series of controls and positive standards to prevent false-positive detection. In most immunohistochemical assays using FITC-labeled secondary antibody, end-point titers of more than 1:500 can be regarded as positive, yielding high specificities. In some patients, however, lower titers can represent true-positive reactivity. [14]
With high serum IgG concentrations, background staining can occasionally make the assay difficult to interpret. Isolation and direct labeling of serum IgG may eliminate background reactivity and may improve the quality of the assay. [38]

Western immunoblot methods.

Essential and optional criteria for positive identification on Western immunoblot are provided in the Table 1.
With the availability of recombinant antigens (HuD, Hel-N1/ple21, HuC, Ri [Nova], CDR34, CDR62, p52/PCD17, and CZF) it may be useful, although not obligatory, to use these complementary to neuronal extracts. [39-45] One should realize, especially in the United States, that the commercial diagnostic use of the recombinant proteins HuD, Yo (CDR62), and Ri (Nova) is licensed by Genica (Boston, MA).
When using neuronal proteins as antigenic substrate, an important factor for the diagnostic reliability of this technique is the nature and concentration of the protein extracts. Collected tissues should be processed as rapidly as possible (preferably within 6 to 8 hours, maximally 24 hours) after death.
For anti-Hu detection on Western blots, a protein extract from isolated neurons or neuronal nuclei from normal human, rat, or murine cerebral or cerebellar cortex is used. [38] If available, the recombinant HuD protein can also be used. For recognition of anti-Yo and other anti-Purkinje cell antibodies on Western blots, a protein extract of isolated human or murine Purkinje cells, separated on a sucrose/Ficoll gradient, is used. Optionally, the Yo recombinant protein (CDR62) or the p52 recombinant protein of Sakai et al can be used next to the Purkinje cell proteins. [39,41]
For identification of anti-Ri antibodies, the same guidelines as used for anti-Hu antibodies are applicable. For the reliable detection of anti-Ri antibodies, Western blotting on neuronal proteins is required. The Ri recombinant protein may also be used for proper recognition of anti-Ri antibodies. However, immunohistochemistry and Western blot on neuronal proteins are sufficiently reliable for demonstrating the anti-Ri antibody.
As a control antigenic substrate, protein extracts from human and murine liver, kidney, or muscle can be used.

Diagnostic value.

Although no large clinicopathologic studies are available to accurately establish sensitivity and specificity of these assays for detection of PNS-associated anti-neuronal antibodies, it is clear that the presence of these antibodies has high diagnostic value. [4,11,14,25] However, in a minority of patients with characteristic PNS and high antibody titers no tumor could be found despite extensive evaluation. [5,46] One presumes that in these cases the tumor either is too small to be detected or may have spontaneously regressed. [4,5] On the other hand, failure to detect anti-Yo, anti-Hu, or anti-Ri antibodies in patients with suspected paraneoplastic syndromes does not exclude a paraneoplastic neurologic disease, as it does not exclude an underlying malignancy.
If, following the guidelines above, anti-Yo (APCA-1), anti-Hu (ANNA-1), or anti-Ri (ANNA-2) antibody is identified, a sufficiently reliable diagnosis of PNS can be made despite a lack of proof of the presence of cancer.
Finally, some cases with a clear clinical diagnosis of PNS are antibody-negative in the presence of cancer. Whether these patients harbor paraneoplastic antibodies that cannot be detected with currently available methods remains unclear.


We appreciate the comments made by Dr. Josep Dalmau and Dr. Jerome B. Posner. We thank Janet van Vliet for help in preparing the manuscript and in organizing the workshop.


Henson RA, Urich H. Cancer and the nervous system: the neurological manifestations of systemic disease. Oxford, UK: Blackwell, 1982.
Posner JB. Paraneoplastic syndromes. Curr Neurol 1989;9:245-278.
Vecht ChJ. Paraneoplastic syndromes. In: Twijnstra A, Keyser A, Ongerboer de Visser BW, eds. Neuro-oncology. Primary tumors and neurological complications of cancer. Amsterdam: Elsevier, 1993:385-418.
Dalmau J, Graus F, Rosenblum MK, Posner JB. Anti-Hu-associated paraneoplastic encephalomyelitis/sensory neuronopathy. A clinical study of 71 patients. Medicine 1992;71:59-72.
Darnell RB, DeAngelis LM. Regression of small-cell lung carcinoma in patients with paraneoplastic neuronal antibodies. Lancet 1993;341:21-22.
Dalmau J, Graus F, Cheung N-KV, et al. Major histocompatibility proteins, anti-Hu antibodies, and paraneoplastic encephalomyelitis in neuroblastoma and small cell lung cancer. Cancer 1995;75:99-109.
Dalmau J, Furneaux HM, Gralla RJ, Kris MG, Posner JB. Detection of the anti-Hu antibody in serum of patients with small cell lung cancer. A quantitative Western blot analysis. Ann Neurol 1990;27:544-552.
Greenlee JE, Brashear HR. Antibodies to cerebellar Purkinje cells in patients with paraneoplastic cerebellar degeneration and ovarian carcinoma. Ann Neurol 1983;14:609-613.
Graus F, Cordon-Cardo C, Posner JB. Neuronal antinuclear antibody in sensory neuronopathy from lung cancer. Neurology 1985;35:538-543.
Jaeckle KA, Houghton AN, Nielsen SL, Posner JB. Demonstration of serum anti-Purkinje antibody in paraneoplastic cerebellar degeneration and preliminary antigenic characterization [abstract]. Ann Neurol 1983;14:111.
Luque FA, Furneaux HM, Ferziger R, et al. Anti-Ri: an antibody associated with paraneoplastic opsoclonus and breast cancer. Ann Neurol 1991;29:241-251.
Lennon VA. Anti-Purkinje cell cytoplasmic and neuronal nuclear antibodies aid diagnosis of paraneoplastic autoimmune neurological disorders. J Neurol Neurosurg Psychiatry 1989;42:1438-1439.
Grisold W, Drlicek M, Popp W, Jellinger K. Antineuronal antibodies in small cell lung carcinoma--a significance for paraneoplastic syndromes? Acta Neuropathol (Berl) 1987;75:199-202.
Moll JWB, Henzen-Logmans SC, Splinter TAW, Van der Burg MEL, Vecht CJ. Diagnostic value of anti-neuronal antibodies for paraneoplastic disorders of the nervous system. J Neurol Neurosurg Psychiatry 1990;53:940-943.
Lennon VA. Paraneoplastic autoantibodies: the case for a descriptive generic nomenclature. Neurology 1994;44:2236-2240.
Lennon VA. The case for a descriptive generic nomenclature: clarification of immunostaining criteria for PCA-1, ANNA-1, and ANNA-2 autoantibodies. Neurology 1994;44:2412-2415.
Dalmau J, Posner JB. Neurologic paraneoplastic antibodies (anti-Yo; anti-Hu; anti-Ri): the case for a nomenclature based on antibody and antigen specificity. Neurology 1994;44:2241-2246.
Darnell RB, Furneaux HM, Posner JB. Antiserum from a patient with cerebellar degeneration identifies a novel protein in Purkinje cells, cortical neurons and neuroectodermal tumors. J Neurosci 1991;11:1224-1230.
Plioplys AV, Thibault J, Bouchard JP, Cockburn C, Hawkes R. Anti-CNS antibodies in neurological and psychiatric disorders. J Neurol Neurosurg Psychiatry 1987;50:1514-1521.
Wong MCW, Salanga VD, Chou S, Mitsumoto H, Kozachuk W, Liwnicz B. Immune-associated paraneoplastic motor neuron disease and limbic encephalopathy. Muscle Nerve 1987;10:661-662.
Trotter JL, Hendin BA, Osterland K. Cerebellar degeneration with Hodgkin disease. Arch Neurol 1976;33:660-661.
Stefansson K, Antel JP, Wollman RL, Levin KH, Larson R, Arnason BGW. Anti-neuronal antibodies in serum of a patient with Hodgkin disease and cerebellar ataxia [abstract]. Neurology 1981;31(suppl):126.
Wilkinson PC, Zeromski J. Immunofluorescent detection of antibodies against neurons in sensory carcinomatous neuropathy. Brain 1965;88:529-538.
Greenlee JE. Is paraneoplastic cerebellar degeneration an immune-mediated condition? [abstract]. Ann Neurol 1982;12:102.
Jaeckle KA, Graus F, Houghton A, Cardon-Cardo C, Nielsen SL, Posner JB. Autoimmune response of patients with paraneoplastic cerebellar degeneration to a Purkinje cell cytoplasmic protein antigen. Ann Neurol 1985;18:592-600.
Furneaux HM, Rosenblum MK, Dalmau J, et al. Selective expression of Purkinje-cell antigens in tumor tissue from patients with paraneoplastic cerebellar degeneration. N Engl J Med 1990;322:1844-1851.
Brashear HR, Greenlee JE, Jaeckle KA, Rose JW. Anticerebellar antibodies in neurologically normal patients with ovarian neoplasms. Neurology 1989;39:1605-1609.
Graus F, Elkon KB, Cordon-Cardo C, Posner JB. Sensory neuronopathy and small cell lung cancer. Antineuronal antibody that also reacts with the tumor. Am J Med 1986;80:45-52.
Budde-Steffen C, Anderson NE, Rosenblum MK, et al. An antineuronal autoantibody in paraneoplastic opsoclonus. Ann Neurol 1988;23:528-531.
Brashear HR, Hill B, Keeney P. Occurrence of antineuronal antibody in patients with breast cancer [abstract]. Neurology 1994;44(suppl 2):A156.
Greenlee JE, Parks TN, Jaeckle KA. Type IIa (`anti-Hu') antineuronal antibodies produce destruction of rat cerebellar granule neurons in vitro. Neurology 1993;43:2049-2054.
Greenlee JE, Jaeckle KA, Brashear HR. Type II ("Anti-Hu") antibody in suspected paraneoplastic syndromes: association with conditions other than small cell lung cancer and initial detection of antibody at very low titer [abstract]. Ann Neurol 1991;30:308.
Graus F, Elkon KB, Lloberes P, et al. Neuronal antinuclear antibody (anti-Hu) in paraneoplastic encephalomyelitis simulating acute polyneuritis. Acta Neurol Scand 1987;75:249-252.
Daroff RB. Message from the Editor-in-Chief. Neurology 1994;44(Dec):15A.
Greenlee JE, Sun M. Immunofluorescent labeling of nonhuman cerebellar tissue with sera from patients with systemic cancer and paraneoplastic cerebellar degeneration. Acta Neuropathol (Berl) 1985;67:226-229.
Graus F, Rowe G, Fueyo J, Darnell RB, Dalmau J. The neuronal nuclear antigen recognized by the human anti-Ri autoantibody is expressed in central but not peripheral nervous system neurons. Neurosci Lett 1993;150:212-214.
Steven MM, Mackay IR, Carnegie PR, Bhathal PS, Anderson RMcD. Cerebellar cortical degeneration with ovarian carcinoma. Postgrad Med J 1982;58:47-51.
Dalmau J, Rosenfeld MR. Characterization of neuronal antigens and anti-neuronal antibodies. Methods Neurosci 1995;24:261-271.
Sakai K, Mitchell DJ, Tsukamoto T, Steinman L. Isolation of a complementary DNA clone encoding an autoantigen recognized by an anti-neuronal cell antibody from a patient with paraneoplastic cerebellar degeneration. Ann Neurol 1990;28:692-698.
Szabo A, Dalmau J, Manley G, et al. HuD, a paraneoplastic encephalomyelitis antigen, contains RNA-binding domains and is homologous to Elav and Sex-lethal. Cell 1991;67:325-333.
Fathalla-Shaykth H, Wolf S, Wong E, Posner JB, Furneaux HM. Cloning of leucine-zipper protein recognized by the sera of patients with antibody-associated paraneoplastic cerebellar degeneration. Proc Natl Acad Sci USA 1991;88:4351-4354.
Dropcho EJ, Chen YT, Posner JB, Old LJ. Cloning of a brain protein identified by autoantibodies from a patient with paraneoplastic cerebellar degeneration. Proc Natl Acad Sci USA 1987;84:4552-4556.
Buckanovich RJ, Posner JB, Darnell RB. Nova, the paraneoplastic Ri antigen, is homologous to an RNA-binding protein and is specifically expressed in the developing motor system. Neuron 1993;11:647-672.
Levine TD, Gao F, King PH, Andrews LG, Keene JD. Hel-N1: an autoimmune RNA-binding protein with specificity for 3 prime uridylate-rich untranslated regions of growth factor mRNAs. Mol Cell Biol 1993;13:3494-3504.
Sato S, Inuzuka T, Nakano R, et al. Antibody to a zinc finger protein in a patient with paraneoplastic cerebellar degeneration. Biochem Biophys Res Commun 1991;178:198-206.
Peterson K, Rosenblum MK, Kotanides H, Posner JB. Paraneoplastic cerebellar degeneration. I. A clinical analysis of 55 anti-Yo antibody-positive patients. Neurology 1992;42:1931-1937.

Information & Authors


Published In

Volume 45Number 10October 1995
Pages: 1937-1941
PubMed: 7478000

Publication History

Published online: October 1, 1995
Published in print: October 1995


Request permissions for this article.


Affiliations & Disclosures

From the Department of Neuro-oncology (Drs. Moll and Vecht), Dr. Daniel den Hoed Cancer Center, and the Departments of Neurology (Dr. Moll) and Immunology (Dr. Moll), Erasmus University and University Hospital Rotterdam (Dr. Moll), The Netherlands; Service de Neurologie (Dr. Antoine), Hopital de Bellevue, Saint-Etienne, France; the Department of Neurology (Dr. Brashear), University of Virginia, Charlottesville, VA; Clinique Neurologique (Dr. Delattre), Hopital de la Salpetriere, Paris, France; Neurologische Abteilung (Dr. Drlicek), Kaiser Franz Josef Spital, Vienna, Austria; the Department of Neurology (Dr. Dropcho), Indiana University School of Medicine, Indianapolis, IN; the Department of Neurology (Second Clinic) (Dr. Giometto), University of Padua, Italy; the Department of Neurology (Dr. Graus), Hopital Clinic i Provincial, Barcelona, Spain; the Neurology Service (Dr. Greenlee), VA Medical Center, Salt Lake City, UT; Laboratoire de Neuropathologie (Dr. Honnorat), Hopital de Neurologique, Lyon, France; the Department of Neuro-Oncology (Dr. Jaeckle), M.D. Anderson Cancer Center, Houston, TX; and the Department of Neurology (Dr. Tanaka), Brain Research Institute, Niigata University, Niigata, Japan.
Received January 9, 1995. Accepted in final form June 14, 1995.
Address correspondence and reprint requests to DrB. Moll, Department of Neuro-oncology, Dr. Daniel den Hoed Cancer Center, P.O. Box 5201, 3008 AE Rotterdam, The Netherlands.

Metrics & Citations



Download Citations

If you have the appropriate software installed, you can download article citation data to the citation manager of your choice. Select your manager software from the list below and click Download.

Cited By
  1. Evolution of methods to detect paraneoplastic antibodies, Paraneoplastic Neurologic Disorders, (113-130), (2024).
  2. The Neuropathology of Autoimmune Ataxias, Brain Sciences, 12, 2, (257), (2022).
  3. Subacute sensory neuronopathy associated with Merkel cell carcinoma with unknown primary: a case report with literature review, Journal of Neurology, 269, 8, (4080-4088), (2022).
  4. Bacterial production and purification of immunoreactive paraneoplastic neurological syndrome autoantigen Ma2, Journal of Cellular Biotechnology, 2, 2, (85-91), (2017).
  5. Immunological Features of Paraneoplastic Neurological Syndromes, International Journal of Immunopathology and Pharmacology, 17, 2, (135-144), (2017).
  6. Diagnostics of paraneoplastic neurological syndromes, Neurological Sciences, 38, S2, (237-242), (2017).
  7. Anti-Yo Antibody Uptake and Interaction with Its Intracellular Target Antigen Causes Purkinje Cell Death in Rat Cerebellar Slice Cultures: A Possible Mechanism for Paraneoplastic Cerebellar Degeneration in Humans with Gynecological or Breast Cancers, PLOS ONE, 10, 4, (e0123446), (2015).
  8. The Prevalence of Autoantibodies in Complex Regional Pain Syndrome Type I, Mediators of Inflammation, 2015, (1-5), (2015).
  9. Pathogenesis and treatment of paraneoplastic neurologic syndrome, Expert Review of Neurotherapeutics, 2, 6, (901-909), (2014).
  10. Neuronal uptake of anti-Hu antibody, but not anti-Ri antibody, leads to cell death in brain slice cultures, Journal of Neuroinflammation, 11, 1, (2014).
  11. See more

View Options

View options

Full Text

View Full Text

Get Access

Login options

Check if you have access through your login credentials or your institution to get full access on this article.

Personal login Institutional Login
Purchase Options

The payment platform is currently offline. Our technical team is working as quickly as possible to restore service.

If you need immediate support or to place an order, please call or email customer service:

  • 1-800-638-3030 for U.S. customers - 8:30 - 7 pm ET (M-F)
  • 1-301-223-2300 for customers outside the U.S. - 8:30 - 7 pm ET (M-F)
  • [email protected]

We appreciate your patience during this time and apologize for any inconvenience.







Share article link